TAILIEUCHUNG - Báo cáo khoa học: The tetraspanin CD151 regulates cell morphology and intracellular signaling on laminin-511

The tetraspanin CD151 forms a stable complex with integrina3b1, a widely expressed laminin receptor, and is implicated in the regulation of integrin a3b1-mediated cellular responses, including cell attachment, spreading and migration. | ỊFEBS Journal The tetraspanin CD151 regulates cell morphology and intracellular signaling on laminin-511 Masashi Yamada Yasuhiro Sumida Akemi Fujibayashi Kiyomitsu Fukaguchi Noriko Sanzen Ryoko Nishiuchi and Kiyotoshi Sekiguchi Laboratory of Extracellular Matrix Biochemistry Institute for Protein Research Osaka University Japan Keywords basement membrane cell adhesion FAK integrin Src Correspondence K. Sekiguchi Laboratory of Extracellular Matrix Biochemistry Institute for Protein Research Osaka University 3-2 Yamadaoka Suita Osaka 565-0871 Japan Fax 81 6 6879 8619 Tel 81 6 6879 8617 E-mail sekiguch@ Received 8 January 2008 revised 18 April 2008 accepted 28 April 2008 doi The tetraspanin CD151 forms a stable complex with integrin a3pi a widely expressed laminin receptor and is implicated in the regulation of integrin a3p1-mediated cellular responses including cell attachment spreading and migration. However the molecular mechanism by which CD151 regulates integrin a3p1 functions remains unclear. To address this issue we knocked down CD151 expression in A549 human lung adenocarcinoma cells by RNA interference. When plated on laminin-511 laminin-10 the CD151-knocked-down cells showed aberrant membrane protrusions and exhibited reductions in the tyrosine phosphorylation of focal adhesion kinase Src p130Cas and paxillin. The formation of membrane protrusions was attenuated when the cells were either plated on surfaces coated with higher concentrations of laminin-511 or treated with the integrin p1-acti-vating mAb TS2 16 however neither treatment could rescue the reduced tyrosine phosphorylation. These results indicate that CD151 knockdown weakens the integrin a3p1-mediated adhesion to laminin-511 and thereby provokes an aberrant morphology but this reduced adhesive activity is not involved in the decline of signaling events in CD151-knocked-down cells. Thus our results suggest that CD151 regulates integrin a3p1 .

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