A gelatin-specific protease from hamster lung-derived cell cultures |
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Authors: | Joanne Blondin Ronald H Goldstein Carl Franzblau |
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Institution: | (1) Department of Biochemistry and Medicine, Boston University School of Medicine, 80 East Concord Street, 02118 Boston, Massachusetts |
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Abstract: | Summary 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 byp-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.
This research was supported by Program Project Grant HL-19717 from the National Heart, Lung, and Blood Institute, Grant AG
000-38-02 from the National Institute of Aging, and National Institute of Health Grant 5T32HL07035. |
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Keywords: | gelatinase lung fibroblasts collagen synthesis |
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