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  • Role of actin cytoskeleton in mammalian sperm capacitation and the acrosome reaction
  • Breitbart H; Cohen G; Rubinstein S
  • Reproduction 2005[Mar]; 129 (3): 263-8
  • In order to fertilize, the mammalian spermatozoa should reside in the female reproductive tract for several hours, during which they undergo a series of biochemical modifications collectively called capacitation. Only capacitated sperm can undergo the acrosome reaction after binding to the egg zona pellucida, a process which enables sperm to penetrate into the egg and fertilize it. Polymerization of globular (G)-actin to filamentous (F)-actin occurs during capacitation, depending on protein kinase A activation, protein tyrosine phosphorylation, and phospholipase D activation. F-actin formation is important for the translocation of phospholipase C from the cytosol to the sperm plasma membrane during capacitation. Prior to the occurrence of the acrosome reaction, the F-actin should undergo depolymerization, a necessary process which enables the outer acrosomal membrane and the overlying plasma membrane to come into close proximity and fuse. The binding of the capacitated sperm to the zona pellucida induces a fast increase in sperm intracellular calcium, activation of actin severing proteins which break down the actin fibers, and allows the acrosome reaction to take place.
  • |Acrosome Reaction/physiology[MESH]
  • |Actin Cytoskeleton/*metabolism[MESH]
  • |Animals[MESH]
  • |Cell Membrane/metabolism[MESH]
  • |Cyclic AMP-Dependent Protein Kinases/metabolism[MESH]
  • |Cytoskeleton/*metabolism[MESH]
  • |Humans[MESH]
  • |Male[MESH]
  • |Phospholipase D/metabolism[MESH]
  • |Protein Kinase C/metabolism[MESH]
  • |Signal Transduction/*physiology[MESH]
  • |Sperm Capacitation/physiology[MESH]
  • |Sperm-Ovum Interactions/*physiology[MESH]
  • |Spermatozoa/metabolism/*ultrastructure[MESH]

  • *{{pmid15749953}}
    *<b>[ Role of actin cytoskeleton in mammalian sperm capacitation and the acrosome reaction ]</b> Reproduction 2005; 129(3) ; 263-8 Breitbart H; Cohen G; Rubinstein S


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    263 3.129 2005