Neutral protease inhibitors from human intervertebral disc and femoral head articular cartilage.
Assays of several proteases, incorporating guanidinium chloride extracts of human femoral head cartilage and intervertebral disc, demonstrated that both tissues contain inhibitors of certain serine proteases. Trypsin, chymotrypsin and a granule extract of human polymorphonuclear leukocytes containing elastase and cathepsin G activities, were inhibited by low molecular weight fractions prepared by Sephadex G-75 chromatography. Using a radioassay, it was further shown that these fractions inhibit proteolysis of cartilage proteoglycan. The inhibitor in intervertebral disc is concentrated in the nucleus pulposus, with a decreasing gradient to the periphery of the annulus fibrosus. It is proposed that these inhibitors confer at least partial protection against pathological proteolysis of the proteoglycans in human articular cartilage and nucleus pulposus.
D000818:Animals; D002358:Cartilage, Articular / Q000032:analysis*; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D005269:Femur; D005341:Fibrinolysin / Q000037:antagonists & inhibitors; D006801:Humans; D007403:Intervertebral Disc / Q000032:analysis*; D009504:Neutrophils / Q000201:enzymology; D011480:Protease Inhibitors / Q000302:isolation & purification / Q000494:pharmacology*; D013552:Swine; D013820:Thermolysin / Q000037:antagonists & inhibitors; D014361:Trypsin Inhibitors / Q000494:pharmacology
D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D002918:Chymotrypsin; D005341:Fibrinolysin; D013820:Thermolysin