B2-kinin receptor like binding in rat glomerular membranes

Biochem Biophys Res Commun. 1989 Jan 16;158(1):99-104. doi: 10.1016/s0006-291x(89)80182-2.

Abstract

Incubation of a radiolabeled bradykinin analog, [125I]-Tyr8-BK with a crude membrane preparation obtained from isolated rat glomeruli revealed a time dependent binding. The binding was saturable, reversible and was a linear function of protein membrane concentration. The radiolabeled Tyr8-BK bound to a single class of binding sites with an equilibrium dissociation constant (KD) of 3.9 +/_ 0.7 nM and a density (Bmax) of 31 +/- 5 fmol/mg protein. The BK-receptor complex was not affected by angiotensin II or by arginine vasopressin and atrial natriuretic factor. BK binding was reversed by bradykinin (Ki = 0.3 10(-9) M), and by other kinin analogs in the following order of potency: Lys-BK, Met-Lys-BK, Thi5,8-D Phe7-BK. However, Des-Arg9-BK had no effect on binding of the radiolabelled BK. These results are consistent with the presence of a B2-kinin like receptor in rat glomeruli.

MeSH terms

  • Animals
  • Binding, Competitive
  • Bradykinin / analogs & derivatives*
  • Bradykinin / metabolism
  • Cell Membrane / metabolism
  • Kidney Glomerulus / metabolism*
  • Kinetics
  • Rats
  • Rats, Inbred Strains
  • Receptors, Bradykinin
  • Receptors, Neurotransmitter / metabolism*

Substances

  • Receptors, Bradykinin
  • Receptors, Neurotransmitter
  • bradykinin, Tyr-
  • Bradykinin