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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5715
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pubmed:dateCreated |
2005-3-11
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pubmed:abstractText |
The steroid hormone estrogen regulates many functionally unrelated processes in numerous tissues. Although it is traditionally thought to control transcriptional activation through the classical nuclear estrogen receptors, it also initiates many rapid nongenomic signaling events. We found that of all G protein-coupled receptors characterized to date, GPR30 is uniquely localized to the endoplasmic reticulum, where it specifically binds estrogen and fluorescent estrogen derivatives. Activating GPR30 by estrogen resulted in intracellular calcium mobilization and synthesis of phosphatidylinositol 3,4,5-trisphosphate in the nucleus. Thus, GPR30 represents an intracellular transmembrane estrogen receptor that may contribute to normal estrogen physiology as well as pathophysiology.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antisense Elements (Genetics),
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Estradiol,
http://linkedlifedata.com/resource/pubmed/chemical/Estrogen Receptor alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Estrogens,
http://linkedlifedata.com/resource/pubmed/chemical/GPER protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Estrogen,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, G-Protein-Coupled,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/phosphatidylinositol...
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
11
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pubmed:volume |
307
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1625-30
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:15705806-Animals,
pubmed-meshheading:15705806-Antisense Elements (Genetics),
pubmed-meshheading:15705806-Calcium,
pubmed-meshheading:15705806-Cell Line,
pubmed-meshheading:15705806-Cell Line, Tumor,
pubmed-meshheading:15705806-Cell Membrane,
pubmed-meshheading:15705806-Cell Nucleus,
pubmed-meshheading:15705806-Endoplasmic Reticulum,
pubmed-meshheading:15705806-Estradiol,
pubmed-meshheading:15705806-Estrogen Receptor alpha,
pubmed-meshheading:15705806-Estrogens,
pubmed-meshheading:15705806-Humans,
pubmed-meshheading:15705806-Nuclear Envelope,
pubmed-meshheading:15705806-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:15705806-Phosphatidylinositol Phosphates,
pubmed-meshheading:15705806-Protein Transport,
pubmed-meshheading:15705806-Receptor, Epidermal Growth Factor,
pubmed-meshheading:15705806-Receptors, Estrogen,
pubmed-meshheading:15705806-Receptors, G-Protein-Coupled,
pubmed-meshheading:15705806-Recombinant Fusion Proteins,
pubmed-meshheading:15705806-Signal Transduction,
pubmed-meshheading:15705806-Transfection
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pubmed:year |
2005
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pubmed:articleTitle |
A transmembrane intracellular estrogen receptor mediates rapid cell signaling.
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pubmed:affiliation |
Department of Cell Biology and Physiology, University of New Mexico Health Sciences Center, Albuquerque, NM 87131, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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