A gelatin-specific protease from hamster lung-derived cell cultures.
Gelatin-specific protease activity from hamster lung fibroblasts and their culture media is described. The fibroblasts were derived from hamster lung explant cultures. The gelatin-specific protease activity is latent and seen only after dialysis of either cells or media. The enzyme activity shares many properties of previously reported gelatinases. The activity is inhibited by EDTA, cysteine, and dithioerythritol, whereas it is not inhibited by p-chloromecuribenzoate, N-ethyl maleimide, or phenylmethylsulfonyl fluoride. Of all substrates tested, activity was observed only against gelatin and not against other substrates tested. It was inactive toward collagen, elastin, and methemoglobin. This enzyme may have a role in the digestion of collagen that has been previously cleaved by mammalian collagenase.
D000818:Animals; D002460:Cell Line; D006224:Cricetinae; D003470:Culture Media; D003545:Cysteine / Q000494:pharmacology; D003956:Dialysis; D004492:Edetic Acid / Q000494:pharmacology; D018093:Gelatinases; D008168:Lung / Q000201:enzymology*; D008647:Mesocricetus; D010434:Pepsin A / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D013379:Substrate Specificity
D003470:Culture Media; D004492:Edetic Acid; D010434:Pepsin A; D018093:Gelatinases; D003545:Cysteine