Premium
Activation of human gingival collagenase
Author(s) -
Uitto V.J.,
Elliot I.,
Robinson P. J.
Publication year - 1984
Publication title -
journal of oral pathology and medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.887
H-Index - 83
eISSN - 1600-0714
pISSN - 0904-2512
DOI - 10.1111/j.1600-0714.1984.tb01441.x
Subject(s) - collagenase , phenylmethylsulfonyl fluoride , chemistry , biochemistry , fibroblast , hydroxyproline , trypsin , in vitro , microbiology and biotechnology , enzyme , serine , biology
To study the regulation of collagen degradation in periodontium, human gingival homogenate was incubated at 36°C and the release of hydroxyproline was assayed as a measure of collagenase activity. Phenylmethylsulfonyl fluoride, soybean trypsin inhibitor and scrum albumin inhibited the in vitro collagenolysis while p‐aminophenylmcreuric 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 clevage, or the activation may occur through a reaction that involves the sulfhydryl groups of the collagenase molecule.