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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

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.

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Genre: Journal Article
Alternative Title : FEBS Lett.

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 Creators:
Sasaki, T.1, Author           
Timpl, R.1, Author           
Affiliations:
1Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565145              

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Free keywords: basement membrane; cell-matrix interaction; radioimmunoassay; recombinant protein
 Abstract: 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.

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Language(s): eng - English
 Dates: 2001-12-07
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 34937
ISI: 000172757500008
 Degree: -

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Title: FEBS Letters
  Alternative Title : FEBS Lett.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 509 (2) Sequence Number: - Start / End Page: 181 - 185 Identifier: ISSN: 0014-5793