The degradation of articular collagen by neutrophil proteinases.
The action of the serine proteinase (EC 3.4.21--)of human neutrophil leucocytes, elastase and cathepsin G, on cartilage and tendon was investigated. With cartilage, both enzymes first degraded the proteoglycan, then solubilized collagen by an attack on the terminal peptides, destroying the inter- and intramolecular cross-links. There was little degradation of the helical region of the type II collagen. Elastase also solubilized type I collagen from tendon, though this was less susceptible than cartilage collagen, and attacked the terminal peptides and perhaps the helical region of type I skin collagen in solution. Cathepsin G had little or no effect on type I collagen of skin or tendon. Since massive infiltration of joint tissues by neutrophil leucocytes is a prominent feature of inflammatory joint disease, it may well be that elastase and cathepsin G make a significant contribution to the tissue damage that occurs.
D000125:Achilles Tendon / Q000378:metabolism; D000818:Animals; D002358:Cartilage, Articular / Q000378:metabolism; D002403:Cathepsins / Q000097:blood*; D003094:Collagen / Q000378:metabolism*; D006801:Humans; D007596:Joints; D007817:Laryngeal Cartilages / Q000378:metabolism; D008954:Models, Biological; D009504:Neutrophils / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000097:blood*; D011509:Proteoglycans / Q000378:metabolism; D011817:Rabbits; D012867:Skin; D013552:Swine; D014357:Trypsin
D011509:Proteoglycans; D003094:Collagen; D002403:Cathepsins; D010196:Pancreatic Elastase; D014357:Trypsin