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Human sperm proteins from testicular and epididymal origin that participate in fertilization: Modulation of sperm binding to zona‐free hamster oocytes, using monoclonal antibodies
Author(s) -
Boue Franck,
Lassalle Bruno,
Duquenne Clotilde,
Villaroya Svetlozara,
Testart Jacques,
Lefevre Anick,
Finaz Catherine
Publication year - 1992
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/mrd.1080330414
Subject(s) - epididymis , biology , sperm , hamster , monoclonal antibody , gamete , andrology , human fertilization , antibody , capacitation , zona pellucida , antigen , oocyte , microbiology and biotechnology , immunology , genetics , embryo , medicine
In order to identify human sperm surface proteins involved in the gamete recognition process, mouse monoclonal antibodies were directed against human spermatozoa and screened with live spermatozoa by enzyme‐linked immunosorbent assay (ELISA). Immunoperoxydase staining of human testis showed the early presence of four corresponding proteins on germinal cells, while six were detected primarily in testis fluid. The presence of 17 proteins was evidenced in the epididymis. Eight were detected with a decreasing gradient from the begining to the end of the organ, including vasa efferentia for three of them. The other nine were observed in only one defined segment, usually the caput epididymis, which was found to be the most active region. Comparison of spermatozoa patterns from testis, vasa efferentia, and the three regions of epididymis pointed out a progressive coating. By contrast, three antibodies displayed a migration of spermatozoa surface domains in the course of epididymal transit. Six antibodies were found to inhibit human spermatozoa adherence to zona‐free hamster oocytes, while nine promoted it. Molecular weights of antigens corresponding to nine of the antibodies ranged from 11 to 215 kDa. No correlation could be established with previously described human proteins. These observations emphasize the role of epididymis in human sperm maturation. © 1992 Wiley‐Liss, Inc.