NDLI: Mechanism of sperm capacitation and the acrosome reaction: role of protein kinases

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ickowicz, Debby Finkelstein, Maya Breitbart, Haim
Description	Country affiliation: Israel Author Affiliation: Ickowicz D ( The Mina & Everard Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan 52100, Israel.)
Abstract	Mammalian sperm must undergo a series of biochemical and physiological modifications, collectively called capacitation, in the female reproductive tract prior to the acrosome reaction (AR). The mechanisms of these modifications are not well characterized though protein kinases were shown to be involved in the regulation of intracellular $Ca^{2+}$ during both capacitation and the AR. In the present review, we summarize some of the signaling events that are involved in capacitation. During the capacitation process, phosphatidyl-inositol-3-kinase (PI3K) is phosphorylated/activated via a protein kinase A (PKA)-dependent cascade, and downregulated by protein kinase C α (PKCα). PKCα is active at the beginning of capacitation, resulting in PI3K inactivation. During capacitation, PKCα as well as PP1γ2 is degraded by a PKA-dependent mechanism, allowing the activation of PI3K. The activation of PKA during capacitation depends mainly on cyclic adenosine monophosphate (cAMP) produced by the bicarbonate-dependent soluble adenylyl cyclase. This activation of PKA leads to an increase in actin polymerization, an essential process for the development of hyperactivated motility, which is necessary for successful fertilization. Actin polymerization is mediated by $PIP_{2}$ in two ways: first, $PIP_{2}$ acts as a cofactor for phospholipase D (PLD) activation, and second, as a molecule that binds and inhibits actin-severing proteins such as gelsolin. Tyrosine phosphorylation of gelsolin during capacitation by Src family kinase (SFK) is also important for its inactivation. Prior to the AR, gelsolin is released from $PIP_{2}$ and undergoes dephosphorylation/activation, resulting in fast F-actin depolymerization, leading to the AR.
File Format	HTM / HTML
ISSN	1008682X
e-ISSN	17457262
DOI	10.1038/aja.2012.81
Journal	Asian Journal of Andrology
Issue Number	6
Volume Number	14
Language	English
Publisher	Wolters Kluwer - Medknow
Publisher Date	2012-11-01
Publisher Place	China
Access Restriction	Open
Subject Keyword	Discipline Urology Acrosome Reaction Physiology Cyclic Amp-dependent Protein Kinases Metabolism Phosphatidylinositol 3-kinases Protein Kinase C Sperm Capacitation Src-family Kinases Actins Animals Bicarbonates Calcium Gelsolin Phosphorylation Protein Kinase C-alpha Protein Processing, Post-translational Tyrosine Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Urology

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