High affinity binding sites for [3H]-nitrendipine in rabbit uterine smooth muscle

Life Sci. 1984 Apr 30;34(18):1717-24. doi: 10.1016/0024-3205(84)90570-8.

Abstract

The binding properties of the high affinity binding site for [3H]-nitrendipine on rabbit uteri membranes were investigated. The specific component had a dissociation constant of 0.46 +/- .07 nM and a maximal binding of 175 +/- 11 pmol/mg. A variety of other calcium channel blockers inhibited the binding of [3H]nitrendipine with varying potencies. Flunarizine demonstrated a high potency (IC50 = 0.30 microM) in inhibiting binding while verapamil and bepridil were less potent with IC50's of approximately 0.6-1.5 microM. Diltiazem did not displace nitrendipine even at very high concentrations. Verapamil displayed negative cooperative inhibition suggesting that a second site exists on uterine membranes for the binding of other calcium channel blockers.

MeSH terms

  • Animals
  • Binding Sites
  • Calcium Channel Blockers / pharmacology*
  • Cell Membrane / metabolism
  • Cinnarizine / analogs & derivatives
  • Cinnarizine / pharmacology
  • Depression, Chemical
  • Dose-Response Relationship, Drug
  • Female
  • Flunarizine
  • Muscle, Smooth / metabolism*
  • Nifedipine / analogs & derivatives*
  • Nifedipine / metabolism
  • Nifedipine / pharmacology
  • Nitrendipine
  • Rabbits
  • Uterus / metabolism
  • Verapamil / pharmacology

Substances

  • Calcium Channel Blockers
  • Cinnarizine
  • Nitrendipine
  • Verapamil
  • Nifedipine
  • Flunarizine