Source:http://linkedlifedata.com/resource/pubmed/id/15288766
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8-9
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pubmed:dateCreated |
2004-8-3
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pubmed:abstractText |
Estrogen receptors act via the regulation of transcriptional processes, involving nuclear translocation and binding on specific response elements, thus leading to regulation of target gene expression. However, novel non-transcriptional mechanisms of signal transduction through steroid hormone receptors have been identified. These so-called "non-genomic" effects are independent by gene transcription or protein synthesis and involve steroid-induced modulation of cytoplasmic or of cell membrane-bound regulatory proteins. Relevant biological actions of steroids have been associated with this signaling in different tissues. Ubiquitary regulatory cascades such as mitogen-activated protein kinases (MAPK), the phosphatidylinositol 3-OH kinase (PI3K) and tyrosine kinases are modulated through non-transcriptional mechanisms by steroid hormones. Furthermore, steroid hormone receptors modulation of cell membrane-associated molecules such as ion channels and G-protein-coupled receptors has been shown in diverse tissues. The vascular wall is a site where non-genomic steroid hormones actions are particularly prominent. For instance, estrogens and glucocorticoids trigger rapid vasodilatation due to rapid induction of nitric oxide synthesis in endothelial cells via the estrogen receptor-dependent activation of MAPK and PI3K, leading to relevant pathophysiological consequences, in vitro and in vivo. The growing amount of evidence collected in the last years claims that non-transcriptional signaling mechanisms play a primary role in the generation of the effects of steroids on endothelial cells, which may turn out to be of relevance for clinical purposes.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Estrogens,
http://linkedlifedata.com/resource/pubmed/chemical/Glucocorticoids,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Estrogen,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, G-Protein-Coupled
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0039-128X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
69
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
537-42
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:15288766-Animals,
pubmed-meshheading:15288766-Cell Membrane,
pubmed-meshheading:15288766-Endothelial Cells,
pubmed-meshheading:15288766-Endothelium, Vascular,
pubmed-meshheading:15288766-Estrogens,
pubmed-meshheading:15288766-Glucocorticoids,
pubmed-meshheading:15288766-Humans,
pubmed-meshheading:15288766-Ion Channels,
pubmed-meshheading:15288766-Mitogen-Activated Protein Kinases,
pubmed-meshheading:15288766-Nitric Oxide,
pubmed-meshheading:15288766-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:15288766-Protein-Tyrosine Kinases,
pubmed-meshheading:15288766-Receptors, Estrogen,
pubmed-meshheading:15288766-Receptors, G-Protein-Coupled,
pubmed-meshheading:15288766-Signal Transduction,
pubmed-meshheading:15288766-Vasodilation
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pubmed:year |
2004
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pubmed:articleTitle |
Genomic and non-genomic effects of estrogens on endothelial cells.
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pubmed:affiliation |
Molecular and Cellular Gynecological Endocrinology Laboratory (MCGEL), Department of Reproductive Medicine and Child Development, Division of Obstetrics and Gynecology, University of Pisa, Via Roma 67, 56100 Pisa, Italy. t.simoncini@obgyn.med.unipi.it
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pubmed:publicationType |
Journal Article,
Review
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