Document Detail


Suppression of progesterone-enhanced hyperactivation in hamster spermatozoa by estrogen.
MedLine Citation:
PMID:  20562298     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In this study, I examined whether sperm hyperactivation in hamster is regulated by steroid hormones such as estrogen (estradiol, E(2)) and progesterone. Although sperm hyperactivation was enhanced by progesterone, 17beta-estradiol (17betaE(2)) itself did not affect sperm hyperactivation. However, 17betaE(2) suppressed progesterone-enhanced hyperactivation in a concentration-dependent manner through non-genomic pathways when spermatozoa were exposed to 17betaE(2) at the same time or before exposure to progesterone. When spermatozoa were exposed to 17betaE(2) after exposure to progesterone, 17betaE(2) did not suppress progesterone-enhanced hyperactivation. Moreover, 17alpha-estradiol, an inactive isomer of E(2), did not suppress progesterone-enhanced hyperactivation. Observations using a FITC-conjugated 17betaE(2) showed that it binds to the acrosome region of the sperm head. Binding of 17betaE(2) to spermatozoa was not inhibited by progesterone, although 17betaE(2) did not suppress progesterone-enhanced hyperactivation when spermatozoa were exposed to 17betaE(2) after exposure to progesterone. On the other hand, binding of progesterone to spermatozoa was also not inhibited by 17betaE(2) even if progesterone-enhanced hyperactivation was suppressed by 17betaE(2). Although tyrosine phosphorylations of sperm proteins were enhanced by progesterone, enhancement of tyrosine phosphorylations by progesterone was suppressed by 17betaE(2). Moreover, tyrosine phosphorylations were inhibited by 17betaE(2) when only 17betaE(2) was added to the medium. From these results, it is likely that 17betaE(2) competitively suppresses progesterone-enhanced hyperactivation through the inhibition of tyrosine phosphorylations via non-genomic pathways.
Authors:
Masakatsu Fujinoki
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-06-18
Journal Detail:
Title:  Reproduction (Cambridge, England)     Volume:  140     ISSN:  1741-7899     ISO Abbreviation:  Reproduction     Publication Date:  2010 Sep 
Date Detail:
Created Date:  2010-08-30     Completed Date:  2010-12-22     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100966036     Medline TA:  Reproduction     Country:  England    
Other Details:
Languages:  eng     Pagination:  453-64     Citation Subset:  IM    
Affiliation:
Department of Physiology, School of Medicine, Dokkyo Medical University, Mibu, Tochigi 321-0293, Japan. fujinoki@dokkyomed.ac.jp
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MeSH Terms
Descriptor/Qualifier:
Acrosome / metabolism
Animals
Cricetinae
Estradiol / metabolism*
Male
Mesocricetus
Phosphorylation
Progesterone / metabolism*
Protein Binding
Protein Processing, Post-Translational
Sperm Capacitation*
Spermatozoa / metabolism*
Time Factors
Tyrosine
Chemical
Reg. No./Substance:
50-28-2/Estradiol; 55520-40-6/Tyrosine; 57-83-0/Progesterone

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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