Characterization of oxytocin receptors on isolated rat fat cells.
The binding of 3H-labelled neurohypophyseal nonapeptide hormone, oxytocin, to isolated rat fat cells has been measured under conditions where this compound elicits the known activation of glucose oxidation by these cells, called "insulin-like" action. Uptake by the cells of the [3H]peptide as a function of various concentrations of the hormone in the medium indicated the presence of two classes of binding sites with different apparent affinities and capacities. The sites of the first type exhibit a rather high affinity, but low capacity, for oxytocin (5 nM; 3 X 10(4) sited per cell) and appear to be saturable under a reversible process. Evaluation of dose-response relationships suggest that they may be directly related to the measured biological response (i.e. activation of the glucose to 14CO2 conversion). Competition experiments show that [3H]oxytocin binding to the cells remains constant within a large range of insulin concentrations. The apparent capacity of different hormone analogs to compete with oxytocin for binding to this class of receptors has been evaluated and compared with the measured insulin-like activity of these different compounds. The sites of the second category have significantly lower affinity, but higher capacity for oxytocin, and were found to be not saturable under the experimental conditions. [3H]Oxytocin uptake by ghosts prepared from the isolated fat cells showed striking similarities to the binding process described for whole cells, although the affinity and total capacity of the former were found to be slightly lower. The basal and adrenalin-stimulated adenylate cyclase of these fractions appeared to be unaffected by various concentrations of oxytocin. It is concluded that there may exist on the rat fat cell membranes a discrete number of oxytocin receptors possessing high specificity for oxytocin and exhibiting affinities and kinetic behaviour similar to those of other characterized oxytocin receptors. They are believed to be independent of the other hormonal receptors of the rat fact cells.
D000262:Adenylyl Cyclases / Q000378:metabolism; D000273:Adipose Tissue / Q000187:drug effects / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D005947:Glucose / Q000378:metabolism; D066298:In Vitro Techniques; D007700:Kinetics; D010121:Oxytocin / Q000378:metabolism* / Q000494:pharmacology; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D051381:Rats; D011956:Receptors, Cell Surface; D014280:Triglycerides / Q000378:metabolism
D011506:Proteins; D011956:Receptors, Cell Surface; D014280:Triglycerides; D010121:Oxytocin; D000262:Adenylyl Cyclases; D005947:Glucose