Fibulin-5 binds human smooth-muscle cells through α5β1 and α4β1 integrins, but does not support receptor activation
Autor: | Daniel V. Bax, C. Adrian Shuttleworth, Kieran T. Mellody, Cay M. Kielty, Lyle J. Freeman, Amanda Lomas |
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Rok vydání: | 2007 |
Předmět: |
Extracellular Matrix Proteins
biology Cell adhesion molecule Myocytes Smooth Muscle Integrin Cell Biology Integrin alpha4beta1 Biochemistry Fibulin Cell biology Fibronectin Focal adhesion Extracellular matrix Gene Expression Regulation Growth factor receptor Cell Movement Cell Adhesion biology.protein Humans Cell adhesion Molecular Biology Cells Cultured Research Article Cell Proliferation Integrin alpha5beta1 |
Zdroj: | Biochemical Journal. 405:417-428 |
ISSN: | 1470-8728 0264-6021 |
DOI: | 10.1042/bj20070400 |
Popis: | Fibulin-5, an extracellular matrix glycoprotein expressed in elastin-rich tissues, regulates vascular cell behaviour and elastic fibre deposition. Recombinant full-length human fibulin-5 supported primary human aortic SMC (smooth-muscle cell) attachment through alpha5beta1 and alpha4beta1 integrins. Cells on fibulin-5 spread poorly and displayed prominent membrane ruffles but no stress fibres or focal adhesions, unlike cells on fibronectin that also binds these integrins. Cell migration and proliferation were significantly lower on fibulin-5 than on fibronectin. Treatment of cells on fibulin-5 with a beta1 integrin-activating antibody induced stress fibres, increased attachment, migration and proliferation, and stimulated signalling of epidermal growth factor receptor and platelet-derived growth factor receptors alpha and beta. Fibulin-5 also modulated fibronectin-mediated cell spreading and morphology. We have thus identified the beta1 integrins on primary SMCs that fibulin-5 interacts with, and have shown that failure of fibulin-5 to activate these receptors limits cell spreading, migration and proliferation. |
Databáze: | OpenAIRE |
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