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Oxytocin stimulation of RGS2 mRNA expression in cultured human myometrial cells

Authors
 Eun Sung Park  ;  Clement O. Echetebu  ;  Solweig Soloff  ;  Melvyn S. Soloff 
Citation
 AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND METABOLISM, Vol.282(3) : 580-584, 2002 
Journal Title
 AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND METABOLISM 
ISSN
 0193-1849 
Issue Date
2002
MeSH
Calcimycin/pharmacology ; Cells, Cultured ; Colforsin/pharmacology ; Cyclic AMP/metabolism ; Drug Synergism ; Egtazic Acid/analogs & derivatives* ; Egtazic Acid/pharmacology ; Enzyme Activation/drug effects ; Female ; GTP-Binding Protein alpha Subunits, Gi-Go/physiology ; GTP-Binding Proteins/physiology ; Gene Expression/drug effects* ; Humans ; Inositol Phosphates/metabolism ; Ionophores/pharmacology ; Myometrium/metabolism* ; Oxytocin/pharmacology* ; Pregnancy ; Protein Kinase C/metabolism ; RGS Proteins/genetics* ; RNA, Messenger/analysis* ; Signal Transduction ; Tetradecanoylphorbol Acetate/pharmacology ; Type C Phospholipases/metabolism ; Virulence Factors, Bordetella/pharmacology
Keywords
intracellular calcium ; protein kinase C ; G proteins ; forskolinadenosine 3′,5′-cyclic monophosphate ; regulator of G protein
Abstract
Regulators of G protein signaling (RGS proteins) interact with Gαq and Gαi and accelerate GTPase activity. These proteins have been characterized only within the past few years, so our understanding of their importance is still preliminary. We examined the effect of oxytocin on RGS2 mRNA expression to help determine the role of RGS proteins in oxytocin signaling in human myometrial cells in primary culture. Oxytocin increased RGS2 mRNA concentration maximally by 1 or 2 h in a dose-dependent and agonist-specific manner. RGS2 mRNA levels were also elevated by treatment with Ca2+ ionophore, phorbol ester, or forskolin. Oxytocin's effects were completely inhibited by an intracellular Ca2+ chelator and partially blocked by a protein kinase C inhibitor, indicating that intracellular Ca2+ concentration is the primary signal for oxytocin elevation of RGS2 mRNA levels. Use of pharmacological inhibitors indicated that part of oxytocin-stimulated RGS2 mRNA expression is mediated by Gi/tyrosine kinase activities. Although oxytocin does not stimulate increases in intracellular cAMP concentration, agents that elevate intracellular cAMP concentrations and cause myometrial relaxation may possibly cause heterologous desensitization to oxytocin via RGS2 expression. These results suggest that RGS2 may be important in regulating the myometrial response to oxytocin.
Files in This Item:
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DOI
10.1152/ajpendo.00437.2001
Appears in Collections:
5. Research Institutes (연구소) > Institute for Medical Convergence (연의-생공연 메디컬융합연구소) > 1. Journal Papers
Yonsei Authors
Park, Eun Sung(박은성)
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/144743
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