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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
2004-12-7
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pubmed:abstractText |
Heme oxygenase-1 (HO-1) is a stress response protein that protects cells against diverse noxious stimuli. Although regulation of HO-1 occurs mainly at the transcriptional level, its posttranslational modifications remain unexplored. We have identified a putative consensus sequence for phosphorylation by Akt/PKB of HO-1 at Ser188. Recombinant human and rat HO-1, but not mutant HO-1(S188A), are phosphorylated in vitro by Akt/PKB. Isotopic 32P-labeling of HEK293T cells confirmed that HO-1 is a phosphoprotein and that the basal HO-1 phosphorylation is increased by Akt1 activation. HO-1(S188D), a single point mutant equivalent to the phosphorylated protein, exhibited over 1.6-fold higher activity than wild type HO-1. Fluorescence resonance energy transfer (FRET) studies indicated that HO-1(S188D) bound to cytochrome P450 reductase (CPR) and biliverdin reductase (BVR) with a slightly lower Kd than wild-type HO-1. Although the changes in activity are small, this study provides the first evidence for a role of the survival kinase Akt in the regulation of HO-1.
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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/AKT1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Akt1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/HMOX1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase (Decyclizing),
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase-1,
http://linkedlifedata.com/resource/pubmed/chemical/Hmox1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-akt,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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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 |
3
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pubmed:volume |
578
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
90-4
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15581622-Amino Acid Sequence,
pubmed-meshheading:15581622-Animals,
pubmed-meshheading:15581622-Cell Line,
pubmed-meshheading:15581622-Consensus Sequence,
pubmed-meshheading:15581622-Enzyme Activation,
pubmed-meshheading:15581622-Fluorescence Resonance Energy Transfer,
pubmed-meshheading:15581622-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:15581622-Heme Oxygenase (Decyclizing),
pubmed-meshheading:15581622-Heme Oxygenase-1,
pubmed-meshheading:15581622-Humans,
pubmed-meshheading:15581622-Membrane Proteins,
pubmed-meshheading:15581622-Mice,
pubmed-meshheading:15581622-Molecular Sequence Data,
pubmed-meshheading:15581622-NIH 3T3 Cells,
pubmed-meshheading:15581622-Phosphorylation,
pubmed-meshheading:15581622-Point Mutation,
pubmed-meshheading:15581622-Protein-Serine-Threonine Kinases,
pubmed-meshheading:15581622-Proto-Oncogene Proteins,
pubmed-meshheading:15581622-Proto-Oncogene Proteins c-akt,
pubmed-meshheading:15581622-Rats,
pubmed-meshheading:15581622-Recombinant Proteins,
pubmed-meshheading:15581622-Second Messenger Systems,
pubmed-meshheading:15581622-Sequence Alignment
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pubmed:year |
2004
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pubmed:articleTitle |
Protein kinase Akt/PKB phosphorylates heme oxygenase-1 in vitro and in vivo.
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pubmed:affiliation |
Instituto de Investigaciones Biomedicas A. Sols UAM-CSIC and Departamento de Bioquímica, Facultad de Medicina, Universidad Autónoma de Madrid, Arzobispo Morcillo 4, Madrid 28029, Spain.
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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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