The effects of selective A1 receptor agonist on human spermatozoa were examined to verify physiological responses and to investigate the signal transduction pathway. N6-Cyclopentyladenosine on uncapacitated spermatozoa did not induce spontaneous acrosome reaction after 5 h capacitation, whereas the number of capacitated spermatozoa, assessed by lysophosphatidylcholine-induced acrosome reaction with Pisum sativum agglutinin staining, was significantly increased. N6-Cyclopentyladenosine was also added to capacitated human spermatozoa to find out whether the agonist could induce the acrosome reaction. Results, although statistically significant, could not be considered biologically significant. A1-Mediated capacitation was followed by the increase of tyrosine phosphorylation of a protein subset ranging between Mr = 200 000 and 30 000. Stimulation of A1 receptor with the selective agonist elicited an agonist-induced inositol phospholipid hydrolysis leading to a transient rise of inositol triphosphate (IP3). This increase was not induced by A1 receptor antagonist and was blocked by phospholipase C inhibitor. Coimmunoprecipitation experiments showed that the A1 receptor is coupled to Gαi2 subunit suggesting that the activation of phospholipase C is mediated by βγ subunits. In conclusion, the A1 adenosine receptor in human spermatozoa is coupled to Gαi2, signals via IP3, and affects the capacitative status of ejaculated spermatozoa.
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