Abstract
In our studies of VLA-3 we have shown (i) that a single integrin (VLA-3) can bind to multiple ligands by different mechanisms, involving RGD and non-RGD sites, which are regulated differently by divalent cations. Also we showed from the primary sequence of VLA-3 that it is only distantly related to the other cleaved alpha subunits. In our studies of VLA-2 we have shown that a single integrin may have at least three functional forms, depending on the cell type where expressed. In addition, we have expressed functional VLA-2 in RD cells, resulting in both Coll and Lm binding functions in vitro, and increased tumor cell metastasis in vivo in nude mice.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Amino Acid Sequence
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Animals
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Binding, Competitive
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Cations, Divalent / metabolism
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Cell Adhesion
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Collagen / metabolism*
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Fibronectins / metabolism*
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Humans
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Laminin / metabolism*
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Ligands
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Mice
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Mice, Nude
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Molecular Sequence Data
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Neoplasm Proteins / metabolism
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Oligopeptides / metabolism
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Protein Conformation
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Receptors, Cell Surface / metabolism*
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Receptors, Collagen
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Receptors, Fibronectin
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Receptors, Immunologic / metabolism*
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Receptors, Laminin
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Receptors, Peptide*
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Receptors, Very Late Antigen / metabolism*
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Recombinant Proteins / metabolism
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Tumor Cells, Cultured / metabolism
Substances
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Cations, Divalent
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Fibronectins
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Laminin
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Ligands
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Neoplasm Proteins
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Oligopeptides
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Receptors, Cell Surface
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Receptors, Collagen
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Receptors, Fibronectin
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Receptors, Immunologic
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Receptors, Laminin
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Receptors, Peptide
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Receptors, Very Late Antigen
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Recombinant Proteins
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arginyl-glycyl-aspartic acid directed cell adhesion receptor
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arginyl-glycyl-aspartic acid
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Collagen
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glycyl-arginyl-glycyl-aspartyl-seryl-proline
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glycyl-arginyl-glycyl-glutamyl-seryl-proline