[Do phospholipases, key enzymes in sperm physiology, represent therapeutic challenges?]

Med Sci (Paris). 2012 May;28(5):512-8. doi: 10.1051/medsci/2012285016. Epub 2012 May 30.
[Article in French]

Abstract

The spermatozoon is one of the most differentiated cells in mammals and its production requires an extremely complex machinery. Subtle but critical molecular changes take place during capacitation, which comprises the last series of maturation steps that naturally occur between the cauda epididymidis where spermatozoa are stored and their ultimate destination inside the oocyte. Phospholipases, by hydrolyzing various phospholipids, have been found to be critical in sperm processes such as 1) the control of flagellum beats, 2) capacitation - the molecular transformations preparing the sperm for fertilization, 3) acrosome reaction and 4) oocyte activation by eliciting calcium oscillations. The emerging important role of phospholipases is also emphasized by the fact that alterations of sperm lipids can lead to infertility. Phospholipases may represent valuable targets to develop anti- and pro-fertility drugs. Results obtained in mice are encouraging, since treatment of sperm with recombinant sPLA(2) of group X, known to be involved in capacitation, improves fertilization in vitro, while co-injection of PLCζ RNA with infertile sperm restores oocyte activation.

Publication types

  • Evaluation Study
  • Review

MeSH terms

  • Acrosome Reaction / genetics
  • Acrosome Reaction / physiology
  • Animals
  • Embryo, Mammalian / enzymology
  • Embryo, Mammalian / metabolism
  • Humans
  • Infertility, Male / etiology
  • Infertility, Male / metabolism
  • Infertility, Male / therapy*
  • Male
  • Mice
  • Models, Biological
  • Molecular Targeted Therapy / methods*
  • Phospholipases / antagonists & inhibitors
  • Phospholipases / genetics
  • Phospholipases / metabolism
  • Phospholipases / physiology*
  • Sperm Motility / genetics
  • Sperm Motility / physiology
  • Spermatozoa / enzymology*
  • Spermatozoa / physiology*

Substances

  • Phospholipases