Document Detail

Prostasome-like particles are involved in the transfer of P25b from the bovine epididymal fluid to the sperm surface.
MedLine Citation:
PMID:  11335953     Owner:  NLM     Status:  MEDLINE    
In bulls, P25b is a sperm protein associated with the plasma membrane covering the acrosome. The amount of P25b bound to a constant number of spermatozoa varies from one individual to the other, low levels being associated with bull subfertility. In this study, we describe the epididymal origin of P25b using Western blot analysis. Whereas P25b was undetectable on caput spermatozoa, the amount of P25b associated to a constant number of spermatozoa increases from the corpus to the cauda. Prostasome-like particles were prepared by ultracentrifugation of epididymal fluid. P25b appears to be also associated with those membranous vesicles in increasing amounts along the epididymis. P25b is anchored to the plasma membrane of spermatozoa through glycosylphosphatidyl-inositol as shown by the ability of phospholipase C. but not of high salt treatment, to release P25b. Coincubation experiments revealed that prostasome-like particles are able to transfer P25b to spermatozoa, this process being more efficient at slightly acidic pH. P25b thus appears to be a marker of sperm epididymal maturation in bulls.
G Frenette; R Sullivan
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular reproduction and development     Volume:  59     ISSN:  1040-452X     ISO Abbreviation:  Mol. Reprod. Dev.     Publication Date:  2001 May 
Date Detail:
Created Date:  2001-05-03     Completed Date:  2001-08-23     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  8903333     Medline TA:  Mol Reprod Dev     Country:  United States    
Other Details:
Languages:  eng     Pagination:  115-21     Citation Subset:  IM    
Centre de Recherche en Biologie de la Reproduction and Département d'Obstétrique-Gynécologie, Faculté de Médecine, Université Laval, Ste-Foy, Canada.
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MeSH Terms
Cysteine Endopeptidases / metabolism*
Epididymis / chemistry*,  physiology
Hydrogen-Ion Concentration
Membrane Proteins / metabolism*
Multienzyme Complexes / metabolism*
Proteasome Endopeptidase Complex
Spermatozoa / chemistry,  metabolism*
Testis / chemistry,  cytology
Type C Phospholipases / metabolism
Reg. No./Substance:
0/Membrane Proteins; 0/Multienzyme Complexes; EC 3.1.4.-/Type C Phospholipases; EC 3.4.22.-/Cysteine Endopeptidases; EC Endopeptidase Complex

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