Biol Reprod Track the topics, authors and articles important to you
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Luria, A.
Right arrow Articles by Breitbart, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Luria, A.
Right arrow Articles by Breitbart, H.
Agricola
Right arrow Articles by Luria, A.
Right arrow Articles by Breitbart, H.
Biology of Reproduction 66, 429-437 (2002)
© 2002 Society for the Study of Reproduction, Inc.


Regular Article

Extracellular Adenosine Triphosphate Stimulates Acrosomal Exocytosis in Bovine Spermatozoa via P2 Purinoceptor1

Ayala Luriaa, Sara Rubinsteina, Yehudit Laxa, and Haim Breitbart2,a

a Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan 52900, Israel

The presence of ATP in the genital tract fluid of mammals provokes questions regarding its function in the fertilization process. We investigated the effect of extracellular ATP (ATPe) on the activation of bovine spermatozoa. A signal transduction mechanism for ATP involving the receptor-mediated release of second messengers is described. Treatment of spermatozoa with ATP, uridine triphosphate (UTP), or 2-methylthio-ATP resulted in a concentration-dependent increase of acrosomal exocytosis, whereas treatment with either AMP or adenosine induced little exocytosis. This suggested that the receptor involved is of the P2 and not the P1 type. Several lines of evidence also suggest that the ATP purinoceptor is of the P2y and not the P2x type. First, the acrosome reaction was induced by the P2y-agonists ATP, UTP, or 2-methylthio-ATP, but no effects were shown by the P2x-agonists {alpha},ß-methylene-ATP or ß,{gamma}-methylene-ATP. Second, ATP-induced acrosomal exocytosis was inhibited by the P2y antagonists, but not by the P2x antagonists. Third, enhanced Ca2+ uptake into the cells was observed with ATP and 2-methylthio-ATP, but not with ß,{gamma}-methylene-ATP. Additionally, ATP induced elevation of intracellular Ca2+ and cAMP, and the effect on cAMP was predominantly enhanced by including Ca2+ and the Ca2+-ionophore A23187 in the incubation medium. Extracellular ATP also activates protein kinase C{alpha} (PKC{alpha}), and the acrosome reaction, stimulated by ATPe, is inhibited by a PKC-specific inhibitor. In summary, we suggest that ATPe activates the P2 purinoceptor that elevates [Ca2+]i, which leads to PKC{alpha} activation and culminates in acrosomal exocytosis.

First decision: 2 August 2001.

1 Supported by the Israel Science Foundation, funded by the Academy of Sciences and Humanities, and by Ihel Foundation to H.B.

2 Correspondence. FAX: 972 3 534 4766; breith{at}mail.biu.ac.il




This article has been cited by other articles:


Home page
Biol. Reprod.Home page
E. Rodriguez-Miranda, M. G Buffone, S. E Edwards, T. S Ord, K. Lin, M. D Sammel, G. L Gerton, S. B Moss, and C. J Williams
Extracellular Adenosine 5'-Triphosphate Alters Motility and Improves the Fertilizing Capability of Mouse Sperm
Biol Reprod, July 1, 2008; 79(1): 164 - 171.
[Abstract] [Full Text] [PDF]


Home page
Reproductive SciencesHome page
S. E. Edwards, M. G. Buffone, G. R. Knee, M. Rossato, G. Bonanni, S. Masiero, S. Ferasin, G. L. Gerton, S. B. Moss, and C. J. Williams
Effects of Extracellular Adenosine 5'-Triphosphate on Human Sperm Motility
Reproductive Sciences, October 1, 2007; 14(7): 655 - 666.
[Abstract] [PDF]


Home page
Mol Hum ReprodHome page
L. Liguori, E. de Lamirande, A. Minelli, and C. Gagnon
Various protein kinases regulate human sperm acrosome reaction and the associated phosphorylation of Tyr residues and of the Thr-Glu-Tyr motif
Mol. Hum. Reprod., March 1, 2005; 11(3): 211 - 221.
[Abstract] [Full Text] [PDF]




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