Effect of polyphenolic compounds on the renal Na(+),K(+)-ATPase during the restoration of normotension after experimentally induced hypertension in rats

Exp Physiol. 2003 Jul;88(4):475-82. doi: 10.1113/eph8802553.

Abstract

It is commonly known that consumption of foods and beverages rich in polyphenols is associated with a lower incidence of cardiovascular disease. The purpose of this study was to assess whether the application of red wine polyphenols influences the kinetic properties of renal Na(+),K(+)-ATPase in rats in which hypertension has been experimentally induced by the nitric oxide synthase inhibitor L-NAME. Treatment with polyphenols during the recovery from hypertension to normotension resulted in the complete revival of the functional properties of the Na(+),K(+)-ATPase, as indicated by the total restoration of K(m), K(Na) (concentration of Na(+) necessary to achieve half-maximal reaction velocity) and V(max) for enzyme activation by ATP and/or Na(+) to pre-hypertension values. Two positive effects of polyphenols during the recovery period are indicated: a restoration of the affinity of the ATP and Na(+) binding sites to control values and a probable increase in the number of Na(+),K(+)-ATPase molecules to a level comparable to that in control conditions, as suggested by the complete renewal of V(max).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • Blood Pressure / drug effects
  • Enzyme Inhibitors
  • Flavonoids / pharmacology*
  • Hypertension / chemically induced
  • Hypertension / drug therapy*
  • Hypertension / metabolism*
  • Kidney / enzymology*
  • Kinetics
  • Male
  • NG-Nitroarginine Methyl Ester
  • Nitric Oxide Synthase / metabolism
  • Phenols / pharmacology*
  • Polyphenols
  • Rats
  • Rats, Inbred WKY
  • Sodium-Potassium-Exchanging ATPase / metabolism*

Substances

  • Enzyme Inhibitors
  • Flavonoids
  • Phenols
  • Polyphenols
  • Adenosine Triphosphate
  • Nitric Oxide Synthase
  • Sodium-Potassium-Exchanging ATPase
  • NG-Nitroarginine Methyl Ester