Biol Reprod Lalor Postdoctoral Fellowships -- Application Deadline January 15, 2009
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


BOR - Papers in Press, published online ahead of print October 4, 2002.
Biol Reprod 2002, 10.1095/biolreprod.102.006684
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
67/6/1763    most recent
biolreprod.102.006684v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Métayer, S.
Right arrow Articles by Gatti, J.-L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Métayer, S.
Right arrow Articles by Gatti, J.-L.
Agricola
Right arrow Articles by Métayer, S.
Right arrow Articles by Gatti, J.-L.
Biology of Reproduction 67, 1763-1767 (2002)
DOI: 10.1095/biolreprod.102.006684 © 2002 Society for the Study of Reproduction, Inc.


Male Reproductive Tract

Germinal Angiotensin I-Converting Enzyme Is Totally Shed from the Rodent Sperm Membrane During Epididymal Maturation1

Sonia Métayera, Françoise Dacheuxa, Jean-Louis Dacheuxa, and Jean-Luc Gatti2,a

a Equipe "Spermatozoïdes," UMR 6073 INRA-CNRS, Institut National de la Recherche Agronomique, Centre de Nouzilly, 37380 Monnaie, France

Acquisition of sperm fertilizing ability is due, in part, to the reorganization of plasma membrane proteins that occurs during epididymal sperm transit. Using polyclonal antibodies against angiotensin I-converting enzyme (ACE), we showed that this enzyme is immunolocalized mainly on the middle piece of rat and mouse testicular sperm and with less intensity along the initial part of the principal piece of the flagellum. In both species, only some sperm from the caput epididymis were still reactive, whereas no labeling was observed on cauda epididymal sperm. The 105- to 110-kDa germinal ACE was absent from the rat testicular fluid but appeared in the fluid of the anterior epididymis. Thereafter, its molecular weight shifted to 94 kDa in the corpus epididymal fluid and remained at this weight in the caudal region. The 105- to 110-kDa immunoreactive protein was present in testicular rat sperm extract but was completely absent from epididymal sperm extracts. Western blot analysis of testicular and epididymal tissue extracts from the rat and mouse also confirmed that the germinal enzyme was absent from the epididymal sperm cell. Our results demonstrated that the rodent germinal ACE is released from the testicular sperm membrane when sperm enter the epididymis, a process similar to that observed in domestic mammals. This result is discussed in view of the suggested role for this enzyme in sperm fertility.

1 Supported by a grant from "Biotechnocentre-Région Centre." S.M. was the holder of a thesis grant from "Région Centre."

2 Correspondence. FAX: 33 247 427 743; gatti{at}tours.inra.fr







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2002 by the Society for the Study of Reproduction.