Reproduction   citetrack
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS  

Reproduction (2004) 127 601-612
DOI: 10.1530/rep.1.00062
Copyright © 2004 Society for Reproduction and Fertility
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
Services
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
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mededovic, S.
Right arrow Articles by Fraser, L. R
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mededovic, S.
Right arrow Articles by Fraser, L. R

RESEARCH

Angiotensin II stimulates cAMP production and protein tyrosine phosphorylation in mouse spermatozoa

Samra Mededovic and Lynn R Fraser

Centre for Reproduction, Endocrinology and Diabetes, School of Biomedical Sciences, King’s College London, Guy’s Campus, London Bridge, London SE1 1UL, UK

Correspondence should be addressed to L R Fraser; Email: lynn.fraser{at}kcl.ac.uk

Angiotensin II (AII), found in seminal plasma, has been shown to stimulate capacitation in uncapacitated mammalian spermatozoa. The present study investigated the location of AII receptors on spermatozoa and AII’s mechanism of action. AT1 type receptors for AII are present on the acrosomal cap region and along the whole of the flagellum of both mouse and human spermatozoa. Because combinations of low concentrations of AII and either calcitonin or fertilization-promoting peptide (FPP), both known to regulate the adenylyl cyclase (AC)/cAMP signal transduction pathway, elicited a significant response, this study investigated the hypothesis that these peptides act on the same pathway. AII was shown to significantly stimulate cAMP production in both uncapacitated and capacitated mouse spermatozoa and this was associated with increases in protein tyrosine phosphorylation. Using an anti-phosphotyrosine antibody to visualize the location of tyrosine phosphoproteins within individual cells, AII significantly stimulated phosphorylation within 20 min in both the head, especially in the acrosomal cap region, and the flagellum, especially in the principal piece, of uncapacitated mouse spermatozoa; combined AII + FPP was stimulatory within 5 min. In addition, Western blotting revealed that AII stimulation increased phosphorylation in a number of tyrosine phosphoproteins in both uncapacitated and capacitated mouse spermatozoa, with some being altered only in the latter category of cells. These results support the hypothesis that AII stimulates AC/cAMP in mammalian spermatozoa.




This article has been cited by other articles:


Home page
Hum ReprodHome page
S.A. Adeoya-Osiguwa and L. R. Fraser
Cathine, an amphetamine-related compound, acts on mammalian spermatozoa via beta1- and {alpha}2A-adrenergic receptors in a capacitation state-dependent manner
Hum. Reprod., March 1, 2007; 22(3): 756 - 765.
[Abstract] [Full Text] [PDF]


Home page
ReproductionHome page
S. Mededovic and L. R Fraser
Mechanisms of action of angiotensin II on mammalian sperm function
Reproduction, February 1, 2005; 129(2): 211 - 218.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS  
Copyright © 2004 by the Society for Reproduction and Fertility.