Activation of human gingival collagenase.
To study the regulation of collagen degradation in periodontium, human gingival homogenate was incubated at 36 degrees C and the release of hydroxyproline was assayed as a measure of collagenase activity. Phenylmethylsulfonyl fluoride, soybean trypsin inhibitor and serum albumin inhibited the in vitro collagenolysis while p-aminophenylmercuric acetate, a sulfhydryl reagent, increased the degradation. When latent collagenase obtained from gingival fibroblast culture was added to the incubation a marked increase in the collagen degradation was found. This increase was prevented by phenylmethylsulfonyl fluoride. The data suggests that collagenase may exist in gingiva partly in a latent form and its activation may be brought about by 2 mechanisms. A serine proteinase present in tissue may activate collagenase by producing a limited cleavage, or the activation may occur through a reaction that involves the sulfhydryl groups of the collagenase molecule.
D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003094:Collagen / Q000378:metabolism; D004789:Enzyme Activation; D005347:Fibroblasts / Q000201:enzymology; D005881:Gingiva / Q000166:cytology / Q000201:enzymology*; D006801:Humans; D003012:Microbial Collagenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010518:Periodontitis / Q000201:enzymology*; D010662:Phenylmercuric Acetate / Q000031:analogs & derivatives / Q000494:pharmacology
C010024:4-aminophenylmercuriacetate; D003094:Collagen; D003012:Microbial Collagenase; D010662:Phenylmercuric Acetate