| Prostasome-like particles are involved in the transfer of P25b from the bovine epididymal fluid to the sperm surface. | |
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MedLine Citation:
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PMID: 11335953 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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G Frenette; R Sullivan |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Molecular reproduction and development Volume: 59 ISSN: 1040-452X ISO Abbreviation: Mol. Reprod. Dev. Publication Date: 2001 May |
Date Detail:
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Created Date: 2001-05-03 Completed Date: 2001-08-23 Revised Date: 2007-11-15 |
Medline Journal Info:
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Nlm Unique ID: 8903333 Medline TA: Mol Reprod Dev Country: United States |
Other Details:
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Languages: eng Pagination: 115-21 Citation Subset: IM |
Affiliation:
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Centre de Recherche en Biologie de la Reproduction and Département d'Obstétrique-Gynécologie, Faculté de Médecine, Université Laval, Ste-Foy, Canada. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cattle Cysteine Endopeptidases / metabolism* Epididymis / chemistry*, physiology Humans Hydrogen-Ion Concentration Immunoblotting Male Membrane Proteins / metabolism* Multienzyme Complexes / metabolism* Proteasome Endopeptidase Complex Spermatozoa / chemistry, metabolism* Testis / chemistry, cytology Type C Phospholipases / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Membrane Proteins; 0/Multienzyme Complexes; EC 3.1.4.-/Type C Phospholipases; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.25.1/Proteasome Endopeptidase Complex |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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