Integrin-Mediated Adhesion and Signalling in Ovarian Cancer Cells

Buczek‐Thomas, Jo Ann; Chen, Norah; Hasan, Tayyaba

doi:10.1016/s0898-6568(97)00074-0

Cited by 34 publications

(33 citation statements)

References 27 publications

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“…Cell preparation A total of 3 × 10 5 OVCAR 3 cells were plated on a microscope cover slip and incubated for at least 24 h. BPD-MA was dissolved in complete medium to a final concentration of 0.092 µmol l -1 and incubated for 3 h. For 20 min, Rhodamine 123 (R123, Eastman Kodak, Rochester, NY, USA) was added to a final concentration of 0.01 µmol l -1 for co-incubation (Chen, 1998). The coverslips were rinsed in PBS and mounted with PBS on a microscope slide using 0.02-mm-thick distance holders in order to prevent compression of the cells.…”

Section: Cellular Localization Of Bpd-mamentioning

confidence: 99%

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BPD-MA-mediated photosensitization in vitro and in vivo: cellular adhesion and β1 integrin expression in ovarian cancer cells

et al. 1999

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Summary Benzoporphyrin derivative monoacid (BPD-MA) photosensitization was examined for its effects on cellular adhesion of a human ovarian cancer cell line, OVCAR 3, to extracellular matrix (ECM) components. Mild BPD-MA photosensitization (~ 85% cell survival) of OVCAR 3 transiently decreased adhesion to collagen IV, fibronectin, laminin and vitronectin to a greater extent than could be attributed to cell death. The loss in adhesiveness was accompanied by a loss of β 1 integrin-containing focal adhesion plaques (FAPs), although β 1 subunits were still recognized by monoclonal antibody directed against human β 1 subunits. In vivo BPD-MA photosensitization decreased OVCAR 3 adhesiveness as well. Photosensitized adhesion was reduced in the presence of sodium azide and enhanced in deuterium oxide, suggesting mediation by singlet oxygen. Co-localization studies of BPD-MA and Rhodamine 123 showed that the photosensitizer was largely mitochondrial, but also exhibited extramitochondrial, intracellullar, diffuse cytosolic fluorescence. Taken together, these data show that intracellular damage mediated by BPD-PDT remote from the FAP site can affect cellular-ECM interactions and result in loss of FAP formation. This may have an impact on long-term effects of photodynamic therapy. The topic merits further investigation.

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Section: Cellular Localization Of Bpd-mamentioning

confidence: 99%

“…Adhesion to the ECM or endothelium, and subsequent migration through vessel walls, is also mediated by integrins. A role for integrin-mediated signalling in ovarian cancer has also been suggested (Buczek-Thomas et al, 1998).…”

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confidence: 99%

BPD-MA-mediated photosensitization in vitro and in vivo: cellular adhesion and β1 integrin expression in ovarian cancer cells

et al. 1999

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“…Cancer and mesothelial cells secrete lysophosphatidic acid (9) and other proteins [fibronectin, periostin, osteopontin, and laminin (10-13)], which stabilize the extracellular matrix (ECM) and promote establishment of metastases. These interactions with the mesothelium and the peritoneal stroma activate ''outside-in'' signaling (14), which stimulates cancer cell proliferation and survival. In this context, neovascularization is facilitated and peritoneal metastases form and grow.…”

Section: Introductionmentioning

confidence: 99%

Enhanced Peritoneal Ovarian Tumor Dissemination by Tissue Transglutaminase

et al. 2007

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Tissue transglutaminase (TG2) is involved in Ca 2+ -dependent aggregation and polymerization of proteins. We previously reported that TG2 mRNA is up-regulated in epithelial ovarian cancer (EOC) cells compared with normal ovarian epithelium. Here, we show overexpression of the TG2 protein in ovarian cancer cells and tumors and its secretion in ascites fluid and define its role in EOC. By stable knockdown and overexpression, we show that TG2 enhances EOC cell adhesion to fibronectin and directional cell migration. This phenotype is preserved in vivo, where the pattern of tumor dissemination in the peritoneal space is dependent on TG2 expression levels.

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“…9) In tumor cells, integrins have been shown to mediate the organization of the extracellular matrix, 10) adhesion to extracellular matrix proteins, [11][12][13] and cell motility. [14][15][16] We have reported that the binding of EGCG to Fas, presumably on the cell surface, triggers Fasmediated apoptosis in tumor cells 17) and that EGCG impairs the adhesion of cancer cells to extracellular matrix proteins such as fibronectin and laminin by binding to fibronectin and laminin. 18,19) However, it is not clear whether the binding of EGCG to tumor cells causes an impairment of cell adhesion.…”

Section: Introductionmentioning

confidence: 99%