High specific gamma-aminobutyric acid binding to membranes of the human ovary

J Neurochem. 1984 May;42(5):1464-7. doi: 10.1111/j.1471-4159.1984.tb02810.x.

Abstract

The concentration of gamma-aminobutyric acid (GABA) in the human ovary and the capacity of a membrane preparation from the same organ to bind [3H]GABA specifically were examined. The GABA concentration in the ovary was found to be 214 +/- 66 nmol/g frozen tissue (mean +/- SEM of six independent determinations). Moreover, a single population of high-affinity GABA binding sites has been identified in the ovarian membranes. The apparent dissociation constant (Kd) and maximum binding capacity (Bmax) were 38.3 nM and 676 fmol/mg protein, respectively. The specific binding of [3H]GABA was displaced by muscimol, unlabelled GABA, or (+)bicuculline, but was unaffected by (+/-)baclofen and picrotoxin. The present results show that GABA and an extremely high density of GABAA receptor binding sites are present in the human ovary, indicating a physiological significance of this amino acid in the female reproductive system.

MeSH terms

  • Adult
  • Binding, Competitive
  • Cell Membrane / metabolism
  • Female
  • Humans
  • Kinetics
  • Middle Aged
  • Ovary / metabolism*
  • Receptors, Cell Surface / metabolism*
  • Receptors, GABA-A
  • gamma-Aminobutyric Acid / metabolism*

Substances

  • Receptors, Cell Surface
  • Receptors, GABA-A
  • gamma-Aminobutyric Acid