The alpha 1-adrenoceptor is inactivated by alterations in membrane phospholipids

Eur J Pharmacol. 1992 May 12;226(1):29-33. doi: 10.1016/0922-4106(92)90079-b.

Abstract

The influence of the membrane environment on the alpha 1-adrenoceptor has been investigated by examining the effect of phospholipase digestion on the binding of [3H]prazosin to aortic and hepatic membranes. Membrane digestion by phospholipase A2 and phospholipase C was found to markedly reduce prazosin binding to the alpha 1-adrenoceptor whereas phospholipase D had comparatively little effect. In addition, there were differences between membrane preparations since the aortic alpha 1-adrenoceptor was less sensitive to phospholipase A2 and phospholipase C than the hepatic receptor. The results support a major role for hydrophobic groups and the negatively charged, hydrophilic phosphate moiety of phospholipids in the interaction between prazosin and the alpha 1-adrenoceptor.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Aorta / metabolism
  • Binding Sites
  • Cell Membrane / chemistry
  • Liver / metabolism
  • Male
  • Membrane Lipids / chemistry*
  • Membrane Lipids / metabolism
  • Muscle, Smooth, Vascular / metabolism
  • Phospholipases A / metabolism
  • Phospholipases A2
  • Phospholipids / chemistry
  • Phospholipids / metabolism*
  • Prazosin / metabolism*
  • Rats
  • Rats, Sprague-Dawley
  • Receptors, Adrenergic, alpha / chemistry
  • Receptors, Adrenergic, alpha / metabolism*
  • Type C Phospholipases / metabolism

Substances

  • Membrane Lipids
  • Phospholipids
  • Receptors, Adrenergic, alpha
  • Phospholipases A
  • Phospholipases A2
  • Type C Phospholipases
  • Prazosin