Increasing cancer permeability by photodynamic priming: from microenvironment to mechanotransduction signaling

1.

Valkenburg, K. C., de Groot, A. E., & Pienta, K. J. (2018). Targeting the tumour stroma to improve cancer therapy. Nature Reviews. Clinical Oncology, 15(6), 366–381. https://doi.org/10.1038/s41571-018-0007-1CrossRef

2.

Hosein, A. N., Brekken, R. A., & Maitra, A. (2020). Pancreatic cancer stroma: An update on therapeutic targeting strategies. Nature Reviews. Gastroenterology & Hepatology, 17(8), 487–505. https://doi.org/10.1038/s41575-020-0300-1CrossRef

3.

Adiseshaiah, P. P., Crist, R. M., Hook, S. S., & McNeil, S. E. (2016). Nanomedicine strategies to overcome the pathophysiological barriers of pancreatic cancer. Nature Reviews Clinical Oncology, 13(12), 750–765. https://doi.org/10.1038/nrclinonc.2016.119CrossRef

4.

Maeda, H. (2015). Toward a full understanding of the EPR effect in primary and metastatic tumors as well as issues related to its heterogeneity. Advanced Drug Delivery Reviews, 91, 3–6. https://doi.org/10.1016/j.addr.2015.01.002CrossRef

5.

Olive, K. P., Jacobetz, M. A., Davidson, C. J., Gopinathan, A., McIntyre, D., Honess, D., & Tuveson, D. A. (2009). Inhibition of Hedgehog signaling enhances delivery of chemotherapy in a mouse model of pancreatic cancer. Science (New York, N.Y.), 324(5933), 1457–1461. https://doi.org/10.1126/science.1171362CrossRef

6.

Catenacci, D. V. T., Junttila, M. R., Karrison, T., Bahary, N., Horiba, M. N., Nattam, S. R., & Kindler, H. L. (2015). Randomized phase Ib/II study of gemcitabine plus placebo or vismodegib, a hedgehog pathway inhibitor, in patients with metastatic pancreatic cancer. Journal of Clinical Oncology: Official Journal of the American Society of Clinical Oncology, 33(36), 4284–4292. https://doi.org/10.1200/JCO.2015.62.8719CrossRef

7.

De Jesus-Acosta, A., Sugar, E. A., O’Dwyer, P. J., Ramanathan, R. K., Von Hoff, D. D., Rasheed, Z., & Laheru, D. A. (2020). Phase 2 study of vismodegib, a hedgehog inhibitor, combined with gemcitabine and nab-paclitaxel in patients with untreated metastatic pancreatic adenocarcinoma. British Journal of Cancer, 122(4), 498–505. https://doi.org/10.1038/s41416-019-0683-3CrossRef

8.

Kim, E. J., Sahai, V., Abel, E. V., Griffith, K. A., Greenson, J. K., Takebe, N., & Simeone, D. M. (2014). Pilot clinical trial of hedgehog pathway inhibitor GDC-0449 (vismodegib) in combination with gemcitabine in patients with metastatic pancreatic adenocarcinoma. Clinical Cancer Research: An Official Journal of the American Association for Cancer Research, 20(23), 5937–5945. https://doi.org/10.1158/1078-0432.CCR-14-1269CrossRef

9.

Lee, J. J., Perera, R. M., Wang, H., Wu, D.-C., Liu, X. S., Han, S., & Beachy, P. A. (2014). Stromal response to Hedgehog signaling restrains pancreatic cancer progression. Proceedings of the National Academy of Sciences of the United States of America, 111(30), E3091-3100. https://doi.org/10.1073/pnas.1411679111CrossRef

10.

Hingorani, S. R., Zheng, L., Bullock, A. J., Seery, T. E., Harris, W. P., Sigal, D. S., & Hendifar, A. E. (2018). HALO 202: Randomized phase II study of PEGPH20 plus nab-paclitaxel/gemcitabine versus nab-paclitaxel/gemcitabine in patients with untreated, metastatic pancreatic ductal adenocarcinoma. Journal of Clinical Oncology: Official Journal of the American Society of Clinical Oncology, 36(4), 359–366. https://doi.org/10.1200/JCO.2017.74.9564CrossRef

11.

Van Cutsem, E., Tempero, M. A., Sigal, D., Oh, D.-Y., Fazio, N., Macarulla, T., HALO 109-301 Investigators. (2020). Randomized phase III trial of pegvorhyaluronidase alfa with nab-paclitaxel plus gemcitabine for patients with hyaluronan-high metastatic pancreatic adenocarcinoma. Journal of Clinical Oncology: Official Journal of the American Society of Clinical Oncology, 38(27), 3185–3194. https://doi.org/10.1200/JCO.20.00590CrossRef

12.

Ramanathan, R. K., McDonough, S. L., Philip, P. A., Hingorani, S. R., Lacy, J., Kortmansky, J. S., & Hochster, H. S. (2019). Phase IB/II randomized study of FOLFIRINOX plus pegylated recombinant human hyaluronidase versus FOLFIRINOX alone in patients with metastatic pancreatic adenocarcinoma: SWOG S1313. Journal of Clinical Oncology: Official Journal of the American Society of Clinical Oncology, 37(13), 1062–1069. https://doi.org/10.1200/JCO.18.01295CrossRef

13.

Castano, A. P., Mroz, P., & Hamblin, M. R. (2006). Photodynamic therapy and anti-tumour immunity. Nature Reviews Cancer, 6(7), 535–545. https://doi.org/10.1038/nrc1894CrossRef

14.

Dolmans, D. E. J. G. J., Fukumura, D., & Jain, R. K. (2003). Photodynamic therapy for cancer. Nature Reviews. Cancer, 3(5), 380–387. https://doi.org/10.1038/nrc1071CrossRef

15.

Celli, J. P., Spring, B. Q., Rizvi, I., Evans, C. L., Samkoe, K. S., Verma, S., & Hasan, T. (2010). Imaging and photodynamic therapy: Mechanisms, monitoring, and optimization. Chemical Reviews, 110(5), 2795–2838. https://doi.org/10.1021/cr900300pCrossRef

16.

Araki, T., Ogawara, K., Suzuki, H., Kawai, R., Watanabe, T., Ono, T., & Higaki, K. (2015). Augmented EPR effect by photo-triggered tumor vascular treatment improved therapeutic efficacy of liposomal paclitaxel in mice bearing tumors with low permeable vasculature. Journal of Controlled Release: Official Journal of the Controlled Release Society, 200, 106–114. https://doi.org/10.1016/j.jconrel.2014.12.038CrossRef

17.

Luo, D., Carter, K. A., Razi, A., Geng, J., Shao, S., Giraldo, D., & Lovell, J. F. (2016). Doxorubicin encapsulated in stealth liposomes conferred with light-triggered drug release. Biomaterials, 75, 193–202. https://doi.org/10.1016/j.biomaterials.2015.10.027CrossRef

18.

Luo, D., Carter, K. A., Molins, E. A. G., Straubinger, N. L., Geng, J., Shao, S., & Lovell, J. F. (2019). Pharmacokinetics and pharmacodynamics of liposomal chemophototherapy with short drug-light intervals. Journal of Controlled Release: Official Journal of the Controlled Release Society, 297, 39–47. https://doi.org/10.1016/j.jconrel.2019.01.030CrossRef

19.

Huang, H.-C., Rizvi, I., Liu, J., Anbil, S., Kalra, A., Lee, H., & Hasan, T. (2018). Photodynamic priming mitigates chemotherapeutic selection pressures and improves drug delivery. Cancer Research, 78(2), 558–571. https://doi.org/10.1158/0008-5472.CAN-17-1700CrossRef

20.

Luo, D., Carter, K. A., Geng, J., He, X., & Lovell, J. F. (2018). Short drug-light intervals improve liposomal chemophototherapy in mice bearing MIA PaCa-2 xenografts. Molecular Pharmaceutics, 15(9), 3682–3689. https://doi.org/10.1021/acs.molpharmaceut.8b00052CrossRef

21.

Sorrin, A. J., Kemal Ruhi, M., Ferlic, N. A., Karimnia, V., Polacheck, W. J., Celli, J. P., & Rizvi, I. (2020). Photodynamic therapy and the biophysics of the tumor microenvironment. Photochemistry and Photobiology, 96(2), 232–259. https://doi.org/10.1111/php.13209CrossRef

22.

Obaid, G., Bano, S., Mallidi, S., Broekgaarden, M., Kuriakose, J., Silber, Z., & Hasan, T. (2019). Impacting pancreatic cancer therapy in heterotypic in vitro organoids and in vivo tumors with specificity-tuned, NIR-activable photoimmunonanoconjugates: Towards conquering desmoplasia? Nano letters, 19(11), 7573–7587. https://doi.org/10.1021/acs.nanolett.9b00859CrossRef

23.

Düzgüneş, N., Piskorz, J., Skupin-Mrugalska, P., Goslinski, T., Mielcarek, J., & Konopka, K. (2018). Photodynamic therapy of cancer with liposomal photosensitizers. Therapeutic Delivery, 9(11), 823–832. https://doi.org/10.4155/tde-2018-0050CrossRef

24.

Broekgaarden, M., Weijer, R., van Gulik, T. M., Hamblin, M. R., & Heger, M. (2015). Tumor cell survival pathways activated by photodynamic therapy: A molecular basis for pharmacological inhibition strategies. Cancer Metastasis Reviews, 34(4), 643–690. https://doi.org/10.1007/s10555-015-9588-7CrossRef

25.

Kushibiki, T., Hirasawa, T., Okawa, S., & Ishihara, M. (2013). Responses of cancer cells induced by photodynamic therapy. Journal of Healthcare Engineering, 4(1), 87–108. https://doi.org/10.1260/2040-2295.4.1.87CrossRef

26.

Li, X., Lovell, J. F., Yoon, J., & Chen, X. (2020). Clinical development and potential of photothermal and photodynamic therapies for cancer. Nature Reviews. Clinical Oncology, 17(11), 657–674. https://doi.org/10.1038/s41571-020-0410-2CrossRef

27.

Willenbrink, T. J., Ruiz, E. S., Cornejo, C. M., Schmults, C. D., Arron, S. T., & Jambusaria-Pahlajani, A. (2020). Field cancerization: Definition, epidemiology, risk factors, and outcomes. Journal of the American Academy of Dermatology, 83(3), 709–717. https://doi.org/10.1016/j.jaad.2020.03.126CrossRef

28.

Jansen, M. H. E., Kessels, J. P. H. M., Nelemans, P. J., Kouloubis, N., Arits, A. H. M. M., van Pelt, H. P. A., & Mosterd, K. (2019). Randomized trial of four treatment approaches for actinic keratosis. The New England Journal of Medicine, 380(10), 935–946. https://doi.org/10.1056/NEJMoa1811850CrossRef

29.

Wollina, U., Gaber, B., & Koch, A. (2018). Photodynamic treatment with nanoemulsified 5-aminolevulinic acid and narrow band red light for field cancerization due to occupational exposure to ultraviolet light irradiation. Georgian Medical News, 274, 138–143.

30.

Haque, T., Rahman, K. M., Thurston, D. E., Hadgraft, J., & Lane, M. E. (2015). Topical therapies for skin cancer and actinic keratosis. European Journal of Pharmaceutical Sciences: Official Journal of the European Federation for Pharmaceutical Sciences, 77, 279–289. https://doi.org/10.1016/j.ejps.2015.06.013CrossRef

31.

Stewart, T. J., Farrell, J., Crainic, O., & Rosen, R. H. (2020). A large series of pigmented Bowen’s disease. International Journal of Dermatology, 59(9), e316–e317. https://doi.org/10.1111/ijd.14977CrossRef

32.

de Faria, C. M. G., Barrera-Patiño, C. P., Santana, J. P. P., da Silva de Avó, L. R., & Bagnato, V. S. (2021). Tumor radiosensitization by photobiomodulation. Journal of Photochemistry and Photobiology. B, Biology, 225, 112349. https://doi.org/10.1016/j.jphotobiol.2021.112349CrossRef

33.

Finlayson, L., Barnard, I. R. M., McMillan, L., Ibbotson, S. H., Brown, C. T. A., Eadie, E., & Wood, K. (2022). Depth penetration of light into skin as a function of wavelength from 200 to 1000 nm. Photochemistry and Photobiology, 98(4), 974–981. https://doi.org/10.1111/php.13550CrossRef

34.

Samarasinghe, V., & Madan, V. (2012). Nonmelanoma skin cancer. Journal of Cutaneous and Aesthetic Surgery, 5(1), 3–10. https://doi.org/10.4103/0974-2077.94323CrossRef

35.

Miller, M. B., & Padilla, A. (2020). CO2 laser ablative fractional resurfacing photodynamic therapy for actinic keratosis and nonmelanoma skin cancer: A randomized split-side study. Cutis, 105(5), 251–254.

36.

Kim, H.-J., & Song, K.-H. (2018). Ablative fractional laser-assisted photodynamic therapy provides superior long-term efficacy compared with standard methyl aminolevulinate photodynamic therapy for lower extremity Bowen disease. Journal of the American Academy of Dermatology, 79(5), 860–868. https://doi.org/10.1016/j.jaad.2018.05.034CrossRef

37.

Vrani, F., Sotiriou, E., Lazaridou, E., Vakirlis, E., Sideris, N., Kirmanidou, E., & Ioannides, D. (2019). Short incubation fractional CO2 laser-assisted photodynamic therapy vs. conventional photodynamic therapy in field-cancerized skin: 12-month follow-up results of a randomized intraindividual comparison study. Journal of the European Academy of Dermatology and Venereology: JEADV, 33(1), 79–83. https://doi.org/10.1111/jdv.15109CrossRef

38.

Genouw, E., Verheire, B., Ongenae, K., De Schepper, S., Creytens, D., Verhaeghe, E., & Boone, B. (2018). Laser-assisted photodynamic therapy for superficial basal cell carcinoma and Bowen’s disease: A randomized intrapatient comparison between a continuous and a fractional ablative CO2 laser mode. Journal of the European Academy of Dermatology and Venereology: JEADV, 32(11), 1897–1905. https://doi.org/10.1111/jdv.14989CrossRef

39.

Pires, M. T. F., Pereira, A. D., Durães, S. M. B., Issa, M. C. A., & Pires, M. (2019). Laser-assisted MAL-PDT associated with acoustic pressure wave ultrasound with short incubation time for field cancerization treatment: A left-right comparison. Photodiagnosis and Photodynamic Therapy, 28, 216–220. https://doi.org/10.1016/j.pdpdt.2019.08.034CrossRef

40.

Rizzo, J. M., Segal, R. J., & Zeitouni, N. C. (2018). Combination vismodegib and photodynamic therapy for multiple basal cell carcinomas. Photodiagnosis and Photodynamic Therapy, 21, 58–62. https://doi.org/10.1016/j.pdpdt.2017.10.028CrossRef

41.

Morita, A., Tateishi, C., Muramatsu, S., Kubo, R., Yonezawa, E., Kato, H., & Tsuruta, D. (2020). Efficacy and safety of bexarotene combined with photo(chemo)therapy for cutaneous T-cell lymphoma. The Journal of Dermatology, 47(5), 443–451. https://doi.org/10.1111/1346-8138.15310CrossRef

42.

Wu, Y., Wang, P., Zhang, L., Wang, B., & Wang, X. (2018). Enhancement of photodynamic therapy for Bowen’s disease using plum-blossom needling to augment drug delivery. Dermatologic Surgery: Official Publication for American Society for Dermatologic Surgery [et Al.], 44(12), 1516–1524. https://doi.org/10.1097/DSS.0000000000001608CrossRef

43.

Navarro-Triviño, F. J., Ayén-Rodríguez, Á., Llamas-Molina, J. M., Saenz-Guirado, S., & Ruiz-Villaverde, R. (2021). Treatment of superficial basal cell carcinoma with 7.8% 5-aminolaevulinic acid nanoemulsion-based gel (BF-200 ALA) and photodynamic therapy: Results in clinical practice in a tertiary hospital. Dermatologic Therapy, 34(1), e14558. https://doi.org/10.1111/dth.14558CrossRef

44.

Bu, W., Zhang, M., Zhang, Q., Yuan, C., Chen, X., & Fang, F. (2017). Preliminary results of comparative study for subsequent photodynamic therapy versus secondary excision after primary excision for treating basal cell carcinoma. Photodiagnosis and Photodynamic Therapy, 17, 134–137. https://doi.org/10.1016/j.pdpdt.2016.11.003CrossRef

45.

Ikeda, H., Tobita, T., Ohba, S., Uehara, M., & Asahina, I. (2013). Treatment outcome of Photofrin-based photodynamic therapy for T1 and T2 oral squamous cell carcinoma and dysplasia. Photodiagnosis and Photodynamic Therapy, 10(3), 229–235. https://doi.org/10.1016/j.pdpdt.2013.01.006CrossRef

46.

Siddiqui, S. A., Siddiqui, S., Hussain, M. A. B., Khan, S., Liu, H., Akhtar, K., & Hasan, T. (2022). Clinical evaluation of a mobile, low-cost system for fluorescence guided photodynamic therapy of early oral cancer in India. Photodiagnosis and Photodynamic Therapy, 38, 102843. https://doi.org/10.1016/j.pdpdt.2022.102843CrossRef

47.

Yano, T., Kasai, H., Horimatsu, T., Yoshimura, K., Teramukai, S., Morita, S., & Muto, M. (2017). A multicenter phase II study of salvage photodynamic therapy using talaporfin sodium (ME2906) and a diode laser (PNL6405EPG) for local failure after chemoradiotherapy or radiotherapy for esophageal cancer. Oncotarget, 8(13), 22135–22144. https://doi.org/10.18632/oncotarget.14029CrossRef

48.

Kohoutova, D., Haidry, R., Banks, M., Butt, M. A., Dunn, J., Thorpe, S., & Lovat, L. (2018). Long-term outcomes of the randomized controlled trial comparing 5-aminolaevulinic acid and Photofrin photodynamic therapy for Barrett’s oesophagus related neoplasia. Scandinavian Journal of Gastroenterology, 53(5), 527–532. https://doi.org/10.1080/00365521.2017.1403646CrossRef

49.

Usuda, J., Inoue, T., Tsuchida, T., Ohtani, K., Maehara, S., Ikeda, N., & Oka, K. (2020). Clinical trial of photodynamic therapy for peripheral-type lung cancers using a new laser device in a pilot study. Photodiagnosis and Photodynamic Therapy, 30, 101698. https://doi.org/10.1016/j.pdpdt.2020.101698CrossRef

50.

Herbst, R. S., Morgensztern, D., & Boshoff, C. (2018). The biology and management of non-small cell lung cancer. Nature, 553(7689), 446–454. https://doi.org/10.1038/nature25183CrossRef

51.

Kelley, K. D., Benninghoff, D. L., Stein, J. S., Li, J. Z., Byrnes, R. T., Potters, L., & Zinkin, H. D. (2015). Medically inoperable peripheral lung cancer treated with stereotactic body radiation therapy. Radiation Oncology (London, England), 10, 120. https://doi.org/10.1186/s13014-015-0423-7CrossRef

52.

Strohl, M. P., Raigani, S., Ammori, J. B., Hardacre, J. M., & Kim, J. A. (2016). Surgery for localized pancreatic cancer: The trend is not improving. Pancreas, 45(5), 687–693. https://doi.org/10.1097/MPA.0000000000000511CrossRef

53.

de Geus, S. W. L., Eskander, M. F., Kasumova, G. G., Ng, S. C., Kent, T. S., Mancias, J. D., & Tseng, J. F. (2017). Stereotactic body radiotherapy for unresected pancreatic cancer: A nationwide review. Cancer, 123(21), 4158–4167. https://doi.org/10.1002/cncr.30856CrossRef

54.

Bown, S. G., Rogowska, A. Z., Whitelaw, D. E., Lees, W. R., Lovat, L. B., Ripley, P., & Hatfield, A. W. R. (2002). Photodynamic therapy for cancer of the pancreas. Gut, 50(4), 549–557. https://doi.org/10.1136/gut.50.4.549CrossRef

55.

DeWitt, J. M., Sandrasegaran, K., O’Neil, B., House, M. G., Zyromski, N. J., Sehdev, A., & Shahda, S. (2019). Phase 1 study of EUS-guided photodynamic therapy for locally advanced pancreatic cancer. Gastrointestinal Endoscopy, 89(2), 390–398. https://doi.org/10.1016/j.gie.2018.09.007CrossRef

56.

Wagner, A., Denzer, U. W., Neureiter, D., Kiesslich, T., Puespoeck, A., Rauws, E. A. J., & Wolkersdörfer, G. W. (2015). Temoporfin improves efficacy of photodynamic therapy in advanced biliary tract carcinoma: A multicenter prospective phase II study. Hepatology (Baltimore, Md.), 62(5), 1456–1465. https://doi.org/10.1002/hep.27905CrossRef

57.

Yang, J., Shen, H., Jin, H., Lou, Q., & Zhang, X. (2016). Treatment of unresectable extrahepatic cholangiocarcinoma using hematoporphyrin photodynamic therapy: A prospective study. Photodiagnosis and Photodynamic Therapy, 16, 110–118. https://doi.org/10.1016/j.pdpdt.2016.10.001CrossRef

58.

Hauge, T., Hauge, P. W., Warloe, T., Drolsum, A., Johansen, C., Viktil, E., & Konopski, Z. (2016). Randomised controlled trial of temoporfin photodynamic therapy plus chemotherapy in nonresectable biliary carcinoma–PCS Nordic study. Photodiagnosis and Photodynamic Therapy, 13, 330–333. https://doi.org/10.1016/j.pdpdt.2015.09.004CrossRef

59.

Lebdai, S., Bigot, P., Leroux, P.-A., Berthelot, L.-P., Maulaz, P., & Azzouzi, A.-R. (2017). Vascular targeted photodynamic therapy with padeliporfin for low risk prostate cancer treatment: Midterm oncologic outcomes. The Journal of Urology, 198(2), 335–344. https://doi.org/10.1016/j.juro.2017.03.119CrossRef

60.

Noweski, A., Roosen, A., Lebdai, S., Barret, E., Emberton, M., Benzaghou, F., & Azzouzi, A. R. (2019). Medium-term follow-up of vascular-targeted photodynamic therapy of localized prostate cancer using TOOKAD soluble WST-11 (phase II trials). European Urology Focus, 5(6), 1022–1028. https://doi.org/10.1016/j.euf.2018.04.003CrossRef

61.

Azzouzi, A.-R., Vincendeau, S., Barret, E., Cicco, A., Kleinclauss, F., van der Poel, H. G., PCM301 Study Group. (2017). Padeliporfin vascular-targeted photodynamic therapy versus active surveillance in men with low-risk prostate cancer (CLIN1001 PCM301): An open-label, phase 3, randomised controlled trial. The Lancet. Oncology, 18(2), 181–191. https://doi.org/10.1016/S1470-2045(16)30661-1CrossRef

62.

O’Day, R. F., Pejnovic, T. M., Isaacs, T., Muecke, J. S., Glasson, W. J., & Campbell, W. G. (2020). Australian and New Zealand study of photodynamic therapy in choroidal amelanotic melanoma. Retina (Philadelphia, Pa.), 40(5), 972–976. https://doi.org/10.1097/IAE.0000000000002520CrossRef

63.

Fabian, I. D., Stacey, A. W., Papastefanou, V., Al Harby, L., Arora, A. K., Sagoo, M. S., Medscape. (2017). Primary photodynamic therapy with verteporfin for small pigmented posterior pole choroidal melanoma. Eye (London, England), 31(4), 519–528. https://doi.org/10.1038/eye.2017.22CrossRef

64.

Xu, S., Bulin, A.-L., Hurbin, A., Elleaume, H., Coll, J.-L., & Broekgaarden, M. (2020). Photodynamic diagnosis and therapy for peritoneal carcinomatosis: Emerging perspectives. Cancers, 12(9), E2491. https://doi.org/10.3390/cancers12092491CrossRef

65.

Hillemanns, P., Wimberger, P., Reif, J., Stepp, H., & Klapdor, R. (2017). Photodynamic diagnosis with 5-aminolevulinic acid for intraoperative detection of peritoneal metastases of ovarian cancer: A feasibility and dose finding study. Lasers in Surgery and Medicine, 49(2), 169–176. https://doi.org/10.1002/lsm.22613CrossRef

66.

Liu, Y., Endo, Y., Fujita, T., Ishibashi, H., Nishioka, T., Canbay, E., & Yonemura, Y. (2014). Cytoreductive surgery under aminolevulinic acid-mediated photodynamic diagnosis plus hyperthermic intraperitoneal chemotherapy in patients with peritoneal carcinomatosis from ovarian cancer and primary peritoneal carcinoma: Results of a phase I trial. Annals of Surgical Oncology, 21(13), 4256–4262. https://doi.org/10.1245/s10434-014-3901-5CrossRef

67.

Cuenca, R. E., Allison, R. R., Sibata, C., & Downie, G. H. (2004). Breast cancer with chest wall progression: Treatment with photodynamic therapy. Annals of Surgical Oncology, 11(3), 322–327. https://doi.org/10.1245/aso.2004.03.025CrossRef

68.

Spring, B. Q., Bryan Sears, R., Zheng, L. Z., Mai, Z., Watanabe, R., Sherwood, M. E., & Hasan, T. (2016). A photoactivable multi-inhibitor nanoliposome for tumour control and simultaneous inhibition of treatment escape pathways. Nature Nanotechnology, 11(4), 378–387. https://doi.org/10.1038/nnano.2015.311CrossRef

69.

Plaetzer, K., Krammer, B., Berlanda, J., Berr, F., & Kiesslich, T. (2009). Photophysics and photochemistry of photodynamic therapy: Fundamental aspects. Lasers in Medical Science, 24(2), 259–268. https://doi.org/10.1007/s10103-008-0539-1CrossRef

70.

Kwiatkowski, S., Knap, B., Przystupski, D., Saczko, J., Kędzierska, E., Knap-Czop, K., & Kulbacka, J. (2018). Photodynamic therapy - Mechanisms, photosensitizers and combinations. Biomedicine & Pharmacotherapy = Biomedecine & Pharmacotherapie, 106, 1098–1107. https://doi.org/10.1016/j.biopha.2018.07.049CrossRef

71.

Baptista, M. S., Cadet, J., Di Mascio, P., Ghogare, A. A., Greer, A., Hamblin, M. R., & Yoshimura, T. M. (2017). Type I and type II photosensitized oxidation reactions: Guidelines and mechanistic pathways. Photochemistry and Photobiology, 93(4), 912–919. https://doi.org/10.1111/php.12716CrossRef

72.

Davies, M. J. (2016). Protein oxidation and peroxidation. The Biochemical Journal, 473(7), 805–825. https://doi.org/10.1042/BJ20151227CrossRef

73.

Davies, M. J. (2004). Reactive species formed on proteins exposed to singlet oxygen. Photochemical & Photobiological Sciences, 3(1), 17–25. https://doi.org/10.1039/B307576CCrossRef

74.

Zhang, W., Xiao, S., & Ahn, D. U. (2013). Protein oxidation: Basic principles and implications for meat quality. Critical Reviews in Food Science and Nutrition, 53(11), 1191–1201. https://doi.org/10.1080/10408398.2011.577540CrossRef

75.

Stadtman, E. R. (2001). Protein oxidation in aging and age-related diseases. Annals of the New York Academy of Sciences, 928, 22–38. https://doi.org/10.1111/j.1749-6632.2001.tb05632.xCrossRef

76.

Girotti, A. W. (2001). Photosensitized oxidation of membrane lipids: Reaction pathways, cytotoxic effects, and cytoprotective mechanisms. Journal of Photochemistry and Photobiology. B, Biology, 63(1–3), 103–113. https://doi.org/10.1016/s1011-1344(01)00207-xCrossRef

77.

Massiot, J., Rosilio, V., & Makky, A. (2019). Photo-triggerable liposomal drug delivery systems: From simple porphyrin insertion in the lipid bilayer towards supramolecular assemblies of lipid–porphyrin conjugates. Journal of Materials Chemistry B, 7(11), 1805–1823. https://doi.org/10.1039/C9TB00015ACrossRef

78.

Ayala, A., Muñoz, M. F., & Argüelles, S. (2014). Lipid peroxidation: Production, metabolism, and signaling mechanisms of malondialdehyde and 4-hydroxy-2-nonenal. Oxidative Medicine and Cellular Longevity, 2014, 360438. https://doi.org/10.1155/2014/360438CrossRef

79.

Tsaytler, P. A., O’Flaherty, M. C., Sakharov, D. V., Krijgsveld, J., & Egmond, M. R. (2008). Immediate protein targets of photodynamic treatment in carcinoma cells. Journal of Proteome Research, 7(9), 3868–3878. https://doi.org/10.1021/pr800189qCrossRef

80.

Spickett, C. M., & Pitt, A. R. (2020). Modification of proteins by reactive lipid oxidation products and biochemical effects of lipoxidation. Essays in Biochemistry, 64(1), 19–31. https://doi.org/10.1042/EBC20190058CrossRef

81.

Magi, B., Ettorre, A., Liberatori, S., Bini, L., Andreassi, M., Frosali, S., & Di Stefano, A. (2004). Selectivity of protein carbonylation in the apoptotic response to oxidative stress associated with photodynamic therapy: A cell biochemical and proteomic investigation. Cell Death and Differentiation, 11(8), 842–852. https://doi.org/10.1038/sj.cdd.4401427CrossRef

82.

Hsieh, Y.-J., Chien, K.-Y., Yang, I.-F., Lee, I.-N., Wu, C.-C., Huang, T.-Y., & Yu, J.-S. (2017). Oxidation of protein-bound methionine in photofrin-photodynamic therapy-treated human tumor cells explored by methionine-containing peptide enrichment and quantitative proteomics approach. Scientific Reports, 7(1), 1370. https://doi.org/10.1038/s41598-017-01409-9CrossRef

83.

Helander, L., Sharma, A., Krokan, H. E., Plaetzer, K., Krammer, B., Tortik, N., & Hagen, L. (2016). Photodynamic treatment with hexyl-aminolevulinate mediates reversible thiol oxidation in core oxidative stress signaling proteins. Molecular bioSystems, 12(3), 796–805. https://doi.org/10.1039/c5mb00744eCrossRef

84.

Ariffin, A. B., Forde, P. F., Jahangeer, S., Soden, D. M., & Hinchion, J. (2014). Releasing pressure in tumors: What do we know so far and where do we go from here? A review. Cancer Research, 74(10), 2655–2662. https://doi.org/10.1158/0008-5472.CAN-13-3696CrossRef

85.

Mukherjee, A., Madamsetty, V. S., Paul, M. K., & Mukherjee, S. (2020). Recent advancements of nanomedicine towards antiangiogenic therapy in cancer. International Journal of Molecular Sciences, 21(2), E455. https://doi.org/10.3390/ijms21020455CrossRef

86.

Jain, R. K. (2005). Normalization of tumor vasculature: An emerging concept in antiangiogenic therapy. Science (New York, N.Y.), 307(5706), 58–62. https://doi.org/10.1126/science.1104819CrossRef

87.

Al-Husein, B., Abdalla, M., Trepte, M., Deremer, D. L., & Somanath, P. R. (2012). Antiangiogenic therapy for cancer: An update. Pharmacotherapy, 32(12), 1095–1111. https://doi.org/10.1002/phar.1147CrossRef

88.

Minchinton, A. I., & Tannock, I. F. (2006). Drug penetration in solid tumours. Nature Reviews. Cancer, 6(8), 583–592. https://doi.org/10.1038/nrc1893CrossRef

89.

Chen, B., Pogue, B. W., Hoopes, P. J., & Hasan, T. (2006). Vascular and cellular targeting for photodynamic therapy. Critical Reviews in Eukaryotic Gene Expression, 16(4), 279–305. https://doi.org/10.1615/critreveukargeneexpr.v16.i4.10CrossRef

90.

Bhuvaneswari, R., Gan, Y. Y., Soo, K. C., & Olivo, M. (2009). The effect of photodynamic therapy on tumor angiogenesis. Cellular and molecular life sciences: CMLS, 66(14), 2275–2283. https://doi.org/10.1007/s00018-009-0016-4CrossRef

91.

Chen, B., Pogue, B. W., Hoopes, P. J., & Hasan, T. (2005). Combining vascular and cellular targeting regimens enhances the efficacy of photodynamic therapy. International Journal of Radiation Oncology, Biology, Physics, 61(4), 1216–1226. https://doi.org/10.1016/j.ijrobp.2004.08.006CrossRef

92.

Nowak-Sliwinska, P., van Beijnum, J. R., van Berkel, M., van den Bergh, H., & Griffioen, A. W. (2010). Vascular regrowth following photodynamic therapy in the chicken embryo chorioallantoic membrane. Angiogenesis, 13(4), 281–292. https://doi.org/10.1007/s10456-010-9185-xCrossRef

93.

Melincovici, C. S., Boşca, A. B., Şuşman, S., Mărginean, M., Mihu, C., Istrate, M., & Mihu, C. M. (2018). Vascular endothelial growth factor (VEGF) - Key factor in normal and pathological angiogenesis. Romanian Journal of Morphology and Embryology = Revue Roumaine De Morphologie Et Embryologie, 59(2), 455–467.

94.

Mashayekhi, V., t’Hoog, C. O., & Oliveira, S. (2019). Vascular targeted photodynamic therapy: A review of the efforts towards molecular targeting of tumor vasculature. Journal of Porphyrins and Phthalocyanines, 23(11–12), 1229–1240. https://doi.org/10.1142/s1088424619300180CrossRef

95.

Kim, S.-M., Rhee, Y.-H., & Kim, J.-S. (2017). The anticancer effects of radachlorin-mediated photodynamic therapy in the human endometrial adenocarcinoma cell line HEC-1-A. Anticancer Research, 37(11), 6251–6258. https://doi.org/10.21873/anticanres.12076CrossRef

96.

Dong, W., Zhang, X., & Lu, Z. (2020). Effect of 532nm photodynamic therapy with hemoporfin on the expression of vascular endothelial growth factor in cultured human vascular endothelial cells. Photodiagnosis and Photodynamic Therapy, 30, 101793. https://doi.org/10.1016/j.pdpdt.2020.101793CrossRef

97.

Ma, J., Lai, G., & Lu, Z. (2019). Effect of 410 nm photodynamic therapy with hemoporfin on the expression of vascular endothelial growth factor (VEGF) in cultured human vascular endothelial cells. Lasers in Medical Science, 34(1), 149–155. https://doi.org/10.1007/s10103-018-2649-8CrossRef

98.

Tsioumpekou, M., Cunha, S. I., Ma, H., Åhgren, A., Cedervall, J., Olsson, A.-K., & Lennartsson, J. (2020). Specific targeting of PDGFRβ in the stroma inhibits growth and angiogenesis in tumors with high PDGF-BB expression. Theranostics, 10(3), 1122–1135. https://doi.org/10.7150/thno.37851CrossRef

99.

Schieke, S. M., von Montfort, C., Buchczyk, D. P., Timmer, A., Grether-Beck, S., Krutmann, J., & Klotz, L.-O. (2004). Singlet oxygen-induced attenuation of growth factor signaling: Possible role of ceramides. Free Radical Research, 38(7), 729–737. https://doi.org/10.1080/10715760410001712764CrossRef

100.

Patmore, S., Dhami, S. P. S., & O’Sullivan, J. M. (2020). Von Willebrand factor and cancer; metastasis and coagulopathies. Journal of thrombosis and haemostasis: JTH, 18(10), 2444–2456. https://doi.org/10.1111/jth.14976CrossRef

101.

Han, X., Guo, B., Li, Y., & Zhu, B. (2014). Tissue factor in tumor microenvironment: A systematic review. Journal of Hematology & Oncology, 7, 54. https://doi.org/10.1186/s13045-014-0054-8CrossRef

102.

Fungaloi, P., Statius van Eps, R., Wu, Y.-P., Blankensteijn, J., de Groot, P., van Urk, H., & LaMuraglia, G. (2002). Platelet adhesion to photodynamic therapy-treated extracellular matrix proteins. Photochemistry and Photobiology, 75(4), 412–417. https://doi.org/10.1562/0031-8655(2002)075%3c0412:patptt%3e2.0.co;2CrossRef

103.

Shi, W., Yin, Y., Wang, Y., Zhang, B., Tan, P., Jiang, T., & Hu, Y. (2017). A tissue factor-cascade-targeted strategy to tumor vasculature: A combination of EGFP-EGF1 conjugation nanoparticles with photodynamic therapy. Oncotarget, 8(19), 32212–32227. https://doi.org/10.18632/oncotarget.12922CrossRef

104.

Cheng, J., Xu, J., Duanmu, J., Zhou, H., Booth, C. J., & Hu, Z. (2011). Effective treatment of human lung cancer by targeting tissue factor with a factor VII-targeted photodynamic therapy. Current Cancer Drug Targets, 11(9), 1069–1081. https://doi.org/10.2174/156800911798073023CrossRef

105.

Hu, Z., Rao, B., Chen, S., & Duanmu, J. (2010). Targeting tissue factor on tumour cells and angiogenic vascular endothelial cells by factor VII-targeted verteporfin photodynamic therapy for breast cancer in vitro and in vivo in mice. BMC Cancer, 10, 235. https://doi.org/10.1186/1471-2407-10-235CrossRef

106.

Hu, Z., Rao, B., Chen, S., & Duanmu, J. (2011). Selective and effective killing of angiogenic vascular endothelial cells and cancer cells by targeting tissue factor using a factor VII-targeted photodynamic therapy for breast cancer. Breast Cancer Research and Treatment, 126(3), 589–600. https://doi.org/10.1007/s10549-010-0957-1CrossRef

107.

Shi, Q., Tao, Z., Yang, H., Fan, Q., Wei, D., Wan, L., & Lu, X. (2017). PDGFRβ-specific affibody-directed delivery of a photosensitizer, IR700, is efficient for vascular-targeted photodynamic therapy of colorectal cancer. Drug Delivery, 24(1), 1818–1830. https://doi.org/10.1080/10717544.2017.1407011CrossRef

108.

Cox, T. R. (2021). The matrix in cancer. Nature Reviews. Cancer, 21(4), 217–238. https://doi.org/10.1038/s41568-020-00329-7CrossRef

109.

Kalluri, R. (2016). The biology and function of fibroblasts in cancer. Nature Reviews. Cancer, 16(9), 582–598. https://doi.org/10.1038/nrc.2016.73CrossRef

110.

Heldin, C.-H., Rubin, K., Pietras, K., & Ostman, A. (2004). High interstitial fluid pressure - An obstacle in cancer therapy. Nature Reviews. Cancer, 4(10), 806–813. https://doi.org/10.1038/nrc1456CrossRef

111.

Heino, J. (2007). The collagen family members as cell adhesion proteins. BioEssays: News and Reviews in Molecular, Cellular and Developmental Biology, 29(10), 1001–1010. https://doi.org/10.1002/bies.20636CrossRef

112.

Davidenko, N., Schuster, C. F., Bax, D. V., Farndale, R. W., Hamaia, S., Best, S. M., & Cameron, R. E. (2016). Evaluation of cell binding to collagen and gelatin: A study of the effect of 2D and 3D architecture and surface chemistry. Journal of Materials Science. Materials in Medicine, 27(10), 148. https://doi.org/10.1007/s10856-016-5763-9CrossRef

113.

Fang, M., Yuan, J., Peng, C., & Li, Y. (2014). Collagen as a double-edged sword in tumor progression. Tumour Biology: The Journal of the International Society for Oncodevelopmental Biology and Medicine, 35(4), 2871–2882. https://doi.org/10.1007/s13277-013-1511-7CrossRef

114.

El-Far, M. A., & Pimstone, N. R. (1985). The interaction of tumour-localizing porphyrins with collagen, elastin, gelatin, fibrin and fibrinogen. Cell Biochemistry and Function, 3(2), 115–119. https://doi.org/10.1002/cbf.290030206CrossRef

115.

Musser, D. A., Wagner, J. M., & Datta-Gupta, M. (1982). The interaction of tumor localizing porphyrins with collagen and elastin. Research Communications in Chemical Pathology and Pharmacology, 36(2), 251–259.

116.

Vincent, P., Bruza, P., Palisoul, S. M., Gunn, J. R., Samkoe, K. S., Hoopes, P. J., … Pogue, B. W. (2021). Visualization and quantification of pancreatic tumor stroma in fresh tissue via ultraviolet surface excitation. Journal of Biomedical Optics, 26(1). https://doi.org/10.1117/1.JBO.26.1.016002

117.

Overchuk, M., Harmatys, K. M., Sindhwani, S., Rajora, M. A., Koebel, A., Charron, D. M., & Zheng, G. (2021). Subtherapeutic photodynamic treatment facilitates tumor nanomedicine delivery and overcomes desmoplasia. Nano Letters, 21(1), 344–352. https://doi.org/10.1021/acs.nanolett.0c03731CrossRef

118.

Li, J., Huang, J., Ao, Y., Li, S., Miao, Y., Yu, Z., & Yang, X. (2018). Synergizing upconversion nanophotosensitizers with hyperbaric oxygen to remodel the extracellular matrix for enhanced photodynamic cancer therapy. ACS applied materials & interfaces, 10(27), 22985–22996. https://doi.org/10.1021/acsami.8b07090CrossRef

119.

Maas, A. L., Carter, S. L., Wileyto, E. P., Miller, J., Yuan, M., Yu, G., & Busch, T. M. (2012). Tumor vascular microenvironment determines responsiveness to photodynamic therapy. Cancer Research, 72(8), 2079–2088. https://doi.org/10.1158/0008-5472.CAN-11-3744CrossRef

120.

Nelson, J. S., Liaw, L. H., Orenstein, A., Roberts, W. G., & Berns, M. W. (1988). Mechanism of tumor destruction following photodynamic therapy with hematoporphyrin derivative, chlorin, and phthalocyanine. Journal of the National Cancer Institute, 80(20), 1599–1605. https://doi.org/10.1093/jnci/80.20.1599CrossRef

121.

Georgiou, S., Papazoglou, T., Dafnomili, D., Coutsolelos, A. G., Kouklaki, V., & Tosca, A. (1994). Photophysical characterization of hematoporphyrin incorporated within collagen gels. Journal of Photochemistry and Photobiology. B, Biology, 22(1), 45–50. https://doi.org/10.1016/1011-1344(93)06950-8CrossRef

122.

Zhang, C., Wang, J., Chou, A., Gong, T., Devine, E. E., & Jiang, J. J. (2018). Photodynamic therapy induces antifibrotic alterations in primary human vocal fold fibroblasts. The Laryngoscope, 128(9), E323–E331. https://doi.org/10.1002/lary.27219CrossRef

123.

Verrico, A. K., & Moore, J. V. (1997). Expression of the collagen-related heat shock protein HSP47 in fibroblasts treated with hyperthermia or photodynamic therapy. British Journal of Cancer, 76(6), 719–724. https://doi.org/10.1038/bjc.1997.452CrossRef

124.

Zheng, Z., Zhu, L., Zhang, X., Li, L., Moon, S., Roh, M. R., & Jin, Z. (2015). RUNX3 expression is associated with sensitivity to pheophorbide a-based photodynamic therapy in keloids. Lasers in Medical Science, 30(1), 67–75. https://doi.org/10.1007/s10103-014-1614-4CrossRef

125.

Barr, H., Bown, S. G., Krasner, N., & Boulos, P. B. (1989). Photodynamic therapy for colorectal disease. International Journal of Colorectal Disease, 4(1), 15–19. https://doi.org/10.1007/BF01648544CrossRef

126.

Szeimies, R. M., Torezan, L., Niwa, A., Valente, N., Unger, P., Kohl, E., & Festa-Neto, C. (2012). Clinical, histopathological and immunohistochemical assessment of human skin field cancerization before and after photodynamic therapy. The British Journal of Dermatology, 167(1), 150–159. https://doi.org/10.1111/j.1365-2133.2012.10887.xCrossRef

127.

Shackley, D. C., Haylett, A., Whitehurst, C., Betts, C. D., O’Flynn, K., Clarke, N. W., & Moore, J. V. (2002). Comparison of the cellular molecular stress responses after treatments used in bladder cancer. BJU international, 90(9), 924–932. https://doi.org/10.1046/j.1464-410x.2002.03024.xCrossRef

128.

Ayaru, L., Wittmann, J., Macrobert, A. J., Novelli, M., Bown, S. G., & Pereira, S. P. (2007). Photodynamic therapy using verteporfin photosensitization in the pancreas and surrounding tissues in the Syrian golden hamster. Pancreatology: official journal of the International Association of Pancreatology (IAP) … [et al.], 7(1), 20–27. https://doi.org/10.1159/000101874CrossRef

129.

Barr, H., Tralau, C. J., MacRobert, A. J., Krasner, N., Boulos, P. B., Clark, C. G., & Bown, S. G. (1987). Photodynamic therapy in the normal rat colon with phthalocyanine sensitisation. British Journal of Cancer, 56(2), 111–118. https://doi.org/10.1038/bjc.1987.166CrossRef

130.

Barr, H., Tralau, C. J., Boulos, P. B., MacRobert, A. J., Tilly, R., & Bown, S. G. (1987). The contrasting mechanisms of colonic collagen damage between photodynamic therapy and thermal injury. Photochemistry and Photobiology, 46(5), 795–800. https://doi.org/10.1111/j.1751-1097.1987.tb04850.xCrossRef

131.

Barr, H., MacRobert, A. J., Tralau, C. J., Boulos, P. B., & Bown, S. G. (1990). The significance of the nature of the photosensitizer for photodynamic therapy: Quantitative and biological studies in the colon. British Journal of Cancer, 62(5), 730–735. https://doi.org/10.1038/bjc.1990.368CrossRef

132.

Kohl, E., Torezan, L. A. R., Landthaler, M., & Szeimies, R.-M. (2010). Aesthetic effects of topical photodynamic therapy. Journal of the European Academy of Dermatology and Venereology: JEADV, 24(11), 1261–1269. https://doi.org/10.1111/j.1468-3083.2010.03625.xCrossRef

133.

Lv, T., Huang, Z.-F., Wang, H.-W., Lin, J.-Q., Chen, G.-N., Chen, X.-W., & Wang, X.-L. (2012). Evaluation of collagen alteration after topical photodynamic therapy (PDT) using second harmonic generation (SHG) microscopy–in vivo study in a mouse model. Photodiagnosis and Photodynamic Therapy, 9(2), 164–169. https://doi.org/10.1016/j.pdpdt.2011.12.006CrossRef

134.

Lima, C. A., Goulart, V. P., Bechara, E. J. H., Correa, L., & Zezell, D. M. (2016). Optimization and therapeutic effects of PDT mediated by ALA and MAL in the treatment of cutaneous malignant lesions: A comparative study. Journal of Biophotonics, 9(11–12), 1355–1361. https://doi.org/10.1002/jbio.201600164CrossRef

135.

Bhuvaneswari, R., Gan, Y. Y., Lucky, S. S., Chin, W. W. L., Ali, S. M., Soo, K. C., & Olivo, M. (2008). Molecular profiling of angiogenesis in hypericin mediated photodynamic therapy. Molecular Cancer, 7, 56. https://doi.org/10.1186/1476-4598-7-56CrossRef

136.

Uehara, M., Inokuchi, T., Tobita, T., Ohba, S., & Asahina, I. (2007). Expression of heat shock protein 47 in the fibrous tissue adjacent to mouse tumour subjected to photodynamic therapy. Oral Oncology, 43(8), 804–810. https://doi.org/10.1016/j.oraloncology.2006.10.002CrossRef

137.

Lin, T.-C., Yang, C.-H., Cheng, L.-H., Chang, W.-T., Lin, Y.-R., & Cheng, H.-C. (2019). Fibronectin in cancer: Friend or foe. Cells, 9(1), E27. https://doi.org/10.3390/cells9010027CrossRef

138.

Vaheri, A., Kurkinen, M., Lehto, V. P., Linder, E., & Timpl, R. (1978). Codistribution of pericellular matrix proteins in cultured fibroblasts and loss in transformation: Fibronectin and procollagen. Proceedings of the National Academy of Sciences of the United States of America, 75(10), 4944–4948. https://doi.org/10.1073/pnas.75.10.4944CrossRef

139.

Vaheri, A., & Mosher, D. F. (1978). High molecular weight, cell surface-associated glycoprotein (fibronectin) lost in malignant transformation. Biochimica Et Biophysica Acta, 516(1), 1–25. https://doi.org/10.1016/0304-419x(78)90002-1CrossRef

140.

Li, Y., Miao, L., Yu, M., Shi, M., Wang, Y., Yang, J., & Cai, H. (2017). α1-antitrypsin promotes lung adenocarcinoma metastasis through upregulating fibronectin expression. International Journal of Oncology, 50(6), 1955–1964. https://doi.org/10.3892/ijo.2017.3962CrossRef

141.

Kenny, H. A., Chiang, C.-Y., White, E. A., Schryver, E. M., Habis, M., Romero, I. L., & Lengyel, E. (2014). Mesothelial cells promote early ovarian cancer metastasis through fibronectin secretion. The Journal of Clinical Investigation, 124(10), 4614–4628. https://doi.org/10.1172/JCI74778CrossRef

142.

Niknami, Z., Eslamifar, A., Emamirazavi, A., Ebrahimi, A., & Shirkoohi, R. (2017). The association of vimentin and fibronectin gene expression with epithelial-mesenchymal transition and tumor malignancy in colorectal carcinoma. EXCLI journal, 16, 1009–1017. https://doi.org/10.17179/excli2017-481CrossRef

143.

Fernandez-Garcia, B., Eiró, N., Marín, L., González-Reyes, S., González, L. O., Lamelas, M. L., & Vizoso, F. J. (2014). Expression and prognostic significance of fibronectin and matrix metalloproteases in breast cancer metastasis. Histopathology, 64(4), 512–522. https://doi.org/10.1111/his.12300CrossRef

144.

Choi, I.-K., Strauss, R., Richter, M., Yun, C.-O., & Lieber, A. (2013). Strategies to increase drug penetration in solid tumors. Frontiers in Oncology, 3, 193. https://doi.org/10.3389/fonc.2013.00193CrossRef

145.

Chuang, C. Y., Degendorfer, G., Hammer, A., Whitelock, J. M., Malle, E., & Davies, M. J. (2014). Oxidation modifies the structure and function of the extracellular matrix generated by human coronary artery endothelial cells. The Biochemical Journal, 459(2), 313–322. https://doi.org/10.1042/BJ20131471CrossRef

146.

Aumailley, M. (2013). The laminin family. Cell Adhesion & Migration, 7(1), 48–55. https://doi.org/10.4161/cam.22826CrossRef

147.

Ramovs, V., Te Molder, L., & Sonnenberg, A. (2017). The opposing roles of laminin-binding integrins in cancer. Matrix Biology: Journal of the International Society for Matrix Biology, 57–58, 213–243. https://doi.org/10.1016/j.matbio.2016.08.007CrossRef

148.

Nybo, T., Dieterich, S., Gamon, L. F., Chuang, C. Y., Hammer, A., Hoefler, G., & Davies, M. J. (2019). Chlorination and oxidation of the extracellular matrix protein laminin and basement membrane extracts by hypochlorous acid and myeloperoxidase. Redox Biology, 20, 496–513. https://doi.org/10.1016/j.redox.2018.10.022CrossRef

149.

Lorentzen, L. G., Chuang, C. Y., Rogowska-Wrzesinska, A., & Davies, M. J. (2019). Identification and quantification of sites of nitration and oxidation in the key matrix protein laminin and the structural consequences of these modifications. Redox Biology, 24, 101226. https://doi.org/10.1016/j.redox.2019.101226CrossRef

150.

Ziółkowski, P., Symonowicz, K., Osiecka, B. J., Rabczyn Ski, J., & Gerber, J. (1999). Photodynamic treatment of epithelial tissue derived from patients with endometrial cancer: A contribution to the role of laminin and epidermal growth factor receptor in photodynamic therapy. Journal of Biomedical Optics, 4(3), 272–275. https://doi.org/10.1117/1.429928CrossRef

151.

Lei, T. C., Vieira, W. D., & Hearing, V. J. (2002). In vitro migration of melanoblasts requires matrix metalloproteinase-2: Implications to vitiligo therapy by photochemotherapy. Pigment Cell Research, 15(6), 426–432. https://doi.org/10.1034/j.1600-0749.2002.02044.xCrossRef

152.

Wong, K. M., Horton, K. J., Coveler, A. L., Hingorani, S. R., & Harris, W. P. (2017). Targeting the tumor stroma: The biology and clinical development of pegylated recombinant human hyaluronidase (PEGPH20). Current Oncology Reports, 19(7), 47. https://doi.org/10.1007/s11912-017-0608-3CrossRef

153.

Snetkov, P., Zakharova, K., Morozkina, S., Olekhnovich, R., & Uspenskaya, M. (2020). Hyaluronic acid: The influence of molecular weight on structural, physical, physico-chemical, and degradable properties of biopolymer. Polymers, 12(8), 1800. https://doi.org/10.3390/polym12081800CrossRef

154.

Yusupov, M., Privat-Maldonado, A., Cordeiro, R. M., Verswyvel, H., Shaw, P., Razzokov, J., & Bogaerts, A. (2021). Oxidative damage to hyaluronan-CD44 interactions as an underlying mechanism of action of oxidative stress-inducing cancer therapy. Redox Biology, 43, 101968. https://doi.org/10.1016/j.redox.2021.101968CrossRef

155.

Mithieux, S. M., & Weiss, A. S. (2005). Elastin. Advances in protein chemistry, 70, 437–461. https://doi.org/10.1016/S0065-3233(05)70013-9CrossRef

156.

Santi, A., Kugeratski, F. G., & Zanivan, S. (2018). Cancer associated fibroblasts: The architects of stroma remodeling. Proteomics, 18(5–6), e1700167. https://doi.org/10.1002/pmic.201700167CrossRef

157.

Socovich, A. M., & Naba, A. (2019). The cancer matrisome: From comprehensive characterization to biomarker discovery. Seminars in Cell & Developmental Biology, 89, 157–166. https://doi.org/10.1016/j.semcdb.2018.06.005CrossRef

158.

Balkwill, F. R., Capasso, M., & Hagemann, T. (2012). The tumor microenvironment at a glance. Journal of Cell Science, 125(Pt 23), 5591–5596. https://doi.org/10.1242/jcs.116392CrossRef

159.

Levental, K. R., Yu, H., Kass, L., Lakins, J. N., Egeblad, M., Erler, J. T., & Weaver, V. M. (2009). Matrix crosslinking forces tumor progression by enhancing integrin signaling. Cell, 139(5), 891–906. https://doi.org/10.1016/j.cell.2009.10.027CrossRef

160.

Yasui, Y., Abe, T., Kurosaki, M., Higuchi, M., Komiyama, Y., Yoshida, T., & Izumi, N. (2016). Elastin fiber accumulation in liver correlates with the development of hepatocellular carcinoma. PLoS ONE, 11(4), e0154558. https://doi.org/10.1371/journal.pone.0154558CrossRef

161.

Li, J., Xu, X., Jiang, Y., Hansbro, N. G., Hansbro, P. M., Xu, J., & Liu, G. (2020). Elastin is a key factor of tumor development in colorectal cancer. BMC Cancer, 20(1), 217. https://doi.org/10.1186/s12885-020-6686-xCrossRef

162.

Grant, W. E., Buonaccorsi, G., Speight, P. M., MacRobert, A. J., Hopper, C., & Bown, S. G. (1995). The effect of photodynamic therapy on the mechanical integrity of normal rabbit carotid arteries. The Laryngoscope, 105(8 Pt 1), 867–871. https://doi.org/10.1288/00005537-199508000-00019CrossRef

163.

Garrier, J., Bezdetnaya, L., Barlier, C., Gräfe, S., Guillemin, F., & D’Hallewin, M.-A. (2011). Foslip®-based photodynamic therapy as a means to improve wound healing. Photodiagnosis and Photodynamic Therapy, 8(4), 321–327. https://doi.org/10.1016/j.pdpdt.2011.06.003CrossRef

164.

Ji, J., Zhang, L.-L., Ding, H.-L., Wang, H.-W., Huang, Z., Wang, X.-X., & Wang, X.-L. (2014). Comparison of 5-aminolevulinic acid photodynamic therapy and red light for treatment of photoaging. Photodiagnosis and Photodynamic Therapy, 11(2), 118–121. https://doi.org/10.1016/j.pdpdt.2014.02.007CrossRef

165.

da-de-Jesus, P. C. C., Saeki, S. I. N., & Tedesco, A. C. (2016). An ex vivo study of photobiostimulation in the treatment of skin pathologies. Journal of Biophotonics, 9(11–12), 1189–1198. https://doi.org/10.1002/jbio.201500288CrossRef

166.

Park, M. Y., Sohn, S., Lee, E.-S., & Kim, Y. C. (2010). Photorejuvenation induced by 5-aminolevulinic acid photodynamic therapy in patients with actinic keratosis: A histologic analysis. Journal of the American Academy of Dermatology, 62(1), 85–95. https://doi.org/10.1016/j.jaad.2009.06.025CrossRef

167.

Campbell, S. M., Tyrrell, J., Marshall, R., & Curnow, A. (2010). Effect of MAL-photodynamic therapy on hypertrophic scarring. Photodiagnosis and Photodynamic Therapy, 7(3), 183–188. https://doi.org/10.1016/j.pdpdt.2010.07.003CrossRef

168.

Mills, S. J., Farrar, M. D., Ashcroft, G. S., Griffiths, C. E. M., Hardman, M. J., & Rhodes, L. E. (2014). Topical photodynamic therapy following excisional wounding of human skin increases production of transforming growth factor-β3 and matrix metalloproteinases 1 and 9, with associated improvement in dermal matrix organization. The British Journal of Dermatology, 171(1), 55–62. https://doi.org/10.1111/bjd.12843CrossRef

169.

Pazos, M. D. C., & Nader, H. B. (2007). Effect of photodynamic therapy on the extracellular matrix and associated components. Brazilian Journal of Medical and Biological Research, 40, 1025–1035.CrossRef

170.

Takada, Y., Ye, X., & Simon, S. (2007). The integrins. Genome Biology, 8(5), 215. https://doi.org/10.1186/gb-2007-8-5-215CrossRef

171.

Milla Sanabria, L., Rodríguez, M. E., Cogno, I. S., Rumie Vittar, N. B., Pansa, M. F., Lamberti, M. J., & Rivarola, V. A. (2013). Direct and indirect photodynamic therapy effects on the cellular and molecular components of the tumor microenvironment. Biochimica Et Biophysica Acta, 1835(1), 36–45. https://doi.org/10.1016/j.bbcan.2012.10.001CrossRef

172.

Hamidi, H., & Ivaska, J. (2018). Every step of the way: Integrins in cancer progression and metastasis. Nature Reviews Cancer, 18(9), 533–548. https://doi.org/10.1038/s41568-018-0038-zCrossRef

173.

Najafi, M., Farhood, B., & Mortezaee, K. (2019). Extracellular matrix (ECM) stiffness and degradation as cancer drivers. Journal of Cellular Biochemistry, 120(3), 2782–2790. https://doi.org/10.1002/jcb.27681CrossRef

174.

Cruz da Silva, E., Dontenwill, M., Choulier, L., & Lehmann, M. (2019). Role of integrins in resistance to therapies targeting growth factor receptors in cancer. Cancers, 11(5), 692. https://doi.org/10.3390/cancers11050692CrossRef

175.

Klein, O. J., Yuan, H., Nowell, N. H., Kaittanis, C., Josephson, L., & Evans, C. L. (2017). An integrin-targeted, highly diffusive construct for photodynamic therapy. Scientific Reports, 7(1), 13375. https://doi.org/10.1038/s41598-017-13803-4CrossRef

176.

Yan, F., Wu, H., Liu, H., Deng, Z., Liu, H., Duan, W., & Zheng, H. (2016). Molecular imaging-guided photothermal/photodynamic therapy against tumor by iRGD-modified indocyanine green nanoparticles. Journal of Controlled Release: Official Journal of the Controlled Release Society, 224, 217–228. https://doi.org/10.1016/j.jconrel.2015.12.050CrossRef

177.

Yuan, Y., & Liu, B. (2014). Self-assembled nanoparticles based on PEGylated conjugated polyelectrolyte and drug molecules for image-guided drug delivery and photodynamic therapy. ACS applied materials & interfaces, 6(17), 14903–14910. https://doi.org/10.1021/am5020925CrossRef

178.

Li, M.-M., Cao, J., Yang, J.-C., Shen, Y.-J., Cai, X.-L., Chen, Y.-W., & Xu, L.-M. (2017). Effects of arginine-glycine-aspartic acid peptide-conjugated quantum dots-induced photodynamic therapy on pancreatic carcinoma in vivo. International Journal of Nanomedicine, 12, 2769–2779. https://doi.org/10.2147/IJN.S130799CrossRef

179.

Frochot, C., Di Stasio, B., Vanderesse, R., Belgy, M.-J., Dodeller, M., Guillemin, F., & Barberi-Heyob, M. (2007). Interest of RGD-containing linear or cyclic peptide targeted tetraphenylchlorin as novel photosensitizers for selective photodynamic activity. Bioorganic Chemistry, 35(3), 205–220. https://doi.org/10.1016/j.bioorg.2006.11.005CrossRef

180.

Kim, S. K., Lee, J. M., Oh, K. T., & Lee, E. S. (2017). Extremely small-sized globular poly(ethylene glycol)-cyclic RGD conjugates targeting integrin αvβ3 in tumor cells. International Journal of Pharmaceutics, 528(1–2), 1–7. https://doi.org/10.1016/j.ijpharm.2017.05.068CrossRef

181.

Mani, J., Fleger, J., Rutz, J., Maxeiner, S., Bernd, A., Kippenberger, S., & Blaheta, R. A. (2019). Curcumin combined with exposure to visible light blocks bladder cancer cell adhesion and migration by an integrin dependent mechanism. European Review for Medical and Pharmacological Sciences, 23(23), 10564–10574. https://doi.org/10.26355/eurrev_201912_19698CrossRef

182.

Galaz, S., Espada, J., Stockert, J. C., Pacheco, M., Sanz-Rodríguez, F., Arranz, R., & Juarranz, A. (2005). Loss of E-cadherin mediated cell-cell adhesion as an early trigger of apoptosis induced by photodynamic treatment. Journal of Cellular Physiology, 205(1), 86–96. https://doi.org/10.1002/jcp.20374CrossRef

183.

Pacheco-Soares, C., Maftou-Costa, M., DA Cunha-Menezes Costa, C. G., DE Siqueira Silva, A. C., & Moraes, K. C. M. (2014). Evaluation of photodynamic therapy in adhesion protein expression. Oncology Letters, 8(2), 714–718. https://doi.org/10.3892/ol.2014.2149CrossRef

184.

Runnels, J. M., Chen, N., Ortel, B., Kato, D., & Hasan, T. (1999). BPD-MA-mediated photosensitization in vitro and in vivo: Cellular adhesion and beta1 integrin expression in ovarian cancer cells. British Journal of Cancer, 80(7), 946–953. https://doi.org/10.1038/sj.bjc.6690448CrossRef

185.

Uzdensky, A. B., Juzeniene, A., Kolpakova, E., Hjortland, G.-O., Juzenas, P., & Moan, J. (2004). Photosensitization with protoporphyrin IX inhibits attachment of cancer cells to a substratum. Biochemical and Biophysical Research Communications, 322(2), 452–457. https://doi.org/10.1016/j.bbrc.2004.07.132CrossRef

186.

Margaron, P., Sorrenti, R., & Levy, J. G. (1997). Photodynamic therapy inhibits cell adhesion without altering integrin expression. Biochimica Et Biophysica Acta, 1359(3), 200–210. https://doi.org/10.1016/s0167-4889(97)00115-8CrossRef

187.

Fahey, J. M., & Girotti, A. W. (2015). Accelerated migration and invasion of prostate cancer cells after a photodynamic therapy-like challenge: Role of nitric oxide. Nitric Oxide: Biology and Chemistry, 49, 47–55. https://doi.org/10.1016/j.niox.2015.05.006CrossRef

188.

Casas, A., Venosa, G. D., Vanzulli, S., Perotti, C., Mamome, L., Rodriguez, L., & Batlle, A. (2008). Decreased metastatic phenotype in cells resistant to aminolevulinic acid-photodynamic therapy. Cancer Letters, 271(2), 342–351. https://doi.org/10.1016/j.canlet.2008.06.023CrossRef

189.

Mahmoudi, K., Garvey, K. L., Bouras, A., Cramer, G., Stepp, H., Jesu Raj, J. G., & Hadjipanayis, C. G. (2019). 5-aminolevulinic acid photodynamic therapy for the treatment of high-grade gliomas. Journal of Neuro-Oncology, 141(3), 595–607. https://doi.org/10.1007/s11060-019-03103-4CrossRef

190.

Özdemir, B. C., Pentcheva-Hoang, T., Carstens, J. L., Zheng, X., Wu, C.-C., Simpson, T. R., & Kalluri, R. (2014). Depletion of carcinoma-associated fibroblasts and fibrosis induces immunosuppression and accelerates pancreas cancer with reduced survival. Cancer Cell, 25(6), 719–734. https://doi.org/10.1016/j.ccr.2014.04.005CrossRef

191.

Leitinger, B. (2014). Discoidin domain receptor functions in physiological and pathological conditions. International Review of Cell and Molecular Biology, 310, 39–87. https://doi.org/10.1016/B978-0-12-800180-6.00002-5CrossRef

192.

Hou, G., Vogel, W., & Bendeck, M. P. (2001). The discoidin domain receptor tyrosine kinase DDR1 in arterial wound repair. The Journal of Clinical Investigation, 107(6), 727–735. https://doi.org/10.1172/JCI10720CrossRef

193.

Ferri, N., Carragher, N. O., & Raines, E. W. (2004). Role of discoidin domain receptors 1 and 2 in human smooth muscle cell-mediated collagen remodeling: Potential implications in atherosclerosis and lymphangioleiomyomatosis. The American Journal of Pathology, 164(5), 1575–1585. https://doi.org/10.1016/S0002-9440(10)63716-9CrossRef

194.

Roberts, M. E., Magowan, L., Hall, I. P., & Johnson, S. R. (2011). Discoidin domain receptor 1 regulates bronchial epithelial repair and matrix metalloproteinase production. The European Respiratory Journal, 37(6), 1482–1493. https://doi.org/10.1183/09031936.00039710CrossRef

195.

Kawai, I., Hisaki, T., Sugiura, K., Naito, K., & Kano, K. (2012). Discoidin domain receptor 2 (DDR2) regulates proliferation of endochondral cells in mice. Biochemical and Biophysical Research Communications, 427(3), 611–617. https://doi.org/10.1016/j.bbrc.2012.09.106CrossRef

196.

Suh, H. N., & Han, H. J. (2011). Collagen I regulates the self-renewal of mouse embryonic stem cells through α2β1 integrin- and DDR1-dependent Bmi-1. Journal of Cellular Physiology, 226(12), 3422–3432. https://doi.org/10.1002/jcp.22697CrossRef

197.

Hachehouche, L. N., Chetoui, N., & Aoudjit, F. (2010). Implication of discoidin domain receptor 1 in T cell migration in three-dimensional collagen. Molecular Immunology, 47(9), 1866–1869. https://doi.org/10.1016/j.molimm.2010.02.023CrossRef

198.

Valiathan, R. R., Marco, M., Leitinger, B., Kleer, C. G., & Fridman, R. (2012). Discoidin domain receptor tyrosine kinases: New players in cancer progression. Cancer Metastasis Reviews, 31(1–2), 295–321. https://doi.org/10.1007/s10555-012-9346-zCrossRef

199.

Valencia, K., Ormazábal, C., Zandueta, C., Luis-Ravelo, D., Antón, I., Pajares, M. J., & Lecanda, F. (2012). Inhibition of collagen receptor discoidin domain receptor-1 (DDR1) reduces cell survival, homing, and colonization in lung cancer bone metastasis. Clinical Cancer Research: An Official Journal of the American Association for Cancer Research, 18(4), 969–980. https://doi.org/10.1158/1078-0432.CCR-11-1686CrossRef

200.

Shintani, Y., Fukumoto, Y., Chaika, N., Svoboda, R., Wheelock, M. J., & Johnson, K. R. (2008). Collagen I-mediated up-regulation of N-cadherin requires cooperative signals from integrins and discoidin domain receptor 1. The Journal of Cell Biology, 180(6), 1277–1289. https://doi.org/10.1083/jcb.200708137CrossRef

201.

Morgan, M. R., Humphries, M. J., & Bass, M. D. (2007). Synergistic control of cell adhesion by integrins and syndecans. Nature Reviews. Molecular Cell Biology, 8(12), 957–969. https://doi.org/10.1038/nrm2289CrossRef

202.

Beauvais, D. M., & Rapraeger, A. C. (2004). Syndecans in tumor cell adhesion and signaling. Reproductive biology and endocrinology: RB&E, 2, 3. https://doi.org/10.1186/1477-7827-2-3CrossRef

203.

Woods, A., & Couchman, J. R. (2001). Syndecan-4 and focal adhesion function. Current Opinion in Cell Biology, 13(5), 578–583. https://doi.org/10.1016/s0955-0674(00)00254-4CrossRef

204.

Keller-Pinter, A., Gyulai-Nagy, S., Becsky, D., Dux, L., & Rovo, L. (2021). Syndecan-4 in tumor cell motility. Cancers, 13(13), 3322. https://doi.org/10.3390/cancers13133322CrossRef

205.

Liao, W.-C., Yen, H.-R., Chen, C.-H., Chu, Y.-H., Song, Y.-C., Tseng, T.-J., & Liu, C.-H. (2021). CHPF promotes malignancy of breast cancer cells by modifying syndecan-4 and the tumor microenvironment. American Journal of Cancer Research, 11(3), 812–826.

206.

de Pazos, M. C., Ricci, R., Simioni, A. R., Lopes, C. C., Tedesco, A. C., & Nader, H. B. (2007). Putative role of heparan sulfate proteoglycan expression and shedding on the proliferation and survival of cells after photodynamic therapy. The International Journal of Biochemistry & Cell Biology, 39(6), 1130–1141. https://doi.org/10.1016/j.biocel.2007.02.008CrossRef

207.

Chen, C., Zhao, S., Karnad, A., & Freeman, J. W. (2018). The biology and role of CD44 in cancer progression: Therapeutic implications. Journal of Hematology & Oncology, 11(1), 64. https://doi.org/10.1186/s13045-018-0605-5CrossRef

208.

Ponta, H., Sherman, L., & Herrlich, P. A. (2003). CD44: From adhesion molecules to signalling regulators. Nature Reviews. Molecular Cell Biology, 4(1), 33–45. https://doi.org/10.1038/nrm1004CrossRef

209.

Hassn Mesrati, M., Syafruddin, S. E., Mohtar, M. A., & Syahir, A. (2021). CD44: A multifunctional mediator of cancer progression. Biomolecules, 11(12), 1850. https://doi.org/10.3390/biom11121850CrossRef

210.

Zhang, H., Brown, R. L., Wei, Y., Zhao, P., Liu, S., Liu, X., & Cheng, C. (2019). CD44 splice isoform switching determines breast cancer stem cell state. Genes & Development, 33(3–4), 166–179. https://doi.org/10.1101/gad.319889.118CrossRef

211.

Durko, L., Wlodarski, W., Stasikowska-Kanicka, O., Wagrowska-Danilewicz, M., Danilewicz, M., Hogendorf, P., & Malecka-Panas, E. (2017). Expression and clinical significance of cancer stem cell markers CD24, CD44, and CD133 in pancreatic ductal adenocarcinoma and chronic pancreatitis. Disease Markers, 2017, 3276806. https://doi.org/10.1155/2017/3276806CrossRef

212.

Gzil, A., Zarębska, I., Bursiewicz, W., Antosik, P., Grzanka, D., & Szylberg, Ł. (2019). Markers of pancreatic cancer stem cells and their clinical and therapeutic implications. Molecular Biology Reports, 46(6), 6629–6645. https://doi.org/10.1007/s11033-019-05058-1CrossRef

213.

Mima, K., Okabe, H., Ishimoto, T., Hayashi, H., Nakagawa, S., Kuroki, H., & Baba, H. (2012). CD44s regulates the TGF-β-mediated mesenchymal phenotype and is associated with poor prognosis in patients with hepatocellular carcinoma. Cancer Research, 72(13), 3414–3423. https://doi.org/10.1158/0008-5472.CAN-12-0299CrossRef

214.

Ni, J., Cozzi, P. J., Hao, J. L., Beretov, J., Chang, L., Duan, W., & Li, Y. (2014). CD44 variant 6 is associated with prostate cancer metastasis and chemo-/radioresistance. The Prostate, 74(6), 602–617. https://doi.org/10.1002/pros.22775CrossRef

215.

Gholizadeh, M., Doustvandi, M. A., Mohammadnejad, F., Shadbad, M. A., Tajalli, H., Brunetti, O., & Baradaran, B. (2021). Photodynamic therapy with zinc phthalocyanine inhibits the stemness and development of colorectal cancer: Time to overcome the challenging barriers? Molecules (Basel, Switzerland), 26(22), 6877. https://doi.org/10.3390/molecules26226877CrossRef

216.

Yu, C.-H., & Yu, C.-C. (2014). Photodynamic therapy with 5-aminolevulinic acid (ALA) impairs tumor initiating and chemo-resistance property in head and neck cancer-derived cancer stem cells. PLoS ONE, 9(1), e87129. https://doi.org/10.1371/journal.pone.0087129CrossRef

217.

Fang, C.-Y., Chen, P.-Y., Ho, D.C.-Y., Tsai, L.-L., Hsieh, P.-L., Lu, M.-Y., & Yu, C.-H. (2018). miR-145 mediates the anti-cancer stemness effect of photodynamic therapy with 5-aminolevulinic acid (ALA) in oral cancer cells. Journal of the Formosan Medical Association = Taiwan Yi Zhi, 117(8), 738–742. https://doi.org/10.1016/j.jfma.2018.05.018CrossRef

218.

Li, B., Chu, X., Gao, M., & Li, W. (2010). Apoptotic mechanism of MCF-7 breast cells in vivo and in vitro induced by photodynamic therapy with C-phycocyanin. Acta Biochimica Et Biophysica Sinica, 42(1), 80–89. https://doi.org/10.1093/abbs/gmp104CrossRef

219.

Gaio, E., Conte, C., Esposito, D., Reddi, E., Quaglia, F., & Moret, F. (2020). CD44 targeting mediated by polymeric nanoparticles and combination of chlorine TPCS2a-PDT and docetaxel-chemotherapy for efficient killing of breast differentiated and stem cancer cells in vitro. Cancers, 12(2), E278. https://doi.org/10.3390/cancers12020278CrossRef

220.

Wang, X., Ouyang, X., Chen, J., Hu, Y., Sun, X., & Yu, Z. (2019). Nanoparticulate photosensitizer decorated with hyaluronic acid for photodynamic/photothermal cancer targeting therapy. Nanomedicine (London, England), 14(2), 151–167. https://doi.org/10.2217/nnm-2018-0204CrossRef

221.

Ding, Y., Yang, R., Yu, W., Hu, C., Zhang, Z., Liu, D., & Chen, D. (2021). Chitosan oligosaccharide decorated liposomes combined with TH302 for photodynamic therapy in triple negative breast cancer. Journal of Nanobiotechnology, 19(1), 147. https://doi.org/10.1186/s12951-021-00891-8CrossRef

222.

Feng, Q., Zhang, Y., Zhang, W., Shan, X., Yuan, Y., Zhang, H., & Zhang, Z. (2016). Tumor-targeted and multi-stimuli responsive drug delivery system for near-infrared light induced chemo-phototherapy and photoacoustic tomography. Acta biomaterialia, 38, 129–142. https://doi.org/10.1016/j.actbio.2016.04.024CrossRef

223.

Jamora, C., & Fuchs, E. (2002). Intercellular adhesion, signalling and the cytoskeleton. Nature Cell Biology, 4(4), E101-108. https://doi.org/10.1038/ncb0402-e101CrossRef

224.

Mitra, S. K., Hanson, D. A., & Schlaepfer, D. D. (2005). Focal adhesion kinase: In command and control of cell motility. Nature Reviews. Molecular Cell Biology, 6(1), 56–68. https://doi.org/10.1038/nrm1549CrossRef

225.

Burridge, K., & Chrzanowska-Wodnicka, M. (1996). Focal adhesions, contractility, and signaling. Annual Review of Cell and Developmental Biology, 12, 463–518. https://doi.org/10.1146/annurev.cellbio.12.1.463CrossRef

226.

Zachary, I. (1997). Focal adhesion kinase. The International Journal of Biochemistry & Cell Biology, 29(7), 929–934. https://doi.org/10.1016/s1357-2725(97)00008-3CrossRef

227.

Villanueva, A., Juarranz, A., Diaz, V., Gomez, J., & Cañete, M. (1992). Photodynamic effects of a cationic mesosubstituted porphyrin in cell cultures. Anti-Cancer Drug Design, 7(4), 297–303.

228.

Juarranz, A., Espada, J., Stockert, J. C., Villanueva, A., Polo, S., Domínguez, V., & Cañete, M. (2001). Photodamage induced by zinc(II)-phthalocyanine to microtubules, actin, alpha-actinin and keratin of HeLa cells. Photochemistry and Photobiology, 73(3), 283–289. https://doi.org/10.1562/0031-8655(2001)073%3c0283:pibzip%3e2.0.co;2CrossRef

229.

Canete, M., Villanueva, A., Dominguez, V., Polo, S., Juarranz, A., & Stockert, J. C. (1998). Meso-tetraphenylporphyrin: Photosensitizing properties and cytotoxic effects on cultured tumor cells. International Journal of Oncology, 13(3), 497–504. https://doi.org/10.3892/ijo.13.3.497CrossRef

230.

Tsai, J.-C., Wu, C.-L., Chien, H.-F., & Chen, C.-T. (2005). Reorganization of cytoskeleton induced by 5-aminolevulinic acid-mediated photodynamic therapy and its correlation with mitochondrial dysfunction. Lasers in Surgery and Medicine, 36(5), 398–408. https://doi.org/10.1002/lsm.20179CrossRef

231.

Hall, J. E., Fu, W., & Schaller, M. D. (2011). Focal adhesion kinase: Exploring Fak structure to gain insight into function. International Review of Cell and Molecular Biology, 288, 185–225. https://doi.org/10.1016/B978-0-12-386041-5.00005-4CrossRef

232.

Sonoda, Y., Watanabe, S., Matsumoto, Y., Aizu-Yokota, E., & Kasahara, T. (1999). FAK is the upstream signal protein of the phosphatidylinositol 3-kinase-Akt survival pathway in hydrogen peroxide-induced apoptosis of a human glioblastoma cell line. The Journal of Biological Chemistry, 274(15), 10566–10570. https://doi.org/10.1074/jbc.274.15.10566CrossRef

233.

Sulzmaier, F. J., Jean, C., & Schlaepfer, D. D. (2014). FAK in cancer: Mechanistic findings and clinical applications. Nature Reviews. Cancer, 14(9), 598–610. https://doi.org/10.1038/nrc3792CrossRef

234.

Kato, A., Kato, K., Miyazawa, H., Kobayashi, H., Noguchi, N., & Kawashiri, S. (2020). Focal adhesion kinase (FAK) overexpression and phosphorylation in oral squamous cell carcinoma and their clinicopathological significance. Pathology oncology research: POR, 26(3), 1659–1667. https://doi.org/10.1007/s12253-019-00732-yCrossRef

235.

Hecker, T. P., Ding, Q., Rege, T. A., Hanks, S. K., & Gladson, C. L. (2004). Overexpression of FAK promotes Ras activity through the formation of a FAK/p120RasGAP complex in malignant astrocytoma cells. Oncogene, 23(22), 3962–3971. https://doi.org/10.1038/sj.onc.1207541CrossRef

236.

Golubovskaya, V. M., Conway-Dorsey, K., Edmiston, S. N., Tse, C.-K., Lark, A. A., Livasy, C. A., & Cance, W. G. (2009). FAK overexpression and p53 mutations are highly correlated in human breast cancer. International Journal of Cancer, 125(7), 1735–1738. https://doi.org/10.1002/ijc.24486CrossRef

237.

Zhuang, K., Guo, H., Tang, H., Yan, Y., Yang, Z., & Wang, Y. (2020). Suppression of FAK by nexrutine inhibits gastric cancer progression. Life Sciences, 257, 118100. https://doi.org/10.1016/j.lfs.2020.118100CrossRef

238.

Thakur, R., Trivedi, R., Rastogi, N., Singh, M., & Mishra, D. P. (2015). Inhibition of STAT3, FAK and Src mediated signaling reduces cancer stem cell load, tumorigenic potential and metastasis in breast cancer. Scientific Reports, 5, 10194. https://doi.org/10.1038/srep10194CrossRef

239.

Casas, A., Sanz-Rodriguez, F., Di Venosa, G., Rodriguez, L., Mamone, L., Blázquez, A., & Juarranz, A. (2008). Disorganisation of cytoskeleton in cells resistant to photodynamic treatment with decreased metastatic phenotype. Cancer Letters, 270(1), 56–65. https://doi.org/10.1016/j.canlet.2008.04.029CrossRef

240.

Dabrowska, A., Goś, M., & Janik, P. (2005). “Bystander effect” induced by photodynamically or heat-injured ovarian carcinoma cells (OVP10) in vitro. Medical Science Monitor: International Medical Journal of Experimental and Clinical Research, 11(9), BR316-324.

241.

Acedo, P., Stockert, J. C., Cañete, M., & Villanueva, A. (2014). Two combined photosensitizers: A goal for more effective photodynamic therapy of cancer. Cell Death & Disease, 5, e1122. https://doi.org/10.1038/cddis.2014.77CrossRef

242.

Katoh, K. (2017). Activation of Rho-kinase and focal adhesion kinase regulates the organization of stress fibers and focal adhesions in the central part of fibroblasts. PeerJ, 5, e4063. https://doi.org/10.7717/peerj.4063CrossRef

243.

Ren, X. D., Kiosses, W. B., Sieg, D. J., Otey, C. A., Schlaepfer, D. D., & Schwartz, M. A. (2000). Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover. Journal of Cell Science, 113(Pt 20), 3673–3678. https://doi.org/10.1242/jcs.113.20.3673CrossRef

244.

Roskoski, R. (2004). Src protein-tyrosine kinase structure and regulation. Biochemical and Biophysical Research Communications, 324(4), 1155–1164. https://doi.org/10.1016/j.bbrc.2004.09.171CrossRef

245.

Roskoski, R. (2015). Src protein-tyrosine kinase structure, mechanism, and small molecule inhibitors. Pharmacological Research, 94, 9–25. https://doi.org/10.1016/j.phrs.2015.01.003CrossRef

246.

Caner, A., Asik, E., & Ozpolat, B. (2021). SRC signaling in cancer and tumor microenvironment. Advances in Experimental Medicine and Biology, 1270, 57–71. https://doi.org/10.1007/978-3-030-47189-7_4CrossRef

247.

Mitra, S. K., & Schlaepfer, D. D. (2006). Integrin-regulated FAK-Src signaling in normal and cancer cells. Current Opinion in Cell Biology, 18(5), 516–523. https://doi.org/10.1016/j.ceb.2006.08.011CrossRef

248.

Yang, T.-H., Chen, C.-T., Wang, C.-P., & Lou, P.-J. (2007). Photodynamic therapy suppresses the migration and invasion of head and neck cancer cells in vitro. Oral Oncology, 43(4), 358–365. https://doi.org/10.1016/j.oraloncology.2006.04.007CrossRef

249.

Woźniak, M., Hotowy, K., Czapińska, E., Duś-Szachniewicz, K., Szczuka, I., Gamian, E., & Ziółkowski, P. (2014). Early induction of stress-associated Src activator/Homo sapiens chromosome 9 open reading frame 10 protein following photodynamic therapy. Photodiagnosis and Photodynamic Therapy, 11(1), 27–33. https://doi.org/10.1016/j.pdpdt.2013.11.002CrossRef

250.

Blázquez-Castro, A., Carrasco, E., Calvo, M. I., Jaén, P., Stockert, J. C., Juarranz, A., & Espada, J. (2012). Protoporphyrin IX-dependent photodynamic production of endogenous ROS stimulates cell proliferation. European Journal of Cell Biology, 91(3), 216–223. https://doi.org/10.1016/j.ejcb.2011.12.001CrossRef

251.

Xue, L. Y., He, J., & Oleinick, N. L. (1997). Rapid tyrosine phosphorylation of HS1 in the response of mouse lymphoma L5178Y-R cells to photodynamic treatment sensitized by the phthalocyanine Pc 4. Photochemistry and Photobiology, 66(1), 105–113. https://doi.org/10.1111/j.1751-1097.1997.tb03145.xCrossRef

252.

Giannoni, E., Taddei, M. L., & Chiarugi, P. (2010). Src redox regulation: Again in the front line. Free Radical Biology & Medicine, 49(4), 516–527. https://doi.org/10.1016/j.freeradbiomed.2010.04.025CrossRef

253.

Ridley, A. J., & Hall, A. (1992). The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell, 70(3), 389–399. https://doi.org/10.1016/0092-8674(92)90163-7CrossRef

254.

Sahai, E., & Marshall, C. J. (2002). RHO-GTPases and cancer. Nature Reviews. Cancer, 2(2), 133–142. https://doi.org/10.1038/nrc725CrossRef

255.

Sadok, A., & Marshall, C. J. (2014). Rho GTPases: Masters of cell migration. Small GTPases, 5, e29710. https://doi.org/10.4161/sgtp.29710CrossRef

256.

Phuyal, S., & Farhan, H. (2019). Multifaceted Rho GTPase signaling at the endomembranes. Frontiers in Cell and Developmental Biology, 7, 127. https://doi.org/10.3389/fcell.2019.00127CrossRef

257.

Tomar, A., & Schlaepfer, D. D. (2009). Focal adhesion kinase: Switching between GAPs and GEFs in the regulation of cell motility. Current Opinion in Cell Biology, 21(5), 676–683. https://doi.org/10.1016/j.ceb.2009.05.006CrossRef

258.

Jaffe, A. B., & Hall, A. (2005). Rho GTPases: Biochemistry and biology. Annual Review of Cell and Developmental Biology, 21, 247–269. https://doi.org/10.1146/annurev.cellbio.21.020604.150721CrossRef

259.

Chen, B.-H., Tzen, J. T. C., Bresnick, A. R., & Chen, H.-C. (2002). Roles of Rho-associated kinase and myosin light chain kinase in morphological and migratory defects of focal adhesion kinase-null cells. The Journal of Biological Chemistry, 277(37), 33857–33863. https://doi.org/10.1074/jbc.M204429200CrossRef

260.

Haga, R. B., & Ridley, A. J. (2016). Rho GTPases: Regulation and roles in cancer cell biology. Small GTPases, 7(4), 207–221. https://doi.org/10.1080/21541248.2016.1232583CrossRef

261.

Amano, M., Chihara, K., Nakamura, N., Kaneko, T., Matsuura, Y., & Kaibuchi, K. (1999). The COOH terminus of Rho-kinase negatively regulates rho-kinase activity. The Journal of Biological Chemistry, 274(45), 32418–32424. https://doi.org/10.1074/jbc.274.45.32418CrossRef

262.

Kim, S., Kim, S. A., Han, J., & Kim, I.-S. (2021). Rho-kinase as a target for cancer therapy and its immunotherapeutic potential. International Journal of Molecular Sciences, 22(23), 12916. https://doi.org/10.3390/ijms222312916CrossRef

263.

Zhang, J., He, X., Ma, Y., Liu, Y., Shi, H., Guo, W., & Liu, L. (2015). Overexpression of ROCK1 and ROCK2 inhibits human laryngeal squamous cell carcinoma. International Journal of Clinical and Experimental Pathology, 8(1), 244–251.

264.

Wu, H., Chen, Y., Li, B., Li, C., Guo, J., You, J., & Xu, C. (2021). Targeting ROCK1/2 blocks cell division and induces mitotic catastrophe in hepatocellular carcinoma. Biochemical Pharmacology, 184, 114353. https://doi.org/10.1016/j.bcp.2020.114353CrossRef

265.

Matsuoka, T., & Yashiro, M. (2014). Rho/ROCK signaling in motility and metastasis of gastric cancer. World Journal of Gastroenterology, 20(38), 13756–13766. https://doi.org/10.3748/wjg.v20.i38.13756CrossRef

266.

Mei, Y., Wu, Y., Ma, L., Zhang, H., Li, L., & Wang, F. (2021). Overexpression of ROCK1 promotes cancer cell proliferation and is associated with poor prognosis in human urothelial bladder cancer. Mammalian Genome: Official Journal of the International Mammalian Genome Society, 32(6), 466–475. https://doi.org/10.1007/s00335-021-09896-yCrossRef

267.

Wang, Z., Li, T.-E., Chen, M., Pan, J.-J., & Shen, K.-W. (2020). miR-106b-5p contributes to the lung metastasis of breast cancer via targeting CNN1 and regulating Rho/ROCK1 pathway. Aging, 12(2), 1867–1887. https://doi.org/10.18632/aging.102719CrossRef

268.

Xin, T., Lv, W., Liu, D., Jing, Y., & Hu, F. (2020). ROCK1 knockdown inhibits non-small-cell lung cancer progression by activating the LATS2-JNK signaling pathway. Aging, 12(12), 12160–12174. https://doi.org/10.18632/aging.103386CrossRef

269.

Peng, L., Sang, H., Wei, S., Li, Y., Jin, D., Zhu, X., & Zhang, G. (2020). circCUL2 regulates gastric cancer malignant transformation and cisplatin resistance by modulating autophagy activation via miR-142-3p/ROCK2. Molecular Cancer, 19(1), 156. https://doi.org/10.1186/s12943-020-01270-xCrossRef

270.

Gao, W., Zhang, S., Guorong, L., Liu, Q., Zhu, A., Gui, F., & Hong, Z. (2022). Nc886 promotes renal cancer cell drug-resistance by enhancing EMT through Rock2 phosphorylation-mediated β-catenin nuclear translocation. Cell Cycle (Georgetown, Tex.), 21(4), 340–351. https://doi.org/10.1080/15384101.2021.2020431CrossRef

271.

Wufuer, R., Ma, H.-X., Luo, M.-Y., Xu, K.-Y., & Kang, L. (2021). Downregulation of Rac1/PAK1/LIMK1/cofilin signaling pathway in colon cancer SW620 cells treated with Chlorin e6 photodynamic therapy. Photodiagnosis and Photodynamic Therapy, 33, 102143. https://doi.org/10.1016/j.pdpdt.2020.102143CrossRef

272.

Zhan, F., He, T., Chen, Z., Zuo, Q., Wang, Y., Li, Q., & Ou, Y. (2021). RhoA enhances osteosarcoma resistance to MPPa-PDT via the Hippo/YAP signaling pathway. Cell & Bioscience, 11(1), 179. https://doi.org/10.1186/s13578-021-00690-6CrossRef

273.

Ota, H., Matsumura, M., Miki, N., & Minamitami, H. (2009). Photochemically induced increase in endothelial permeability regulated by RhoA activation. Photochemical & Photobiological Sciences: Official Journal of the European Photochemistry Association and the European Society for Photobiology, 8(10), 1401–1407. https://doi.org/10.1039/b906028fCrossRef

274.

Cavin, S., Riedel, T., Rosskopfova, P., Gonzalez, M., Baldini, G., Zellweger, M., & Perentes, J. Y. (2019). Vascular-targeted low dose photodynamic therapy stabilizes tumor vessels by modulating pericyte contractility. Lasers in Surgery and Medicine, 51(6), 550–561. https://doi.org/10.1002/lsm.23069CrossRef

275.

Suzuki, T., Tanaka, M., Sasaki, M., Ichikawa, H., Nishie, H., & Kataoka, H. (2020). Vascular shutdown by photodynamic therapy using talaporfin sodium. Cancers, 12(9), E2369. https://doi.org/10.3390/cancers12092369CrossRef

276.

Kim, W., & Jho, E.-H. (2018). The history and regulatory mechanism of the Hippo pathway. BMB reports, 51(3), 106–118. https://doi.org/10.5483/bmbrep.2018.51.3.022CrossRef

277.

Zanconato, F., Forcato, M., Battilana, G., Azzolin, L., Quaranta, E., Bodega, B., & Piccolo, S. (2015). Genome-wide association between YAP/TAZ/TEAD and AP-1 at enhancers drives oncogenic growth. Nature Cell Biology, 17(9), 1218–1227. https://doi.org/10.1038/ncb3216CrossRef

278.

Zanconato, F., Cordenonsi, M., & Piccolo, S. (2016). YAP/TAZ at the roots of cancer. Cancer Cell, 29(6), 783–803. https://doi.org/10.1016/j.ccell.2016.05.005CrossRef

279.

Hua, G., Lv, X., He, C., Remmenga, S. W., Rodabough, K. J., Dong, J., & Wang, C. (2016). YAP induces high-grade serous carcinoma in fallopian tube secretory epithelial cells. Oncogene, 35(17), 2247–2265. https://doi.org/10.1038/onc.2015.288CrossRef

280.

Zhang, L., Yang, S., Chen, X., Stauffer, S., Yu, F., Lele, S. M., & Dong, J. (2015). The hippo pathway effector YAP regulates motility, invasion, and castration-resistant growth of prostate cancer cells. Molecular and Cellular Biology, 35(8), 1350–1362. https://doi.org/10.1128/MCB.00102-15CrossRef

281.

Kapoor, A., Yao, W., Ying, H., Hua, S., Liewen, A., Wang, Q., & DePinho, R. A. (2014). Yap1 activation enables bypass of oncogenic Kras addiction in pancreatic cancer. Cell, 158(1), 185–197. https://doi.org/10.1016/j.cell.2014.06.003CrossRef

282.

Kandoussi, I., Lakhlili, W., Taoufik, J., & Ibrahimi, A. (2017). Docking analysis of verteporfin with YAP WW domain. Bioinformation, 13(7), 237–240. https://doi.org/10.6026/97320630013237CrossRef

283.

Wang, C., Zhu, X., Feng, W., Yu, Y., Jeong, K., Guo, W., & Mills, G. B. (2016). Verteporfin inhibits YAP function through up-regulating 14-3-3σ sequestering YAP in the cytoplasm. American Journal of Cancer Research, 6(1), 27–37.

284.

Gibault, F., Corvaisier, M., Bailly, F., Huet, G., Melnyk, P., & Cotelle, P. (2016). Non-photoinduced biological properties of verteporfin. Current Medicinal Chemistry, 23(11), 1171–1184. https://doi.org/10.2174/0929867323666160316125048CrossRef

285.

Wei, H., Wang, F., Wang, Y., Li, T., Xiu, P., Zhong, J., & Li, J. (2017). Verteporfin suppresses cell survival, angiogenesis and vasculogenic mimicry of pancreatic ductal adenocarcinoma via disrupting the YAP-TEAD complex. Cancer Science, 108(3), 478–487. https://doi.org/10.1111/cas.13138CrossRef

286.

Al-Moujahed, A., Brodowska, K., Stryjewski, T. P., Efstathiou, N. E., Vasilikos, I., Cichy, J., & Vavvas, D. G. (2017). Verteporfin inhibits growth of human glioma in vitro without light activation. Scientific Reports, 7(1), 7602. https://doi.org/10.1038/s41598-017-07632-8CrossRef

287.

Feng, J., Gou, J., Jia, J., Yi, T., Cui, T., & Li, Z. (2016). Verteporfin, a suppressor of YAP-TEAD complex, presents promising antitumor properties on ovarian cancer. OncoTargets and Therapy, 9, 5371–5381. https://doi.org/10.2147/OTT.S109979CrossRef

288.

Chen, M., Zhong, L., Yao, S.-F., Zhao, Y., Liu, L., Li, L.-W., & Liu, B.-Z. (2017). Verteporfin inhibits cell proliferation and induces apoptosis in human leukemia NB4 cells without light activation. International Journal of Medical Sciences, 14(10), 1031–1039. https://doi.org/10.7150/ijms.19682CrossRef

289.

Brodowska, K., Al-Moujahed, A., Marmalidou, A., Meyer Zu Horste, M., Cichy, J., Miller, J. W., & Vavvas, D. G. (2014). The clinically used photosensitizer verteporfin (VP) inhibits YAP-TEAD and human retinoblastoma cell growth in vitro without light activation. Experimental Eye Research, 124, 67–73. https://doi.org/10.1016/j.exer.2014.04.011CrossRef

290.

Rytlewski, J. D., Scalora, N., Garcia, K., Tanas, M., Toor, F., Miller, B., & Monga, V. (2021). Photodynamic therapy using hippo pathway inhibitor verteporfin: A potential dual mechanistic approach in treatment of soft tissue sarcomas. Cancers, 13(4), 675. https://doi.org/10.3390/cancers13040675CrossRef

291.

Noorolyai, S., Shajari, N., Baghbani, E., Sadreddini, S., & Baradaran, B. (2019). The relation between PI3K/AKT signalling pathway and cancer. Gene, 698, 120–128. https://doi.org/10.1016/j.gene.2019.02.076CrossRef

292.

Fresno Vara, J. A., Casado, E., de Castro, J., Cejas, P., Belda-Iniesta, C., & González-Barón, M. (2004). PI3K/Akt signalling pathway and cancer. Cancer Treatment Reviews, 30(2), 193–204. https://doi.org/10.1016/j.ctrv.2003.07.007CrossRef

293.

Porta, C., Paglino, C., & Mosca, A. (2014). Targeting PI3K/Akt/mTOR signaling in cancer. Frontiers in Oncology, 4, 64. https://doi.org/10.3389/fonc.2014.00064CrossRef

294.

Huang, L., Lin, H., Chen, Q., Yu, L., & Bai, D. (2019). MPPa-PDT suppresses breast tumor migration/invasion by inhibiting Akt-NF-κB-dependent MMP-9 expression via ROS. BMC Cancer, 19(1), 1159. https://doi.org/10.1186/s12885-019-6374-xCrossRef

295.

Zheng, X., Pan, D., Chen, X., Wu, L., Chen, M., Wang, W., & Luo, K. (2021). Self-stabilized supramolecular assemblies constructed from PEGylated dendritic peptide conjugate for augmenting tumor retention and therapy. Advanced Science (Weinheim Baden-Wurttemberg, Germany), 8(22), e2102741. https://doi.org/10.1002/advs.202102741CrossRef

296.

Zhang, Q., Li, Z., Li, Y., Shi, S., Zhou, S., Fu, Y., & Lu, L. (2015). Hypericin-photodynamic therapy induces human umbilical vein endothelial cell apoptosis. Scientific Reports, 5, 18398. https://doi.org/10.1038/srep18398CrossRef

297.

Chakrabarti, M., Banik, N. L., & Ray, S. K. (2013). Photofrin based photodynamic therapy and miR-99a transfection inhibited FGFR3 and PI3K/Akt signaling mechanisms to control growth of human glioblastoma in vitro and in vivo. PLoS ONE, 8(2), e55652. https://doi.org/10.1371/journal.pone.0055652CrossRef

298.

Zhang, X., Cai, L., He, J., Li, X., Li, L., Chen, X., & Lan, P. (2017). Influence and mechanism of 5-aminolevulinic acid-photodynamic therapy on the metastasis of esophageal carcinoma. Photodiagnosis and Photodynamic Therapy, 20, 78–85. https://doi.org/10.1016/j.pdpdt.2017.08.004CrossRef

299.

Li, Y., Wu, S., Zhang, J., Zhou, R., & Cai, X. (2020). Sulphur doped carbon dots enhance photodynamic therapy via PI3K/Akt signalling pathway. Cell Proliferation, 53(5), e12821. https://doi.org/10.1111/cpr.12821CrossRef

300.

Xie, J., Wang, S., Li, Z., Ao, C., Wang, J., Wang, L., & Zeng, K. (2019). 5-aminolevulinic acid photodynamic therapy reduces HPV viral load via autophagy and apoptosis by modulating Ras/Raf/MEK/ERK and PI3K/AKT pathways in HeLa cells. Journal of Photochemistry and Photobiology B, Biology, 194, 46–55. https://doi.org/10.1016/j.jphotobiol.2019.03.012CrossRef

301.

Xu, C., Wang, Q., Feng, X., & Bo, Y. (2014). Effect of evodiagenine mediates photocytotoxicity on human breast cancer cells MDA-MB-231 through inhibition of PI3K/AKT/mTOR and activation of p38 pathways. Fitoterapia, 99, 292–299. https://doi.org/10.1016/j.fitote.2014.10.010CrossRef

302.

Matsubara, A., Nakazawa, T., Noda, K., She, H., Connolly, E., Young, T. A., & Miller, J. W. (2007). Photodynamic therapy induces caspase-dependent apoptosis in rat CNV model. Investigative Ophthalmology & Visual Science, 48(10), 4741–4747. https://doi.org/10.1167/iovs.06-1534CrossRef

303.

An, Y.-W., Liu, H.-Q., Zhou, Z.-Q., Wang, J.-C., Jiang, G.-Y., Li, Z.-W., & Jin, H.-T. (2020). Sinoporphyrin sodium is a promising sensitizer for photodynamic and sonodynamic therapy in glioma. Oncology Reports, 44(4), 1596–1604. https://doi.org/10.3892/or.2020.7695CrossRef

304.

Fang, S., Wu, Y., Zhang, H., Zeng, Q., Wang, P., Zhang, L., & Wang, X. (2022). Molecular characterization of gene expression changes in murine cutaneous squamous cell carcinoma after 5-aminolevulinic acid photodynamic therapy. Photodiagnosis and Photodynamic Therapy, 39, 102907. https://doi.org/10.1016/j.pdpdt.2022.102907CrossRef

305.

Franklin, M. C., Cheung, J., Rudolph, M. J., Burshteyn, F., Cassidy, M., Gary, E., & Love, J. D. (2015). Structural genomics for drug design against the pathogen Coxiella burnetii. Proteins, 83(12), 2124–2136. https://doi.org/10.1002/prot.24841CrossRef

306.

Valli, F., García Vior, M. C., Roguin, L. P., & Marino, J. (2020). Crosstalk between oxidative stress-induced apoptotic and autophagic signaling pathways in Zn(II) phthalocyanine photodynamic therapy of melanoma. Free Radical Biology & Medicine, 152, 743–754. https://doi.org/10.1016/j.freeradbiomed.2020.01.018CrossRef

307.

Fahey, J. M., Korytowski, W., & Girotti, A. W. (2019). Upstream signaling events leading to elevated production of pro-survival nitric oxide in photodynamically-challenged glioblastoma cells. Free Radical Biology & Medicine, 137, 37–45. https://doi.org/10.1016/j.freeradbiomed.2019.04.013CrossRef

308.

Zheng, X., Jiang, F., Katakowski, M., Zhang, X., Jiang, H., Zhang, Z. G., & Chopp, M. (2008). Sensitization of cerebral tissue in nude mice with photodynamic therapy induces ADAM17/TACE and promotes glioma cell invasion. Cancer Letters, 265(2), 177–187. https://doi.org/10.1016/j.canlet.2008.02.023CrossRef

309.

McCubrey, J. A., Steelman, L. S., Chappell, W. H., Abrams, S. L., Wong, E. W. T., Chang, F., & Franklin, R. A. (2007). Roles of the Raf/MEK/ERK pathway in cell growth, malignant transformation and drug resistance. Biochimica Et Biophysica Acta, 1773(8), 1263–1284. https://doi.org/10.1016/j.bbamcr.2006.10.001CrossRef

310.

Matei, C., Tampa, M., Caruntu, C., Ion, R.-M., Georgescu, S.-R., Dumitrascu, G. R., & Neagu, M. (2014). Protein microarray for complex apoptosis monitoring of dysplastic oral keratinocytes in experimental photodynamic therapy. Biological Research, 47, 33. https://doi.org/10.1186/0717-6287-47-33CrossRef

311.

Chatterjee, S., Rhee, Y., Chung, P.-S., Ge, R.-F., & Ahn, J.-C. (2018). Sulforaphene enhances the efficacy of photodynamic therapy in anaplastic thyroid cancer through Ras/RAF/MEK/ERK pathway suppression. Journal of Photochemistry and Photobiology B, Biology, 179, 46–53. https://doi.org/10.1016/j.jphotobiol.2017.12.013CrossRef

312.

Mao, W., Sun, Y., Zhang, H., Cao, L., Wang, J., & He, P. (2016). A combined modality of carboplatin and photodynamic therapy suppresses epithelial-mesenchymal transition and matrix metalloproteinase-2 (MMP-2)/MMP-9 expression in HEp-2 human laryngeal cancer cells via ROS-mediated inhibition of MEK/ERK signalling pathway. Lasers in Medical Science, 31(8), 1697–1705. https://doi.org/10.1007/s10103-016-2040-6CrossRef

313.

Zhang, H., Shen, B., Swinarska, J. T., Li, W., Xiao, K., & He, P. (2014). 9-Hydroxypheophorbide α-mediated photodynamic therapy induces matrix metalloproteinase-2 (MMP-2) and MMP-9 down-regulation in Hep-2 cells via ROS-mediated suppression of the ERK pathway. Photodiagnosis and Photodynamic Therapy, 11(1), 55–62. https://doi.org/10.1016/j.pdpdt.2013.12.001CrossRef

314.

Ogbodu, R. O., Nitzsche, B., Ma, A., Atilla, D., Gürek, A. G., & Höpfner, M. (2020). Photodynamic therapy of hepatocellular carcinoma using tetra-triethyleneoxysulfonyl zinc phthalocyanine as photosensitizer. Journal of Photochemistry and Photobiology. B, Biology, 208, 111915. https://doi.org/10.1016/j.jphotobiol.2020.111915CrossRef

315.

Gu, X., Qiu, Y., Lin, M., Cui, K., Chen, G., Chen, Y., & Xiao, Z. (2019). CuS Nanoparticles as a photodynamic nanoswitch for abrogating bypass signaling to overcome gefitinib resistance. Nano Letters, 19(5), 3344–3352. https://doi.org/10.1021/acs.nanolett.9b01065CrossRef

316.

Weyergang, A., Selbo, P. K., & Berg, K. (2013). Sustained ERK [corrected] inhibition by EGFR targeting therapies is a predictive factor for synergistic cytotoxicity with PDT as neoadjuvant therapy. Biochimica Et Biophysica Acta, 1830(3), 2659–2670. https://doi.org/10.1016/j.bbagen.2012.11.010CrossRef

317.

Chan, W.-H. (2011). Photodynamic treatment induces an apoptotic pathway involving calcium, nitric oxide, p53, p21-activated kinase 2, and c-Jun N-terminal kinase and inactivates survival signal in human umbilical vein endothelial cells. International Journal of Molecular Sciences, 12(2), 1041–1059. https://doi.org/10.3390/ijms12021041CrossRef

318.

Ahn, M. Y., Yoon, H.-E., Kwon, S.-M., Lee, J., Min, S.-K., Kim, Y.-C., & Yoon, J.-H. (2013). Synthesized pheophorbide a-mediated photodynamic therapy induced apoptosis and autophagy in human oral squamous carcinoma cells. Journal of Oral Pathology & Medicine: Official Publication of the International Association of Oral Pathologists and the American Academy of Oral Pathology, 42(1), 17–25. https://doi.org/10.1111/j.1600-0714.2012.01187.xCrossRef

319.

Bui-Xuan, N.-H., Tang, P.M.-K., Wong, C.-K., & Fung, K.-P. (2010). Photo-activated pheophorbide-a, an active component of Scutellaria barbata, enhances apoptosis via the suppression of ERK-mediated autophagy in the estrogen receptor-negative human breast adenocarcinoma cells MDA-MB-231. Journal of Ethnopharmacology, 131(1), 95–103. https://doi.org/10.1016/j.jep.2010.06.007CrossRef

320.

Bui-Xuan, N.-H., Tang, P.M.-K., Wong, C.-K., Chan, J.Y.-W., Cheung, K. K. Y., Jiang, J. L., & Fung, K.-P. (2011). Pheophorbide a: A photosensitizer with immunostimulating activities on mouse macrophage RAW 264.7 cells in the absence of irradiation. Cellular Immunology, 269(1), 60–67. https://doi.org/10.1016/j.cellimm.2011.02.010CrossRef

321.

Lamberti, M. J., Pansa, M. F., Vera, R. E., Fernández-Zapico, M. E., Rumie Vittar, N. B., & Rivarola, V. A. (2017). Transcriptional activation of HIF-1 by a ROS-ERK axis underlies the resistance to photodynamic therapy. PLoS ONE, 12(5), e0177801. https://doi.org/10.1371/journal.pone.0177801CrossRef

322.

Le Clainche, T., Carigga Gutierrez, N. M., Pujol-Solé, N., Coll, J.-L., & Broekgaarden, M. (2022). Optimizing the pharmacological and optical dosimetry for photodynamic therapy with methylene blue and nanoliposomal benzoporphyrin on pancreatic cancer spheroids. Onco, 2(1), 19–33. https://doi.org/10.3390/onco2010002CrossRef

323.

Broekgaarden, M., Anbil, S., Bulin, A.-L., Obaid, G., Mai, Z., Baglo, Y., & Hasan, T. (2019). Modulation of redox metabolism negates cancer-associated fibroblasts-induced treatment resistance in a heterotypic 3D culture platform of pancreatic cancer. Biomaterials, 222, 119421. https://doi.org/10.1016/j.biomaterials.2019.119421CrossRef

324.

Broekgaarden, M., Alkhateeb, A., Bano, S., Bulin, A.-L., Obaid, G., Rizvi, I., & Hasan, T. (2020). Cabozantinib inhibits photodynamic therapy-induced auto- and paracrine MET signaling in heterotypic pancreatic microtumors. Cancers, 12(6), E1401. https://doi.org/10.3390/cancers12061401CrossRef

325.

Ge, X., Liu, J., Shi, Z., Jing, L., Yu, N., Zhang, X., & Li, P. A. (2016). Inhibition of MAPK signaling pathways enhances cell death induced by 5-Aminolevulinic acid-photodynamic therapy in skin squamous carcinoma cells. European journal of dermatology: EJD, 26(2), 164–172. https://doi.org/10.1684/ejd.2015.2725CrossRef

326.

Zheng, J.-H., Shi, D., Zhao, Y., & Chen, Z.-L. (2006). Role of calcium signal in apoptosis and protective mechanism of colon cancer cell line SW480 in response to 5-aminolevulinic acid-photodynamic therapy. Ai Zheng = Aizheng = Chinese Journal of Cancer, 25(6), 683–688.

327.

Chelakkot, V. S., Som, J., Yoshioka, E., Rice, C. P., Rutihinda, S. G., & Hirasawa, K. (2019). Systemic MEK inhibition enhances the efficacy of 5-aminolevulinic acid-photodynamic therapy. British Journal of Cancer, 121(9), 758–767. https://doi.org/10.1038/s41416-019-0586-3CrossRef

328.

Chelakkot, V. S., Liu, K., Yoshioka, E., Saha, S., Xu, D., Licursi, M., & Hirasawa, K. (2020). MEK reduces cancer-specific PpIX accumulation through the RSK-ABCB1 and HIF-1α-FECH axes. Scientific Reports, 10(1), 22124. https://doi.org/10.1038/s41598-020-79144-xCrossRef

329.

Yoshioka, E., Chelakkot, V. S., Licursi, M., Rutihinda, S. G., Som, J., Derwish, L., & Hirasawa, K. (2018). Enhancement of cancer-specific protoporphyrin IX fluorescence by targeting oncogenic Ras/MEK pathway. Theranostics, 8(8), 2134–2146. https://doi.org/10.7150/thno.22641CrossRef

330.

Juarez, A. V., Sosa, L. D. V., De Paul, A. L., Costa, A. P., Farina, M., Leal, R. B., & Pons, P. (2015). Riboflavin acetate induces apoptosis in squamous carcinoma cells after photodynamic therapy. Journal of Photochemistry and Photobiology. B, Biology, 153, 445–454. https://doi.org/10.1016/j.jphotobiol.2015.10.030CrossRef

331.

Chen, J., Lovell, J. F., Lo, P.-C., Stefflova, K., Niedre, M., Wilson, B. C., & Zheng, G. (2008). A tumor mRNA-triggered photodynamic molecular beacon based on oligonucleotide hairpin control of singlet oxygen production. Photochemical & Photobiological Sciences: Official Journal of the European Photochemistry Association and the European Society for Photobiology, 7(7), 775–781. https://doi.org/10.1039/b800653aCrossRef

332.

Uzdensky, A., Kristiansen, B., Moan, J., & Juzeniene, A. (2012). Dynamics of signaling, cytoskeleton and cell cycle regulation proteins in glioblastoma cells after sub-lethal photodynamic treatment: Antibody microarray study. Biochimica Et Biophysica Acta, 1820(7), 795–803. https://doi.org/10.1016/j.bbagen.2012.03.008CrossRef

333.

De Luca, A., Maiello, M. R., D’Alessio, A., Pergameno, M., & Normanno, N. (2012). The RAS/RAF/MEK/ERK and the PI3K/AKT signalling pathways: Role in cancer pathogenesis and implications for therapeutic approaches. Expert Opinion on Therapeutic Targets, 16(Suppl 2), S17-27. https://doi.org/10.1517/14728222.2011.639361CrossRef

334.

Ullah, R., Yin, Q., Snell, A. H., & Wan, L. (2021). RAF-MEK-ERK pathway in cancer evolution and treatment. Seminars in Cancer Biology, S1044–579X(21), 00138–3. https://doi.org/10.1016/j.semcancer.2021.05.010CrossRef

335.

Steelman, L. S., Franklin, R. A., Abrams, S. L., Chappell, W., Kempf, C. R., Bäsecke, J., & McCubrey, J. A. (2011). Roles of the Ras/Raf/MEK/ERK pathway in leukemia therapy. Leukemia, 25(7), 1080–1094. https://doi.org/10.1038/leu.2011.66CrossRef

336.

Steelman, L. S., Chappell, W. H., Abrams, S. L., Kempf, R. C., Long, J., Laidler, P., & McCubrey, J. A. (2011). Roles of the Raf/MEK/ERK and PI3K/PTEN/Akt/mTOR pathways in controlling growth and sensitivity to therapy-implications for cancer and aging. Aging, 3(3), 192–222. https://doi.org/10.18632/aging.100296CrossRef

337.

Wagner, E. F., & Nebreda, A. R. (2009). Signal integration by JNK and p38 MAPK pathways in cancer development. Nature Reviews. Cancer, 9(8), 537–549. https://doi.org/10.1038/nrc2694CrossRef

338.

Wu, Q., Wu, W., Fu, B., Shi, L., Wang, X., & Kuca, K. (2019). JNK signaling in cancer cell survival. Medicinal Research Reviews, 39(6), 2082–2104. https://doi.org/10.1002/med.21574CrossRef

339.

Klotz, L. O., Fritsch, C., Briviba, K., Tsacmacidis, N., Schliess, F., & Sies, H. (1998). Activation of JNK and p38 but not ERK MAP kinases in human skin cells by 5-aminolevulinate-photodynamic therapy. Cancer Research, 58(19), 4297–4300.

340.

Assefa, Z., Vantieghem, A., Declercq, W., Vandenabeele, P., Vandenheede, J. R., Merlevede, W., & Agostinis, P. (1999). The activation of the c-Jun N-terminal kinase and p38 mitogen-activated protein kinase signaling pathways protects HeLa cells from apoptosis following photodynamic therapy with hypericin. The Journal of Biological Chemistry, 274(13), 8788–8796. https://doi.org/10.1074/jbc.274.13.8788CrossRef

341.

Hsieh, Y.-J., Wu, C.-C., Chang, C.-J., & Yu, J.-S. (2003). Subcellular localization of photofrin determines the death phenotype of human epidermoid carcinoma A431 cells triggered by photodynamic therapy: When plasma membranes are the main targets. Journal of Cellular Physiology, 194(3), 363–375. https://doi.org/10.1002/jcp.10273CrossRef

342.

Tang, P.M.-K., Zhang, D.-M., Xuan, N.-H.B., Tsui, S.K.-W., Waye, M.M.-Y., Kong, S.-K., & Fung, K.-P. (2009). Photodynamic therapy inhibits P-glycoprotein mediated multidrug resistance via JNK activation in human hepatocellular carcinoma using the photosensitizer pheophorbide a. Molecular Cancer, 8, 56. https://doi.org/10.1186/1476-4598-8-56CrossRef

343.

Ferrario, A., Luna, M., Rucker, N., Wong, S., & Gomer, C. J. (2011). Pro-apoptotic and anti-inflammatory properties of the green tea constituent epigallocatechin gallate increase photodynamic therapy responsiveness. Lasers in Surgery and Medicine, 43(7), 644–650. https://doi.org/10.1002/lsm.21081CrossRef

344.

Xu, Y., Wang, D., Zhuang, Z., Jin, K., Zheng, L., Yang, Q., & Guo, K. (2015). Hypericin-mediated photodynamic therapy induces apoptosis in K562 human leukemia cells through JNK pathway modulation. Molecular Medicine Reports, 12(5), 6475–6482. https://doi.org/10.3892/mmr.2015.4258CrossRef

345.

Tu, P., Huang, Q., Ou, Y., Du, X., Li, K., Tao, Y., & Yin, H. (2016). Aloe-emodin-mediated photodynamic therapy induces autophagy and apoptosis in human osteosarcoma cell line MG-63 through the ROS/JNK signaling pathway. Oncology Reports, 35(6), 3209–3215. https://doi.org/10.3892/or.2016.4703CrossRef

346.

Salmerón, M. L., Quintana-Aguiar, J., De La Rosa, J. V., López-Blanco, F., Castrillo, A., Gallardo, G., & Tabraue, C. (2018). Phenalenone-photodynamic therapy induces apoptosis on human tumor cells mediated by caspase-8 and p38-MAPK activation. Molecular Carcinogenesis, 57(11), 1525–1539. https://doi.org/10.1002/mc.22875CrossRef

347.

Shi, Y., Zhang, B., Feng, X., Qu, F., Wang, S., Wu, L., & Zhang, K. (2018). Apoptosis and autophagy induced by DVDMs-PDT on human esophageal cancer Eca-109 cells. Photodiagnosis and Photodynamic Therapy, 24, 198–205. https://doi.org/10.1016/j.pdpdt.2018.09.013CrossRef

348.

Sun, M., Zhang, Y., He, Y., Xiong, M., Huang, H., Pei, S., & Shao, D. (2019). Green synthesis of carrier-free curcumin nanodrugs for light-activated breast cancer photodynamic therapy. Colloids and Surfaces B, Biointerfaces, 180, 313–318. https://doi.org/10.1016/j.colsurfb.2019.04.061CrossRef

349.

Niu, T., Tian, Y., Wang, G., Guo, G., Tong, Y., & Shi, Y. (2020). Inhibition of ROS-NF-κB-dependent autophagy enhances hypocrellin A united LED red light-induced apoptosis in squamous carcinoma A431 cells. Cellular Signalling, 69, 109550. https://doi.org/10.1016/j.cellsig.2020.109550CrossRef

350.

Liu, J., Yan, G., Chen, Q., Zeng, Q., & Wang, X. (2021). Modified 5-aminolevulinic acid photodynamic therapy (M-PDT) inhibits cutaneous squamous cell carcinoma cell proliferation via targeting PP2A/PP5-mediated MAPK signaling pathway. The International Journal of Biochemistry & Cell Biology, 137, 106036. https://doi.org/10.1016/j.biocel.2021.106036CrossRef

351.

Huang, Q., Ou, Y.-S., Tao, Y., Yin, H., & Tu, P.-H. (2016). Apoptosis and autophagy induced by pyropheophorbide-α methyl ester-mediated photodynamic therapy in human osteosarcoma MG-63 cells. Apoptosis: An International Journal on Programmed Cell Death, 21(6), 749–760. https://doi.org/10.1007/s10495-016-1243-4CrossRef

352.

Wu, R., Yow, C., Law, E., Chu, E., & Huang, Z. (2020). Effect of Foslip® mediated photodynamic therapy on 5-fluorouracil resistant human colorectal cancer cells. Photodiagnosis and Photodynamic Therapy, 31, 101945. https://doi.org/10.1016/j.pdpdt.2020.101945CrossRef

353.

Song, C., Xu, W., Wu, H., Wang, X., Gong, Q., Liu, C., & Zhou, L. (2020). Photodynamic therapy induces autophagy-mediated cell death in human colorectal cancer cells via activation of the ROS/JNK signaling pathway. Cell Death & Disease, 11(10), 938. https://doi.org/10.1038/s41419-020-03136-yCrossRef

354.

Lamouille, S., Xu, J., & Derynck, R. (2014). Molecular mechanisms of epithelial-mesenchymal transition. Nature Reviews. Molecular Cell Biology, 15(3), 178–196. https://doi.org/10.1038/nrm3758CrossRef

355.

Rickard, B. P., Conrad, C., Sorrin, A. J., Ruhi, M. K., Reader, J. C., Huang, S. A., & Rizvi, I. (2021). Malignant ascites in ovarian cancer: Cellular, acellular, and biophysical determinants of molecular characteristics and therapy response. Cancers, 13(17), 4318. https://doi.org/10.3390/cancers13174318CrossRef

356.

Zhang, Y., & Weinberg, R. A. (2018). Epithelial-to-mesenchymal transition in cancer: Complexity and opportunities. Frontiers of Medicine, 12(4), 361–373. https://doi.org/10.1007/s11684-018-0656-6CrossRef

357.

Dongre, A., & Weinberg, R. A. (2019). New insights into the mechanisms of epithelial-mesenchymal transition and implications for cancer. Nature Reviews. Molecular Cell Biology, 20(2), 69–84. https://doi.org/10.1038/s41580-018-0080-4CrossRef

358.

Zhang, J., Wang, N., Li, Q., Zhou, Y., & Luan, Y. (2021). A two-pronged photodynamic nanodrug to prevent metastasis of basal-like breast cancer. Chemical Communications (Cambridge, England), 57(18), 2305–2308. https://doi.org/10.1039/d0cc08162kCrossRef

359.

Ma, H., Yang, K., Li, H., Luo, M., Wufuer, R., & Kang, L. (2021). Photodynamic effect of chlorin e6 on cytoskeleton protein of human colon cancer SW480 cells. Photodiagnosis and photodynamic therapy, 33, 102201. https://doi.org/10.1016/j.pdpdt.2021.102201CrossRef

360.

Theodoraki, M.-N., Yerneni, S. S., Brunner, C., Theodorakis, J., Hoffmann, T. K., & Whiteside, T. L. (2018). Plasma-derived exosomes reverse epithelial-to-mesenchymal transition after photodynamic therapy of patients with head and neck cancer. Oncoscience, 5(3–4), 75–87. https://doi.org/10.18632/oncoscience.410CrossRef

361.

Liu, L.-Y., Man, X.-X., Yao, H.-X., & Tan, Y.-Y. (2017). Effects of pheophorbide a-mediated photodynamic therapy on proliferation and metastasis of human prostate cancer cells. European Review for Medical and Pharmacological Sciences, 21(24), 5571–5579. https://doi.org/10.26355/eurrev_201712_13994CrossRef

362.

Calvo, G., Sáenz, D., Simian, M., Sampayo, R., Mamone, L., Vallecorsa, P., & Di Venosa, G. (2017). Reversal of the migratory and invasive phenotype of Ras-transfected mammary cells by photodynamic therapy treatment. Journal of Cellular Biochemistry, 118(3), 464–477. https://doi.org/10.1002/jcb.25657CrossRef

363.

Ma, C., Shi, L., Huang, Y., Shen, L., Peng, H., Zhu, X., & Zhou, G. (2017). Nanoparticle delivery of Wnt-1 siRNA enhances photodynamic therapy by inhibiting epithelial-mesenchymal transition for oral cancer. Biomaterials Science, 5(3), 494–501. https://doi.org/10.1039/c6bm00833jCrossRef

364.

Guo, Z., Zheng, K., Tan, Z., Liu, Y., Zhao, Z., Zhu, G., & Kang, T. (2018). Overcoming drug resistance with functional mesoporous titanium dioxide nanoparticles combining targeting, drug delivery and photodynamic therapy. Journal of Materials Chemistry. B, 6(46), 7750–7759. https://doi.org/10.1039/c8tb01810cCrossRef

365.

Chen, X., Liu, J., Li, Y., Pandey, N. K., Chen, T., Wang, L., & Chen, W. (2022). Study of copper-cysteamine based X-ray induced photodynamic therapy and its effects on cancer cell proliferation and migration in a clinical mimic setting. Bioactive Materials, 7, 504–514. https://doi.org/10.1016/j.bioactmat.2021.05.016CrossRef

366.

Della Pietra, E., Simonella, F., Bonavida, B., Xodo, L. E., & Rapozzi, V. (2015). Repeated sub-optimal photodynamic treatments with pheophorbide a induce an epithelial mesenchymal transition in prostate cancer cells via nitric oxide. Nitric Oxide: Biology and Chemistry, 45, 43–53. https://doi.org/10.1016/j.niox.2015.02.005CrossRef

367.

Lucena, S. R., Zamarrón, A., Carrasco, E., Marigil, M. A., Mascaraque, M., Fernández-Guarino, M., & Juarranz, A. (2019). Characterisation of resistance mechanisms developed by basal cell carcinoma cells in response to repeated cycles of photodynamic therapy. Scientific Reports, 9(1), 4835. https://doi.org/10.1038/s41598-019-41313-yCrossRef

368.

Sahai, E., Astsaturov, I., Cukierman, E., DeNardo, D. G., Egeblad, M., Evans, R. M., & Werb, Z. (2020). A framework for advancing our understanding of cancer-associated fibroblasts. Nature Reviews. Cancer, 20(3), 174–186. https://doi.org/10.1038/s41568-019-0238-1CrossRef

369.

Chen, Y., McAndrews, K. M., & Kalluri, R. (2021). Clinical and therapeutic relevance of cancer-associated fibroblasts. Nature Reviews. Clinical Oncology, 18(12), 792–804. https://doi.org/10.1038/s41571-021-00546-5CrossRef

370.

Fiori, M. E., Di Franco, S., Villanova, L., Bianca, P., Stassi, G., & De Maria, R. (2019). Cancer-associated fibroblasts as abettors of tumor progression at the crossroads of EMT and therapy resistance. Molecular Cancer, 18(1), 70. https://doi.org/10.1186/s12943-019-0994-2CrossRef

371.

Kuzet, S.-E., & Gaggioli, C. (2016). Fibroblast activation in cancer: When seed fertilizes soil. Cell and Tissue Research, 365(3), 607–619. https://doi.org/10.1007/s00441-016-2467-xCrossRef

372.

Zhen, Z., Tang, W., Wang, M., Zhou, S., Wang, H., Wu, Z., & Xie, J. (2017). Protein nanocage mediated fibroblast-activation protein targeted photoimmunotherapy to enhance cytotoxic t cell infiltration and tumor control. Nano Letters, 17(2), 862–869. https://doi.org/10.1021/acs.nanolett.6b04150CrossRef

373.

Egeblad, M., Littlepage, L. E., & Werb, Z. (2005). The fibroblastic coconspirator in cancer progression. Cold Spring Harbor Symposia on Quantitative Biology, 70, 383–388. https://doi.org/10.1101/sqb.2005.70.007CrossRef

374.

Anbil, S., Pigula, M., Huang, H.-C., Mallidi, S., Broekgaarden, M., Baglo, Y., & Hasan, T. (2020). Vitamin D receptor activation and photodynamic priming enables durable low-dose chemotherapy. Molecular Cancer Therapeutics, 19(6), 1308–1319. https://doi.org/10.1158/1535-7163.MCT-19-0791CrossRef

375.

Bulin, A.-L., Broekgaarden, M., & Hasan, T. (2017). Comprehensive high-throughput image analysis for therapeutic efficacy of architecturally complex heterotypic organoids. Scientific Reports, 7(1), 16645. https://doi.org/10.1038/s41598-017-16622-9CrossRef

376.

Lamberti, M. J., Rettel, M., Krijgsveld, J., Rivarola, V. A., & Rumie Vittar, N. B. (2019). Secretome profiling of heterotypic spheroids suggests a role of fibroblasts in HIF-1 pathway modulation and colorectal cancer photodynamic resistance. Cellular Oncology (Dordrecht), 42(2), 173–196. https://doi.org/10.1007/s13402-018-00418-8CrossRef

377.

Gallego-Rentero, M., Gutiérrez-Pérez, M., Fernández-Guarino, M., Mascaraque, M., Portillo-Esnaola, M., Gilaberte, Y., & Juarranz, Á. (2021). TGFβ1 Secreted by cancer-associated fibroblasts as an inductor of resistance to photodynamic therapy in squamous cell carcinoma cells. Cancers, 13(22), 5613. https://doi.org/10.3390/cancers13225613CrossRef

378.

Moosavi, F., Giovannetti, E., Saso, L., & Firuzi, O. (2019). HGF/MET pathway aberrations as diagnostic, prognostic, and predictive biomarkers in human cancers. Critical Reviews in Clinical Laboratory Sciences, 56(8), 533–566. https://doi.org/10.1080/10408363.2019.1653821CrossRef

379.

Matsumoto, K., Umitsu, M., De Silva, D. M., Roy, A., & Bottaro, D. P. (2017). Hepatocyte growth factor/MET in cancer progression and biomarker discovery. Cancer Science, 108(3), 296–307. https://doi.org/10.1111/cas.13156CrossRef

380.

Li, L., Zhou, S., Lv, N., Zhen, Z., Liu, T., Gao, S., & Ma, Q. (2018). Photosensitizer-encapsulated ferritins mediate photodynamic therapy against cancer-associated fibroblasts and improve tumor accumulation of nanoparticles. Molecular Pharmaceutics, 15(8), 3595–3599. https://doi.org/10.1021/acs.molpharmaceut.8b00419CrossRef

381.

Li, S., Wang, P., Zhang, G., Ji, J., Lv, T., Wang, X., & Wang, H. (2019). The effect of ALA-PDT on reversing the activation of cancer-associated fibroblasts in cutaneous squamous cell carcinoma. Photodiagnosis and Photodynamic Therapy, 27, 234–240. https://doi.org/10.1016/j.pdpdt.2019.05.043CrossRef

382.

Miao, L., Lin, C. M., & Huang, L. (2015). Stromal barriers and strategies for the delivery of nanomedicine to desmoplastic tumors. Journal of Controlled Release: Official Journal of the Controlled Release Society, 219, 192–204. https://doi.org/10.1016/j.jconrel.2015.08.017CrossRef

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