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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2004-11-23
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pubmed:abstractText |
Here, we examined whether catalase binds SHP2 and alters SHP2 susceptibility to H2O2. Our results indicated that serum and fibrinogen commonly evoked catalase binding to SHP2 in HeLa and A549 cells in a herbimycin-A and TNFalpha sensitive manner. Expression of active catalase nearly 15-fold over control levels in tet-off HeLa cells substantially increased the SHP2 binding, and the catalase-associated SHP2 displayed significantly high phosphatase activities with a H2O2-resistance compared to those with little catalase. Site-directed mutagenesis at 280 abolished the binding capability of catalase to SHP2-SH2 in vitro. These results suggest that catalase-280pYIQV binds SHP2 via integrin-signaling to increase a H2O2-resistant SHP2 activity.
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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/Benzoquinones,
http://linkedlifedata.com/resource/pubmed/chemical/Catalase,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Serum-Free,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinogen,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Lactams, Macrocyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN11 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Quinones,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/herbimycin
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
577
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
327-32
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:15556604-Benzoquinones,
pubmed-meshheading:15556604-Binding Sites,
pubmed-meshheading:15556604-Catalase,
pubmed-meshheading:15556604-Cell Line, Tumor,
pubmed-meshheading:15556604-Culture Media, Serum-Free,
pubmed-meshheading:15556604-Dose-Response Relationship, Drug,
pubmed-meshheading:15556604-Drug Resistance,
pubmed-meshheading:15556604-Enzyme Inhibitors,
pubmed-meshheading:15556604-Erythrocytes,
pubmed-meshheading:15556604-Fibrinogen,
pubmed-meshheading:15556604-Glutathione Transferase,
pubmed-meshheading:15556604-HeLa Cells,
pubmed-meshheading:15556604-Humans,
pubmed-meshheading:15556604-Hydrogen Peroxide,
pubmed-meshheading:15556604-Integrins,
pubmed-meshheading:15556604-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:15556604-Kinetics,
pubmed-meshheading:15556604-Lactams, Macrocyclic,
pubmed-meshheading:15556604-Ligands,
pubmed-meshheading:15556604-Models, Biological,
pubmed-meshheading:15556604-Mutagenesis, Site-Directed,
pubmed-meshheading:15556604-Mutation,
pubmed-meshheading:15556604-Phosphoric Monoester Hydrolases,
pubmed-meshheading:15556604-Precipitin Tests,
pubmed-meshheading:15556604-Protein Binding,
pubmed-meshheading:15556604-Protein Tyrosine Phosphatase, Non-Receptor Type 11,
pubmed-meshheading:15556604-Protein Tyrosine Phosphatases,
pubmed-meshheading:15556604-Quinones,
pubmed-meshheading:15556604-Recombinant Fusion Proteins,
pubmed-meshheading:15556604-Serum,
pubmed-meshheading:15556604-Tumor Necrosis Factor-alpha
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pubmed:year |
2004
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pubmed:articleTitle |
SHP2 binds catalase and acquires a hydrogen peroxide-resistant phosphatase activity via integrin-signaling.
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pubmed:affiliation |
Department of Biochemistry, Ponce School of Medicine, Ponce, PR 00731, USA. yanos@coqui.net
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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