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Biochimica et biophysica acta

Effects of the polyamine spermine on binding of follicle-stimulating hormone to membrane-bound immature bovine testis receptors.


PMID 3004602

Abstract

The effect of the polyamine, spermine, on the interaction of human 125I-labeled FSH with membrane-bound receptors derived from bovine calf testes has been examined. Concentrations of spermine less than 0.01 M resulted in a slight but insignificant (P greater than 0.10) enhancement of FSH concentrations of 0.01 M and above caused a progressive reduction of FSH binding. Membrane receptors incubated in the presence of spermine at concentrations inhibitory to human 125I-FSH binding (0.01-0.04 M) resulted in an 8-50% decrease in the apparent FSH receptor concentration and a 10-65% decrease in the affinity constant as determined by computerized analysis of the isothermic ligand-binding data. Within the temperature range 4-20 degrees C, simultaneous addition of spermine (0.025 M) increased the reversibility of human 125I-FSH binding approx. 10% (P less than 0.005). Delayed addition of spermine (0.01-0.04 M) resulted in a dose-related dissociation of human 125I-FSH already bound to its receptor (P less than 0.05). However, preincubation of membrane receptors with spermine (0.002-0.04 M) at 4 degrees C or 34 degrees C followed by washing and addition of human 125I-FSH, resulted in an increase in hormone binding (P less than 0.05) over that of controls. If membrane receptor was incubated at 34 degrees C with spermine in the absence of radioligand, the usual loss of hormone binding was reduced (P less than 0.05), while membrane receptor incubated with spermine at 4 degrees C exhibited hormone binding greater (P less than 0.05) than that observed before treatment. Thus, the mechanism of inhibition of human 125I-FSH binding to membrane receptors appears to be correlated with an increase in reversibility of the membrane receptor-human 125I-FSH complex and is expressed as a decrease in the calculated receptor concentration and affinity constant of that interaction. Second, spermine appears to stabilize the membrane receptor in the absence of ligand, presumably through a membrane effect. These data suggest that spermine, and possibly other polyamines, which are endogenous to eukaryotic cells and undergo increases in concentration following stimulation by trophic hormone may play a role in the modulation of the ligand-membrane receptor interaction, in part, through direct effects on the membrane and/or the receptor.