title: Renin inhibits the vasorelaxation induced by nitroso albumin.
abstract: Nitrosated proteins exhibit actions characteristic of free NO. As the vasorelaxation effect of nitrosated albumin is rapidly inactivated in plasma, we postulated that a protease could remove or modify the NO attached to albumin. We found that the ability of plasma to inactivate the vasorelaxing action of NO-bovine serum albumin (NO-BSA) is restricted to a plasma fraction containing macromolecules. We also found that a crude preparation of renal renin also inactivated the vasorelaxation action of NO-BSA and UV-spectrophotometric analysis showed that the 335-nm signal of NO-BSA was significantly decreased by renin. This decrease could be prevented by a renin inhibitor or by immunodepleting the renin preparation with a monoclonal antibody to renin. The data suggest that renin accelerates the uncoupling of NO to albumin. Such a function may be important in the control of vascular tone and blood pressure.
authors.affiliation: Department of Medicine, Columbia University, 630 West 168 Street, New York, New York, 10032, USA.
authors.forename: S
authors.initials: S
authors.lastname: Seo
authors.forename: D W
authors.initials: DW
authors.lastname: Landry
authors.forename: J A
authors.initials: JA
authors.lastname: Oliver
mesh_terms: D000818:Animals; D009603:Nitroso Compounds; D051381:Rats; D017207:Rats, Sprague-Dawley; D012083:Renin / Q000494:pharmacology*; D012710:Serum Albumin, Bovine / Q000037:antagonists & inhibitors*; D013056:Spectrophotometry, Ultraviolet; D014664:Vasodilation / Q000187:drug effects*
chemical_list: D009603:Nitroso Compounds; C091665:S-nitrosoalbumin; D012710:Serum Albumin, Bovine; D012083:Renin