Purification of the neutral proteoglycan-degrading metalloproteinase from human articular cartilage tissue and its identification as stromelysin matrix metalloproteinase-3.
The 'neutral' proteoglycan-degrading metalloproteinase of human articular cartilage was purified 3,500-fold by use of an anti-(matrix metalloproteinase-3) immunoglobulin G affinity column. Molecular masses of the latent and multiple active forms and specificity of action on casein, transferrin, gelatin and fibronectin were identical with those of authentic stromelysin (matrix metalloproteinase-3) from cultured human rheumatoid synovial fibroblasts. The optimum pH of this proteinase on proteoglycan monomer was pH 5.5, and on Azocoll, 6.2; digestion of fibronectin and gelatin was more extensive at pH 5.5 than at 7.5.
Gunja-Smith
Z
Z
Department of Medicine, University of Miami School of Medicine, FL 33101.
Nagase
H
H
Woessner
J F
JF
D002358:Cartilage, Articular / Q000032:analysis*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D019278:Matrix Metalloproteinase 3; D008666:Metalloendopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D011509:Proteoglycans / Q000378:metabolism; D013379:Substrate Specificity
D011509:Proteoglycans; D008666:Metalloendopeptidases; D019278:Matrix Metalloproteinase 3