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- W3143655195 abstract "Proteases from human neutrophils can generate angiotensin II directly from angiotensin I or angiotensinogen. We examined whether neutrophil protease also influences angiotensin formation by activating human prorenin (also called inactive renin). When incubated with partially purified plasma and amniotic prorenin, sonicates from 10(6) neutrophils resulted in 120 +/- 30% and 1,240 +/- 290% increase in renin activity, respectively. The pH optimum of neutrophil prorenin-activating enzyme(s) is 6.5-7.0, and the activity of the enzyme(s) is inhibited by a mixture of serine protease inhibitors but not by inhibitors of other proteases, suggesting that prorenin-activating enzyme(s) is a neutral serine protease(s). Stimulation of neutrophils by f-met-leu-phe in the presence of cytochalasin B resulted in release of prorenin-activating enzyme(s) in a dose-dependent fashion. We attempted to isolate prorenin-activating enzyme(s) from neutrophil granules using aprotinin-affinity and carboxymethyl cellulose chromatograph..." @default.
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- W3143655195 date "1987-01-01" @default.
- W3143655195 modified "2023-09-24" @default.
- W3143655195 title "Human neutrophils release serine proteases capable of activating prorenin." @default.
- W3143655195 hasPublicationYear "1987" @default.
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