English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Journal Article

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

MPS-Authors
/persons/resource/persons78606

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

/persons/resource/persons78797

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

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-70EA-D
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.