Tissue inhibitor of metalloproteinases (TIMP) regulates extracellular type I collagen degradation by chondrocytes and endothelial cells.
A specific antiserum to purified rabbit tissue inhibitor of metalloproteinases (TIMP) was raised in sheep, characterized and used to investigate the role of TIMP in a model system. Chondrocytes and endothelial cells cultured on 14C-labelled type I collagen films and stimulated to produce collagenase were unable to degrade the films unless the anti-TIMP antibody was added. The degradation induced was inhibited by a specific anti-rabbit collagenase antibody. It was concluded that TIMP is a major regulatory factor in cell-mediated collagen degradation.
Gavrilovic
J
J
Department of Cell Physiology, Strangeways Research Laboratory, Cambridge, England.
Hembry
R M
RM
Reynolds
J J
JJ
Murphy
G
G
D000818:Animals; D002358:Cartilage, Articular / Q000378:metabolism*; D002478:Cells, Cultured; D003094:Collagen / Q000378:metabolism*; D004727:Endothelium / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000276:immunology / Q000378:metabolism*; D007106:Immune Sera / Q000494:pharmacology; D003012:Microbial Collagenase / Q000276:immunology; D011817:Rabbits; D019714:Tissue Inhibitor of Metalloproteinases
D004791:Enzyme Inhibitors; D007106:Immune Sera; D019714:Tissue Inhibitor of Metalloproteinases; D003094:Collagen; D003012:Microbial Collagenase