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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2008-1-9
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pubmed:abstractText |
Chemotherapeutic agents to induce DNA damage have been limited to use due to severe side effects of cardiotoxicity. ATM (Ataxia-telangiectasia mutated) is an essential protein kinase in triggering DNA damage responses. However, it is unclear how the ATM-mediated DNA damage responses are involved in the cardiac cell damage. To elucidate these functions in heart, we searched for specific substrates of ATM from mouse heart homogenate. Combining an in vitro phosphorylation following anion-exchange chromatography with purification by reverse-phase high-performance liquid chromatography (HPLC), we successfully identified p32, an ASF/SF2-associated protein, as a novel substrate for ATM. An in vitro kinase assay using recombinant p32 revealed that ATM directly phosphorylated p32. Furthermore, we determined Ser 148 of p32 as an ATM phosphorylation site. Since p32 is known to regulate mRNA splicing and transcription, p32 phosphorylation by ATM might be a new transcriptional regulatory pathway for specific DNA damage responses in heart.
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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/Antigens, CD44,
http://linkedlifedata.com/resource/pubmed/chemical/C1qbp protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoserine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ataxia telangiectasia mutated...
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1090-2104
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pubmed:author |
pubmed-author:AsanoYoshihiroY,
pubmed-author:HigoShuichiroS,
pubmed-author:HoriMasatsuguM,
pubmed-author:KatoHisakazuH,
pubmed-author:KitakazeMasafumiM,
pubmed-author:MinaminoTetsuoT,
pubmed-author:NakanoAtsushiA,
pubmed-author:OgaiAkikoA,
pubmed-author:SeguchiOsamuO,
pubmed-author:ShintaniYasunoriY,
pubmed-author:TakashimaSeijiS,
pubmed-author:YamamotoHiroyukiH,
pubmed-author:YamazakiSatoruS
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pubmed:issnType |
Electronic
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pubmed:day |
22
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pubmed:volume |
366
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
885-91
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:18070599-Amino Acid Sequence,
pubmed-meshheading:18070599-Animals,
pubmed-meshheading:18070599-Antigens, CD44,
pubmed-meshheading:18070599-Cell Cycle Proteins,
pubmed-meshheading:18070599-Cell Line,
pubmed-meshheading:18070599-Chromatography, High Pressure Liquid,
pubmed-meshheading:18070599-DNA-Binding Proteins,
pubmed-meshheading:18070599-Humans,
pubmed-meshheading:18070599-Mice,
pubmed-meshheading:18070599-Mice, Inbred C57BL,
pubmed-meshheading:18070599-Molecular Sequence Data,
pubmed-meshheading:18070599-Myocardium,
pubmed-meshheading:18070599-Nuclear Proteins,
pubmed-meshheading:18070599-Phosphorylation,
pubmed-meshheading:18070599-Phosphoserine,
pubmed-meshheading:18070599-Protein-Serine-Threonine Kinases,
pubmed-meshheading:18070599-Substrate Specificity,
pubmed-meshheading:18070599-Tumor Suppressor Proteins
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pubmed:year |
2008
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pubmed:articleTitle |
Identification of p32 as a novel substrate for ATM in heart.
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pubmed:affiliation |
Department of Cardiovascular Medicine, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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