title: Activation of the latent human neutrophil gelatinase by urea.
abstract: The mechanism of activation of the latent human neutrophil gelatinase by urea has been studied in greater detail. After dialysis of the latent gelatinase against increasing concentrations of urea a considerable increase of its activity was observed. Moreover, the results indicate a progressive conversion of the latent 94,000 Da gelatinase into a proteolytically active fragment of 80,000 Da, which was subsequently processed to a few species of lower molecular mass inactive against gelatin. This conversion was completely inhibited by EDTA, suggesting an autocatalytic reaction. The inhibition was reversed by Zn2+ or Co2+. Thus, urea alters both the enzymatic and physical characteristics of the latent gelatinase which suggests that conformational changes may induce autoactivation of the latent enzyme.
authors.affiliation: Department of Biochemistry, Institute of Rheumatology, Warszawa, Poland.
authors.forename: I
authors.initials: I
authors.lastname: Sopata
authors.forename: S
authors.initials: S
authors.lastname: Maśliński
mesh_terms: D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000187:drug effects; D018093:Gelatinases; D006801:Humans; D009504:Neutrophils / Q000187:drug effects / Q000201:enzymology*; D010434:Pepsin A / Q000378:metabolism*; D014508:Urea / Q000494:pharmacology*
chemical_list: D014508:Urea; D010434:Pepsin A; D018093:Gelatinases