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Thrombospondin 1 binds to the surface of bovine articular chondrocytes by a linear RGD‐dependent mechanism
Author(s) -
Miller Raymond R.,
McDevitt Cahir A.
Publication year - 1995
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 - 10.1016/0014-5793(95)00311-v
Subject(s) - mechanism (biology) , chemistry , thrombospondin , biophysics , microbiology and biotechnology , biochemistry , biology , metalloproteinase , physics , matrix metalloproteinase , quantum mechanics
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.