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• W145784325 startingPage "131" @default.
• W145784325 abstract "Classical cadherins are single-pass transmembrane glycoproteins engaged in homophilic calcium-dependent cell-cell adhesion complexes, a system highly conserved in all multicellular organisms. E-cadherin is one of these enthralling adhesive receptors, originally named uvomorulin, for its “glue” ability during the early stage of embryogenesis. Highly expressed in differentiated and polarized epithelial cells, the dynamic formation and disassembly of E-cadherin contacts participate in most developmental and pathological processes involving morphogenetic changes in the epithelium. E-cadherins bind through their extracellular region to E-cadherins expressed in adjacent cells and are linked through their intracytoplasmic tail to the cytoskeleton through a family of proteins collectively known as catenins, which also play an important role in E-cadherin-initiated intracellular signaling. E-cadherin is believed to act as a tumor- and metastasis-suppressor gene, as its expression and function are down-regulated or altered in many human cancers, and its re-expression decreases both the proliferative and invasive capacity of tumor cells. Recent evidence suggests the existence of a direct cross-talk between E-cadherin and EGF receptors (EGFR). Indeed, EGFR activation can cause the dismantling of cell-cell contacts by promoting the destabilization of E-cadherin/catenin adhesive complexes, the down-regulation of E-cadherin expression, and the endocytosis and subsequent degradation of pre-existing cell surface E-cadherins. On the other hand, the engagement of E-cadherin in newly formed cell contacts causes the rapid EGF-independent activation of EGFR, thereby triggering EGFR-initiated signaling pathways that enhance cell proliferation or survival through MAPK, PI3-Kinase and Rho GTPases. Further studies into the molecular mechanism underlying the interplay between E-Cadherin and EGFR in normal and tumoral epithelial cells may ultimately help to identify more effective EGFR-targeting strategies for cancer treatment." @default.
• W145784325 created "2016-06-24" @default.
• W145784325 creator A5038753309 @default.
• W145784325 creator A5067698501 @default.
• W145784325 date "2008-01-01" @default.
• W145784325 modified "2023-09-27" @default.
• W145784325 title "A Molecular Crosstalk between E-cadherin and EGFR Signaling Networks" @default.
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