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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2001-7-17
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pubmed:abstractText |
Nitric oxide synthase-2 (NOS2) is responsible for high-output nitric oxide production important in renal inflammation and injury. Using a yeast two-hybrid assay, we identified Rac2, a Rho GTPase member, as a NOS2-interacting protein. NOS2 and Rac2 proteins coimmunoprecipitated from activated RAW 264.7 macrophages. The two proteins colocalized in an intracellular compartment of these cells. Glutathione-S-transferase (GST) pull-down assays revealed that both Rac1 and Rac2 associated with GST-NOS2 and that the NOS2 oxygenase domain was necessary and sufficient for the interaction. [(35)S]methionine-labeled NOS2 interacted directly with GST-Rac2 in the absence of GTP, calmodulin, or NOS2 substrates or cofactors. Stable overexpression of Rac2 in RAW 264.7 cells augmented LPS-induced nitrite generation (~60%) and NOS2 activity (~45%) without measurably affecting NOS2 protein abundance and led to a redistribution of NOS2 to a high-speed Triton X-100-insoluble fraction. We conclude that Rac1 and Rac2 physically interact with NOS2 in activated macrophages and that the interaction with Rac2 correlates with a posttranslational stimulation of NOS2 activity and likely its spatial redistribution within the cell.
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pubmed:grant |
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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/Guanosine Triphosphate,
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/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxides,
http://linkedlifedata.com/resource/pubmed/chemical/rac GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/rac1 GTP-Binding Protein,
http://linkedlifedata.com/resource/pubmed/chemical/rac2 GTP-binding protein
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1931-857X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
281
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
F326-36
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pubmed:dateRevised |
2011-4-28
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pubmed:meshHeading |
pubmed-meshheading:11457725-Animals,
pubmed-meshheading:11457725-Cell Fractionation,
pubmed-meshheading:11457725-Cell Line,
pubmed-meshheading:11457725-Guanosine Triphosphate,
pubmed-meshheading:11457725-Macrophage Activation,
pubmed-meshheading:11457725-Macrophages,
pubmed-meshheading:11457725-Mice,
pubmed-meshheading:11457725-Nitric Oxide Synthase,
pubmed-meshheading:11457725-Nitric Oxide Synthase Type II,
pubmed-meshheading:11457725-Precipitin Tests,
pubmed-meshheading:11457725-Protein Binding,
pubmed-meshheading:11457725-Protein Isoforms,
pubmed-meshheading:11457725-Protein Structure, Tertiary,
pubmed-meshheading:11457725-Recombinant Fusion Proteins,
pubmed-meshheading:11457725-Superoxides,
pubmed-meshheading:11457725-Two-Hybrid System Techniques,
pubmed-meshheading:11457725-rac GTP-Binding Proteins,
pubmed-meshheading:11457725-rac1 GTP-Binding Protein
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pubmed:year |
2001
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pubmed:articleTitle |
Specific association of nitric oxide synthase-2 with Rac isoforms in activated murine macrophages.
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pubmed:affiliation |
Department of Internal Medicine, The University of Texas Medical School at Houston, Houston, Texas 77030, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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