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Regulation of agonist-receptor binding by G proteins and divalent cations in spermatozoa solubilized A1 adenosine receptors.

Abstract：

:Solubilized A1 adenosine receptor (A1AR) was used to investigate the effect of several cations on agonist-binding characteristics and GTP hydrolysis. It was shown by Western blot with G beta-M14 that this preparation contains both G proteins and receptor. The role of the receptor molecule is to facilitate the activation of G proteins as alpha-GTP complex, and GTP hydrolysis has important consequences for the basic deactivation mechanism. Divalent cations, such as Mn2+, Ca2+, and Mg2+, potentiated the agonist-specific binding: Mn2+ had the highest apparent affinity with half-maximal effect at 50 microM. Binding assays, performed in the presence of 100 microM Mn2+, showed an increase in the apparent affinity of the binding sites, whereas, in the presence of 1 mM Mg2+, significant alteration of the apparent affinity, but not of the number of sites, was detected. Concentrations of 1 mM Mg2+ and 100 microM Mn2+ enhanced GTPase activity, whereas 5 mM Ca2+ resulted in the increase of Vmax values without significant alterations of K(m). In the presence of A1-specific agonists, Mn2+ and Mg2+ caused a decrease of Vmax values and an increase of GTP affinity. Other cations, such as Co2+, Cd2+, Cu2+, and Zn2+, inhibited the binding capacity but caused almost no changes in GTP hydrolysis kinetics.

journal_name

Mol Genet Metab

journal_title

Molecular genetics and metabolism

authors

Minelli A,Allegrucci C,Rosati R,Mezzasoma I

doi

10.1006/mgme.1997.2674

subject

Has Abstract

pub_date

1998-03-01 00:00:00

pages

183-90

issue

3

eissn

1096-7192

issn

1096-7206

pii

S1096-7192(97)92674-3

journal_volume

63

pub_type

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