Thrombospondin 1 binds to the surface of bovine articular chondrocytes by a linear RGD-dependent mechanism.
Thrombospondin 1 is present in articular cartilage and is synthesized by chondrocytes. Adult bovine articular chondrocytes in serum-free medium were evaluated in a solid-phase assay for their ability to attach to thrombospondin 1 isolated from human platelets. The chondrocytes attached to the thrombospondin 1 by a mechanism that was inhibited by a synthetic linear GRGDSP but not a GRGESP peptide. The cells, however, did not spread on thrombospondin 1, but did spread on fibronectin and Pep-Tite 2000, a synthetic RGD-containing peptide. Preincubation of thrombospondin 1 with EDTA irreversibly inhibited its capacity to attach to chondrocytes. We conclude that thrombospondin 1 binds to chondrocytes by its RGD sequence.
Miller
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Department of Biomedical Engineering, Cleveland Clinic Foundation Research Institute, OH 44195-5254, USA.
McDevitt
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CA
D000595:Amino Acid Sequence; D000818:Animals; D002118:Calcium / Q000378:metabolism; D002358:Cartilage, Articular / Q000166:cytology / Q000378:metabolism*; D002417:Cattle; D002448:Cell Adhesion / Q000187:drug effects; D002478:Cells, Cultured; D004492:Edetic Acid / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D008562:Membrane Glycoproteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D019699:Thrombospondins
D008562:Membrane Glycoproteins; D009842:Oligopeptides; D019699:Thrombospondins; C047981:arginyl-glycyl-aspartic acid; D004492:Edetic Acid; D002118:Calcium