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Activation of Protein Kinase C in the Lysophosphatidic Acid-Induced Bovine Sperm Acrosome Reaction and Phospholipase D1 Regulation¹

^a Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan 52900, Israel

ABSTRACT

Protein kinase C (PKC) has been implicated in the sperm acrosome reaction. In the present study, we demonstrate induction of the acrosome reaction and activation of sperm PKC by lysophosphatidic acid (LPA), which is known to induce signal transduction cascades in many cell types via binding to specific cell-surface receptors. Under conditions by which LPA activates PKC, there is significant stimulation of the acrosome reaction, which is inhibited by PKC inhibitors. Protein kinase C belongs to the Ca²⁺-dependent classical PKC family of isoforms, and indeed we show that its activation depends upon the presence of Ca²⁺ in the incubation medium. Protein kinase C is a known regulator of phospholipase D (PLD). We investigated the possible regulatory relationships between PKC and PLD1. Using specific antibodies against PLD1, we demonstrate for the first time its presence in bovine sperm. Furthermore, PLD1 coimmunoprecipitates with PKC and the PKC-PLD1 complex decomposes after treatment of the cells with LPA or 12-O-tetradecanoyl phorbol-13-acetate, resulting in the translocation of PKC to the plasma membrane and translocation of PLD1 to the particulate fraction. A possible bilateral regulation of PKC and PLD1 activation during the sperm acrosome reaction is suggested.

FOOTNOTES

First decision: 10 May 2000.

¹ This research was supported by the Israel Science Foundation funded by The Academy of Sciences and Humanities and by Ihel Foundation to H.B.

² Correspondence. FAX: 972 3 5344766; breith{at}mail.biu.ac.il

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