Role of protein kinase C in the acrosome reaction of mammalian spermatozoa.

Abstract

Mammalian spermatozoa undergo a Ca(2+)-dependent exocytotic event before fertilization which is known as the acrosome reaction. The process of exocytosis in several cell systems is mediated by a protein kinase C (PKC)-catalysed phosphorylation. Addition of phorbol 12-myristate-13-acetate or the membrane-permeant diacylglycerol analogue 1-oleoyl-2-acetylglycerol, which are potent activators of PKC, to bovine spermatozoa resulted in stimulation of the acrosome reaction. This stimulation was inhibited by low concentrations (50% inhibition at 0.7 nM) of the PKC inhibitor staurosporine. PKC specific activity in bovine spermatozoa is extremely low in comparison with other cells; however, it is comparable with the activity found in human spermatozoa. Immunohistochemical analysis using anti-PKC antibodies revealed staining in the equatorial segment, the post-acrosomal region and the upper region of the head. We propose that PKC is involved in the mammalian sperm acrosome reaction.

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@article{Breitbart1992RoleOP, title={Role of protein kinase C in the acrosome reaction of mammalian spermatozoa.}, author={Haim Breitbart and Jeffrey R. Lax and Ronit Rotem and Zvi Naor}, journal={The Biochemical journal}, year={1992}, volume={281 ( Pt 2)}, pages={473-6} }