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Domain IVa of laminin α5 chain is cell‐adhesive and binds β1 and αVβ3 integrins through Arg‐Gly‐Asp
Author(s) -
Sasaki Takako,
Timpl Rupert
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03167-2
Subject(s) - integrin , laminin , cell adhesion , recombinant dna , adhesion , microbiology and biotechnology , angiogenesis , chemistry , mutagenesis , cell , biology , biochemistry , mutation , gene , cancer research , organic chemistry
The globular domain IVa from the short arm region of mouse laminin α5 chain was obtained by recombinant production and shown to be a cell‐adhesive substrate and to bind αVβ3 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 α5IVa were shown by site‐directed mutagenesis to make different contributions to cell adhesion but were equivalent in binding αVβ3 integrin. A quantitative radioimmuno‐inhibition assay was established based on domain α5IVa which demonstrated distinct amounts of α5 chain in various tissues, particularly in vessel walls. There it could play a role in angiogenesis steps requiring RGD‐dependent integrins.