Degradation of cartilage collagens type II, IX, X and XI by enzymes derived from human articular chondrocytes.
Conditioned culture medium derived from Interleukin-I alpha-activated human articular chondrocytes contained both collagen- and proteoglycan-degrading activities. Preparations of soluble type I collagen and the cartilage collagens type II, IX, X and XI were all degraded when incubated with the conditioned culture medium at 35 degrees C. Fractionation of the enzymic activities using column chromatography with Ultragel AcA 34 and Heparin-Sepharose allowed the separation and identification of neutral proteinase, collagenolytic and proteoglycan-degrading activities. Eluant fractions which contained type I collagenase activity effectively degraded collagen type II, but these fractions did not correspond precisely with those which degraded collagen types IX, X and XI. These observations indicate that chondrocytes have the potential to produce a conventional interstitial type II collagenase together with other enzymes having some specificity for the minor collagens. Thus IL-1-activated chondrocytes produce a range of collagenolytic and proteoglycan-degrading enzymes which can process most of the structural components of the cartilage matrix.
Gadher
S J
SJ
Department of Medicine, University Hospital of South Manchester, UK.
Eyre
D R
DR
Wotton
S F
SF
Schmid
T M
TM
Woolley
D E
DE
D002358:Cartilage, Articular / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*; D002478:Cells, Cultured; D003094:Collagen / Q000145:classification / Q000378:metabolism*; D003470:Culture Media; D006801:Humans; D007375:Interleukin-1 / Q000494:pharmacology; D003012:Microbial Collagenase / Q000378:metabolism; D011509:Proteoglycans / Q000378:metabolism
D003470:Culture Media; D007375:Interleukin-1; D011509:Proteoglycans; D003094:Collagen; D003012:Microbial Collagenase