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Biological Procedures Online

, Volume 4, Issue 1, pp 81–87

Received: 12 September 2002Revised: 21 September 2002Accepted: 15 October 2002DOI: 10.1251-bpo37

Cite this article as: Bao, W. & Strömblad, S. Biol Proced Online 2002 4: 81. doi:10.1251-bpo37

Abstract

Cell attachment to the extracellular matrix ECM engages integrin signaling into the cell, but part of the signaling response also stem from cell spreading 3. To analyze specific integrin signaling-mediated responses independent of cell spreading, we developed a method engaging integrin signaling by use of an immobilized anti-integrin monoclonal antibody mab directed against the fibronectin FN receptor integrin α5β1. ECV 304 cells were plated onto FN or immobilized mab JBS5 anti-integrin α5β1 or onto poly-L-lysin P-L-L, which mediates integrin-independent attachment. Cells attached and spread on FN, while cells on JBS5 or P-L-L attached but did not spread. Importantly, plating onto FN or mab JBS5 gave rise to identical integrin-induced responses, including a down-regulation of the cyclin-dependent kinase Cdk2 inhibitors p21 and p27, while attachment to P-L-L did not. We conclude that engagement of the FN-receptor integrin α5β1 induces integrin signaling regulating the Cdk2-inhibitors independent of cell spreading and present a method for how integrin signaling can be analyzed separate from the effects of cell spreading.

Indexing termscell adhesion integrins antibodies, monoclonal fibronectins protein kinases Published: November 11, 2002

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Autor: Wenjie Bao - Staffan Strömblad

Fuente: https://link.springer.com/







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