Activation by cathepsin G of latent gelatinase secreted from rat polymorphonuclear leukocytes.
Rat polymorphonuclear leukocytes secrete a latent gelatinase with a molecular weight of about 96 kilodaltons (kDa). Activation of the latent 96-kDa gelatinase by cathepsin G was studied by using sodium dodecyl sulfate-substrate polyacrylamide gel electrophoresis. Cathepsin G activated the 96-kDa gelatinase by converting it to two lower molecular-weight species of 76 and 61 kDa, which were slightly different from the gelatinase species generated by treatment with 4-aminophenylmercuric acetate, an activator of latent gelatinase.
Sakata
K
K
Maeda
T
T
Nakagawa
H
H
D000818:Animals; D056649:Cathepsin G; D002403:Cathepsins / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000187:drug effects; D018093:Gelatinases; D066298:In Vitro Techniques; D008297:Male; D009504:Neutrophils / Q000187:drug effects / Q000201:enzymology*; D010434:Pepsin A / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D012697:Serine Endopeptidases
D002403:Cathepsins; D012697:Serine Endopeptidases; D056649:Cathepsin G; C534097:Ctsg protein, rat; D010434:Pepsin A; D018093:Gelatinases