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Domain IVa of laminin alpha 5 chain is cell-adhesive and binds beta 1 and alpha V beta 3 integrins through Arg-Gly-Asp

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78606

Sasaki,  T.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78797

Timpl,  R.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Sasaki, T., & Timpl, R. (2001). Domain IVa of laminin alpha 5 chain is cell-adhesive and binds beta 1 and alpha V beta 3 integrins through Arg-Gly-Asp. FEBS Letters, 509(2), 181-185.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-70EA-D
Zusammenfassung
The globular domain IVa from the short arm region of mouse laminin alpha5 chain was obtained by recombinant production and shown to be a cell-adhesive substrate and to bind alphaV beta3 integrin in solid-phase assays. These interactions were blocked by RGD peptides and a restricted panel of anti-integrin antibodies. The two RGD sequences present in alpha 5lVa were shown by site-directed mutagenesis to make different contributions to cell adhesion but were equivalent in binding alphaV beta3 integrin. A quantitative radioimmuno-inhibition assay was established based on domain beta 5IVa which demonstrated distinct amounts of a5 chain in various tissues, particularly in vessel walls. There it could play a role in angiogenesis steps requiring RGD-dependent integrins. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.