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- W2026002008 abstract "T-cadherin is a glycosyl-phosphatidylinositol (GPI) anchored cadherin molecule. We previously reported that T-cadherin is normally expressed on the basal keratinocytes of the epidermis and is down-regulated in cutaneous squamous cell carcinoma (SCC). We found that expression of T-cadherin in cutaneous squamous carcinoma cells regulated level of surface β1 integrin, which functioned as extracellular matrix (ECM) receptor. Involvement of T-cadherin in β1 integrin trafficking was studied using three different stable cell lines with cytomegalovirus (CMV)-driven over-expression, tetracycline (Tet)-inducible expression and RNAi-mediated suppressed expression of T-cadherin. Pulse–chase analysis using a cholesterol-depleting reagent and a tyrosine kinase inhibitor showed that β1 integrin mainly internalized via caveolae. Over-expression of T-cadherin suppressed the internalization of both β1 integrin and cholera toxin (CTX), a marker of caveolae-mediated endocytosis. By Western blot analysis of tyrosine-kinase target molecules, we demonstrated a reduced level of EGF receptor (EGFR)-phosphorylation in T-cadherin over-expressing cells. In addition, studies using EGF and EGFR specific inhibitors revealed that EGFR activation stimulated β1 integrin internalization. Taking these results together, T-cadherin may modulate cell–matrix adhesion in basal keratinocytes as well as invasive potency in SCC by regulating surface level of β1 integrin." @default.
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- W2026002008 date "2007-06-06" @default.
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- W2026002008 title "T-cadherin enhances cell?matrix adhesiveness by regulating ?1 integrin trafficking in cutaneous squamous carcinoma cells" @default.
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- W2026002008 doi "https://doi.org/10.1111/j.1365-2443.2007.01092.x" @default.
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