Document Detail


Expression and activation of Akt/protein kinase B in sexually immature and mature rat uterus.
MedLine Citation:
PMID:  15336705     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
This study investigated the expression and activation of Akt/PKB in developing and adult rat uterus. Expression of Akt was observed in uteri from adult ovariectomized and 7-35-day-old rats and no changes were observed in response to in vivo estradiol treatment (1-100 microg/100g b.w.). To examine the mechanisms of PKB/Akt activation, phosphorylation at Thr(308) and Ser(473) regulatory sites were studied in uteri. Akt was constitutively phosphorylated on Ser(473) residue in the untreated, control uteri, while phosphorylation of Thr(308) was observed only after estradiol 17beta (E2) treatment. The effects of E2 treatment were age dependent, no response was induced in 11-day-old uteri, while in 28 days and older rats the activation of Akt at both regulatory sites, Ser(473) and Thr(308), increased, the first response was detected 2h after treatment, reaching the highest rate at 6h. The rate of phosphorylation was stronger at Ser(473) residue. The results suggest that the regulation of Akt activation at two regulatory sites in rat uteri are different, phosphorylation of Thr(308) seems to be entirely estrogen dependent, while the phosphorylation of Ser(473) is regulated by other factors as well as estrogen.
Authors:
Ferenc Lengyel; Zsuzsanna Vértes; Kálmán A Kovács; József L Környei; Balázs Sumegi; Marietta Vértes
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of steroid biochemistry and molecular biology     Volume:  91     ISSN:  0960-0760     ISO Abbreviation:  J. Steroid Biochem. Mol. Biol.     Publication Date:  2004 Aug 
Date Detail:
Created Date:  2004-08-31     Completed Date:  2004-11-02     Revised Date:  2012-06-22    
Medline Journal Info:
Nlm Unique ID:  9015483     Medline TA:  J Steroid Biochem Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  285-8     Citation Subset:  IM    
Affiliation:
Institute of Physiology, Pécs University Medical School, Szigeti út 12, Pécs H7624, Hungary. ferenc.lengyel@aok.pte.hu
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MeSH Terms
Descriptor/Qualifier:
Age Distribution
Animals
Enzyme Activation / drug effects*
Estradiol / pharmacology
Female
Gene Expression Regulation, Developmental*
Ovariectomy
Phosphorylation / drug effects
Protein-Serine-Threonine Kinases / metabolism*
Proto-Oncogene Proteins / metabolism*
Proto-Oncogene Proteins c-akt
Rats
Rats, Wistar
Serine / chemistry
Threonine / chemistry
Uterus / enzymology*,  growth & development*
Chemical
Reg. No./Substance:
0/Proto-Oncogene Proteins; 50-28-2/Estradiol; 56-45-1/Serine; 72-19-5/Threonine; EC 2.7.11.1/Akt1 protein, rat; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.1/Proto-Oncogene Proteins c-akt

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


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