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The Identification of Mouse Sperm-Surface-Associated Proteins and Characterization of Their Ability to Act as Decapacitation Factors
Ist Teil von
Biology of reproduction, 2006-02, Vol.74 (2), p.275-287
Ort / Verlag
Madison, WI: Society for the Study of Reproduction
Erscheinungsjahr
2006
Link zum Volltext
Quelle
MEDLINE
Beschreibungen/Notizen
Mammalian spermatozoa must undergo capacitation before acquiring the ability to fertilize the oocyte. This process is believed
to be initiated following the release of surface-associated decapacitation factors that are elaborated by both the epididymis
and the male accessory organs. Herein, we report the identification of a number of proteins that are actively released from
the surface of mouse spermatozoa during capacitation in vitro. As anticipated, the addition of these factors back to suspensions
of mouse spermatozoa was shown to suppress several correlates of the capacitation process. Specifically, they induced a significant,
dose-dependent inhibition of the ability of spermatozoa to undergo a progesterone-induced acrosome reaction and to bind to
the zona pellucida in vitro. Inhibition of these functions was associated with the suppression of tyrosine phosphorylation
in the sperm plasma membrane but had no effect on the phosphorylation of internal proteins in either the sperm head or tail.
This inhibitory activity was attributed to a subset of the isolated proteins compromising at least four putative decapacitation
factors. These proteins were identified via tandem-mass spectrometry amino acid sequence analysis as plasma membrane fatty
acid binding protein, cysteine-rich secretory protein 1 (CRISP1), phosphatidylethanolamine binding protein 1 (PBP), and an
unnamed protein product that we have termed decapacitation factor 10 (DF10). Of these proteins, PBP was identified as a primary
candidate for a decapacitation factor.
Abstract
Analysis of proteins released from the surface of capacitating murine spermatozoa identified 4 proteins one of which, phosphatidylethanolamine
binding protein-1, exhibited properties consistent with a decapacitating factor.