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rdf:type |
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lifeskim:mentions |
umls-concept:C0004112,
umls-concept:C0010453,
umls-concept:C0020291,
umls-concept:C0031621,
umls-concept:C0033634,
umls-concept:C0206529,
umls-concept:C0443199,
umls-concept:C0600388,
umls-concept:C0851285,
umls-concept:C0871261,
umls-concept:C1704632,
umls-concept:C1706817,
umls-concept:C2911692
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pubmed:issue |
1
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pubmed:dateCreated |
2002-10-2
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pubmed:abstractText |
The metabotropic glutamate receptor 5 (mGluR5) exhibits a rapid loss of receptor responsiveness to prolonged or repeated agonist exposure. This receptor desensitization has been seen in a variety of native and recombinant systems, and is thought to result from receptor-mediated, protein kinase C (PKC)-dependent phosphorylation of the receptor, uncoupling it from the G protein in a negative feedback regulation. We have investigated the rapid PKC-mediated desensitization of mGluR5 in cortical cultured astrocytes by measuring downstream signals from activation of mGluR5. These include activation of phosphoinositide (PI) hydrolysis, intracellular calcium transients, and extracellular signal-regulated kinase 2 (ERK2) phosphorylation. We present evidence that PKC plays an important role in rapid desensitization of PI hydrolysis and calcium signaling, but not in ERK2 phosphorylation. This differential regulation of mGluR5-mediated responses suggests divergent signaling and regulatory pathways which may be important mechanisms for dynamic integration of signal cascades.
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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/3,5-dihydroxyphenylglycine,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Excitatory Amino Acid Agonists,
http://linkedlifedata.com/resource/pubmed/chemical/Glycine,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase C beta,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Metabotropic Glutamate,
http://linkedlifedata.com/resource/pubmed/chemical/Resorcinols,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/metabotropic glutamate receptor 5
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0022-3042
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
83
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
110-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12358734-Animals,
pubmed-meshheading:12358734-Astrocytes,
pubmed-meshheading:12358734-Calcium Signaling,
pubmed-meshheading:12358734-Cells, Cultured,
pubmed-meshheading:12358734-Enzyme Activation,
pubmed-meshheading:12358734-Enzyme Activators,
pubmed-meshheading:12358734-Enzyme Inhibitors,
pubmed-meshheading:12358734-Excitatory Amino Acid Agonists,
pubmed-meshheading:12358734-Glycine,
pubmed-meshheading:12358734-Hydrolysis,
pubmed-meshheading:12358734-Isoenzymes,
pubmed-meshheading:12358734-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:12358734-Phosphatidylinositols,
pubmed-meshheading:12358734-Phospholipase C beta,
pubmed-meshheading:12358734-Phosphorylation,
pubmed-meshheading:12358734-Protein Kinase C,
pubmed-meshheading:12358734-Rats,
pubmed-meshheading:12358734-Rats, Sprague-Dawley,
pubmed-meshheading:12358734-Receptors, Metabotropic Glutamate,
pubmed-meshheading:12358734-Resorcinols,
pubmed-meshheading:12358734-Signal Transduction,
pubmed-meshheading:12358734-Type C Phospholipases
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pubmed:year |
2002
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pubmed:articleTitle |
Differential regulation of metabotropic glutamate receptor 5-mediated phosphoinositide hydrolysis and extracellular signal-regulated kinase responses by protein kinase C in cultured astrocytes.
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pubmed:affiliation |
Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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