- Epididyme
- Published:
Données récentes sur la maturation des spermatozoïdes dans l'épididyme humain
Andrologie volume 12, pages 52–67 (2002)
Résumé
Au cours de leur transit épididymaire, les spermatozoïdes rencontrent un environnement varié, au regard des protéines avec lesquelles ils rentrent en contract. Dans la partie proximale de l'épididyme, ils sont soumis à l'action d'enzymes, et exposés à des protéines susceptibles de modifier les membranes. Dans la partie moyenne prédomine une autre catégorie de protéines et d'enzymes; celles associées au transport de stérols pourraient modifier les membranes spermatiques afin de permettre l'ancrage de protéines de liaison à la zone pellucide: P 34H et CD52. Dans la partie distale les spermatozoïdes rencontrent des activités croissantes d'enzymes lytiques, des protéines impliquées à la fois dans la liaison à la zone pellucidé et la fusion ovocytaire, l'antigène de maturation CD 52, une activité anti-microbienne, et enfin des agents décapacitants qui facilitent leur survie avant l'éjaculation. L'adhérence des protéines aux différents domaines membranaires (comme la région antérieure ou le segment équatorial de l'acrosome) peut dépendre de la nature de la protéine, de la composition lipidique de la région membranaire concernée, et de l'environnement ionique dans la lumière épididymaire. La localisation des protéines sur le spermatozoïde, qu'il soit à acrosome intact (membrane acrosomique) ou acrosome-réagi (segment équatorial) pourra dicter leur rôle, concernant par exemple la fixation à la zona (P 34H), ou la liaison à l'ovocyte (gp 20). Les protéines comme les membranes peuvent être modifiées durant le transit épididymaire par des enzymes qui peuvent ajouter ou retirer des sucres et des peptides de la surface spermatique.
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Traduction française: Jean François GUÉRIN
Communication au XVIII° Congrès de la Société d'Andrologie de Langue Française, Montpellier, 13–15 décembre 2001.
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Cooper, T.G. Données récentes sur la maturation des spermatozoïdes dans l'épididyme humain. Androl. 12, 52–67 (2002). https://doi.org/10.1007/BF03034948
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DOI: https://doi.org/10.1007/BF03034948