| Literature DB >> 24808173 |
Rika Tanaka1, Yutaka Seki1, Yohei Saito1, Sadahiro Kamiya2, Motomichi Fujita1, Hiroaki Okutsu1, Takuya Iyoda1, Tatsuya Takai1, Toshiyuki Owaki1, Hirofumi Yajima3, Junichi Taira4, Ryo Hayashi5, Hiroaki Kodama5, Takuya Matsunaga1, Fumio Fukai6.
Abstract
Tenascin-C is an adhesion modulatory matrix protein that is highly expressed in tumors; however, its biochemical activity involved in tumorigenesis is not fully understood. On the other hand, increasing evidence indicates the importance of integrin α5β1 in cancer development. We previously demonstrated that tenascin-C harbors a functional site that can be released as a proadhesive peptide such as TNIIIA2. Peptide TNIIIA2 is capable of inducing activation of β1-integrins including α5β1 via syndecan-4. In this study the proadhesive effect of TNIIIA2 was characterized by potentiated and sustained activation of integrin α5β1. Based on this effect, TNIIIA2 rendered nontransformed fibroblasts (NIH3T3) resistant to serum deprivation-elicited anoikis through activation of the Akt/Bcl-2 pathway. Moreover, TNIIIA2 hyperstimulated PDGF-dependent proliferation of NIH3T3 by activating integrin α5β1. Tenascin-C, a parental protein of TNIIIA2, also stimulated PDGF-dependent proliferation, which was blocked by a matrix metalloproteinase-2/9 inhibitor and an anti-TNIIIA2 function-blocking antibody, suggesting proteolytic exposure of the proadhesive effect of TNIIIA2. Mechanistic analyses revealed that TNIIIA2 induced a lateral association of PDGF receptor β with the molecular complex of activated integrin α5β1 and syndecan-4 in the membrane microdomains enriched with cholesterol/caveolin-1, resulting in prolonged activation of PDGF receptor β and the subsequent Ras/mitogen-activated protein kinase pathway in a PDGF-dependent manner. Of note, TNIIIA2 induced continuous proliferation in NIH3T3 in an integrin α5β1-dependent manner even after they formed a confluent monolayer. Thus, it was proposed that tenascin-C might be involved in deregulated cell growth through potentiated and sustained activation of integrin α5β1 after exposure of the proadhesive effect of TNIIIA2.Entities:
Keywords: Cell Adhesion; Cell Proliferation; Extracellular Matrix; Integrin; PDGF; Tenascin
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Year: 2014 PMID: 24808173 PMCID: PMC4067204 DOI: 10.1074/jbc.M113.546622
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157