title: Human articular cartilage secretes characteristic metal dependent proteinases upon stimulation by mononuclear cell factor.
abstract: Human articular cartilage stimulated during organ culture by the addition of human blood mononuclear cell factor concomitantly released latent proteinases and proteoglycan. Gel chromatography at pH 7.4 separated 2 distinct latent enzymes: a general proteinase which could degrade proteoglycan, casein and gelatin, and a collagenolytic activity of smaller molecular size. The general proteinase was calcium dependent and could be activated by either trypsin or 4-aminophenylmercuric acetate; the former procedure invariably generating greatest activity. The enzyme exhibited a broad bimodal pH profile against proteoglycan, with optimum activity at pH 5.5.
mesh_terms: D000328:Adult; D002358:Cartilage, Articular / Q000201:enzymology*; D002364:Caseins / Q000378:metabolism; D002850:Chromatography, Gel; D010450:Endopeptidases / Q000096:biosynthesis / Q000378:metabolism*; D004789:Enzyme Activation; D005260:Female; D006801:Humans; D008297:Male; D008670:Metals / Q000502:physiology*; D008875:Middle Aged; D015846:Monokines; D011506:Proteins / Q000494:pharmacology*; D011509:Proteoglycans / Q000378:metabolism; D013268:Stimulation, Chemical
chemical_list: D002364:Caseins; D008670:Metals; D015846:Monokines; D011506:Proteins; D011509:Proteoglycans; D010450:Endopeptidases