Prostasome-like particles are involved in the transfer of P25b from the bovine epididymal fluid to the sperm surface

• Published in: Molecular reproduction and development Vol. 59; no. 1; pp. 115 - 121
• Main Authors: Frenette, Gilles, Sullivan, Robert
• Format: Journal Article
• Language: English
• Published: New York John Wiley & Sons, Inc 01-05-2001; Wiley-Liss
• Subjects: Animals; Biological and medical sciences; bovine epididymis; Cattle; Cysteine Endopeptidases - metabolism; Epididymis - chemistry; Epididymis - physiology; Fundamental and applied biological sciences. Psychology; Humans; Hydrogen-Ion Concentration; Immunoblotting; Male; Mammalian male genital system; Membrane Proteins - metabolism; Morphology. Physiology; Multienzyme Complexes - metabolism; P25b; prostasome-like particles; Proteasome Endopeptidase Complex; sperm maturation; Spermatozoa - chemistry; Spermatozoa - metabolism; Testis - chemistry; Testis - cytology; Type C Phospholipases - metabolism; Vertebrates: reproduction; Membrane protein; Spermatozoa; Enzyme; Biological marker; Ox; Esterases; Male genital duct; Phosphoric diester hydrolases; Germinal cell; Male genital system; Phospholipase C; Ripening; Vertebrata; Epididymis; Mammalia; Hydrolases; Artiodactyla; Ungulata
• ISSN: 1040-452X; 1098-2795
• DOI: 10.1002/mrd.1013

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. Mol. Reprod. Dev. 59:115-121, 2001. © 2001 Wiley-Liss, Inc.