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 alphaVbeta3 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 alpha5IVa were shown by site-directed mutagenesis to make different contributions to cell adhesion but were equivalent in binding alphaVbeta3 integrin. A quantitative radioimmuno-inhibition assay was established based on domain alpha5IVa which demonstrated distinct amounts of alpha5 chain in various tissues, particularly in vessel walls. There it could play a role in angiogenesis steps requiring RGD-dependent integrins.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Binding Sites
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Cell Adhesion
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Cell Adhesion Molecules / genetics
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Cell Adhesion Molecules / isolation & purification
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Cell Adhesion Molecules / metabolism*
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Humans
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Integrin beta1 / metabolism*
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Kidney / cytology
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Laminin / genetics
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Laminin / isolation & purification
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Laminin / metabolism*
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Melanoma, Experimental
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Mice
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Muscle, Skeletal / cytology
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Oligopeptides / metabolism*
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Peptide Fragments / genetics
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Peptide Fragments / isolation & purification
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Peptide Fragments / metabolism
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Protein Structure, Tertiary
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Receptors, Vitronectin / metabolism*
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Recombinant Proteins / metabolism
Substances
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Cell Adhesion Molecules
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Integrin beta1
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Laminin
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Oligopeptides
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Peptide Fragments
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Receptors, Vitronectin
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Recombinant Proteins
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laminin alpha5
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arginyl-glycyl-aspartic acid