Abstract
Cartilage oligomeric matrix protein (COMP) and thrombospondin 1 (TSP1) were purified in a native form from normal bovine articular cartilage. The key step in the purification scheme was selective extraction with EDTA-containing buffer. Final separation of these two molecules was achieved by heparin affinity chromatography. Particles viewed by electron microscopy after rotary shadowing and negative staining revealed structures similar to their prototype molecules; from the Swarm rat chondrosarcoma for COMP, or from platelets for TSP1. Attachment of primary bovine chondrocytes to purified matrix proteins was investigated. Cells attached to COMP but not to the structurally related TSP1 indicating separate functions for these proteins in cartilage.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Cartilage, Articular / chemistry*
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Cartilage, Articular / cytology
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Cattle
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Cell Adhesion
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Cell Adhesion Molecules / isolation & purification*
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Cell Adhesion Molecules / metabolism
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Cell Adhesion Molecules / ultrastructure
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Enzyme-Linked Immunosorbent Assay
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Extracellular Matrix Proteins / isolation & purification*
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Extracellular Matrix Proteins / metabolism
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Extracellular Matrix Proteins / ultrastructure
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Glycoproteins*
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Matrilin Proteins
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Membrane Proteins / isolation & purification*
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Membrane Proteins / metabolism
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Membrane Proteins / ultrastructure
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Microscopy, Electron
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Molecular Sequence Data
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Rats
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Sequence Analysis
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Thrombospondins
Substances
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Cell Adhesion Molecules
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Extracellular Matrix Proteins
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Glycoproteins
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Matrilin Proteins
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Membrane Proteins
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Thrombospondins