Collagen binding proteins derived from the embryonic fibroblast cell surface recognize arginine-glycine-aspartic acid.
Several cell surface proteins (Mr = 120,000, 90,000, 63,000 and 47,000) apparently integral to embryonic fibroblast plasma membranes were extracted with detergent and isolated by collagen affinity chromatography. Certain of these proteins (Mr = 120,000, 90,000, and 47,000) were specifically eluted from collagen affinity columns by synthetic peptides containing the amino acid sequence arginyl-glycyl-aspartic acid (RGD). These data show that a number of collagen binding proteins exist on the embryonic fibroblast cell surface. Some of the proteins may be collagen receptors binding to RGD sequences in the collagen molecule while at least one of the proteins (Mr = 63,000) recognizes features other than RGD.
Ogle
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Department of Anatomy and Cell Biology, University of Virginia, Charlottesville 22908.
Little
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D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D002478:Cells, Cultured; D002642:Chick Embryo; D002846:Chromatography, Affinity; D003094:Collagen / Q000378:metabolism*; D005347:Fibroblasts / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008970:Molecular Weight; D009842:Oligopeptides / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000302:isolation & purification / Q000378:metabolism*; D038981:Receptors, Collagen
D002352:Carrier Proteins; D008565:Membrane Proteins; D009842:Oligopeptides; D011956:Receptors, Cell Surface; D038981:Receptors, Collagen; C047981:arginyl-glycyl-aspartic acid; D003094:Collagen