Renin inhibits the vasorelaxation induced by nitroso albumin Academic Article uri icon

Overview

MeSH Major

  • Renin
  • Serum Albumin, Bovine
  • Vasodilation

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.

publication date

  • September 8, 1998

Research

keywords

  • Academic Article

Identity

Language

  • eng

Digital Object Identifier (DOI)

  • 10.1006/bbrc.1998.9281

PubMed ID

  • 9735338

Additional Document Info

start page

  • 94

end page

  • 8

volume

  • 250

number

  • 1