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rdf:type |
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lifeskim:mentions |
umls-concept:C0001884,
umls-concept:C0024432,
umls-concept:C0025914,
umls-concept:C0026809,
umls-concept:C0132555,
umls-concept:C0205263,
umls-concept:C0311417,
umls-concept:C0747055,
umls-concept:C1524057,
umls-concept:C1709059,
umls-concept:C1709843
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pubmed:issue |
7
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pubmed:dateCreated |
1998-11-16
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pubmed:abstractText |
The influence of osmolarity and compatible organic osmolytes on the phosphorylation of the MAP-kinases Erk-1 and Erk-2 and on the expression of taurine transporter (TAUT) and lipopolysaccharide (LPS)-induced nitric oxide synthetase (iNOS) was studied in RAW 264.7 mouse macrophages. Hypoosmolarity (205 mosmol/l) but not hyperosmolarity (405 mosmol/l) or challenge of the cells with betaine or taurine increased phosphorylation of Erk-1 and Erk-2. Hypoosmotic Erk-phosphorylation was blocked by the MEK-inhibitor PD098059 but was resistant to depletion of extracellular calcium and to inhibition of PLC, PKC, erbstatin-sensitive tyrosine kinases and elevation of intracellular cAMP. Hyperosmolarity stimulated Na+-dependent taurine uptake and led to an increase of TAUT mRNA levels, whereas hypoosmotic exposure diminished both and induced a rapid efflux of the osmolyte from taurine-preloaded cells. The hyperosmotic elevation of TAUT mRNA levels was antagonized upon addition of taurine but not of betaine or myo-inositol. Hyperosmolarity increased the LPS-induced iNOS expression at the mRNA and the protein level. This was suppressed by betaine but not by taurine or myo-inositol. The osmotic regulation of taurine transport and iNOS expression appeared independent of the MEK-Erk pathway and the p38MAPK.
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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/Betaine,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Lipotropic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type II,
http://linkedlifedata.com/resource/pubmed/chemical/Nos2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Taurine,
http://linkedlifedata.com/resource/pubmed/chemical/taurine transporter
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1431-6730
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
379
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
867-74
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9705150-Animals,
pubmed-meshheading:9705150-Betaine,
pubmed-meshheading:9705150-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:9705150-Carrier Proteins,
pubmed-meshheading:9705150-Cell Line,
pubmed-meshheading:9705150-Inositol,
pubmed-meshheading:9705150-Lipopolysaccharides,
pubmed-meshheading:9705150-Lipotropic Agents,
pubmed-meshheading:9705150-Macrophages,
pubmed-meshheading:9705150-Membrane Glycoproteins,
pubmed-meshheading:9705150-Membrane Transport Proteins,
pubmed-meshheading:9705150-Mice,
pubmed-meshheading:9705150-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:9705150-Mitogen-Activated Protein Kinase 3,
pubmed-meshheading:9705150-Mitogen-Activated Protein Kinases,
pubmed-meshheading:9705150-Nitric Oxide Synthase,
pubmed-meshheading:9705150-Nitric Oxide Synthase Type II,
pubmed-meshheading:9705150-Osmolar Concentration,
pubmed-meshheading:9705150-Phosphorylation,
pubmed-meshheading:9705150-Taurine
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pubmed:year |
1998
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pubmed:articleTitle |
Compatible organic osmolytes and osmotic modulation of inducible nitric oxide synthetase in RAW 264.7 mouse macrophages.
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pubmed:affiliation |
Department of Gastroenterology, Hepatology and Infectiology, Heinrich-Heine-University, Düsseldorf, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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