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The sperm acrosome reaction and penetration of the egg follow zona pellucida binding only if the sperm has previously undergone the poorly understood maturation process known as capacitation. We demonstrate here that in vitro capacitation of bull, ram, mouse and human sperm was accompanied by a time-dependent increase in actin polymerization. Induction of the acrosome reaction in the capacitated cells initiated fast F-actin breakdown. Incubation of sperm in media lacking bovine serum albumin or methyl-ß-cyclodextrin, Ca2+, or NaHCO3, components which are all required for capacitation, prevented actin polymerization as well as capacitation as assessed by the cells' ability to undergo acrosome reaction. Inhibition of F-actin formation by cytochalasin D blocked sperm capacitation and reduced the in vitro fertilization rate of metaphase II-arrested mouse eggs. It has been suggested that protein tyrosine phosphorylation may represent an important regulatory pathway associated with sperm capacitation. We show here that factors known to stimulate sperm protein tyrosine phosphorylation including NaHCO3, cAMP, Epidermal Growth Factor, H2O2 and Na-vanadate enhanced actin polymerization, whereas inhibition of tyrosine kinases prevented F-actin formation. These data suggest that actin polymerization may represent an important regulatory pathway associated with sperm capacitation, while F-actin breakdown occurs prior to the acrosome reaction.
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