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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
2001-5-14
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pubmed:abstractText |
The Na+/H+ exchangers (NHEs) comprise a family of transporters that catalyze cell functions such as regulation of the pH and volume of a cell and epithelial absorption of Na+ and bicarbonate. Ubiquitous calcineurin B homologous protein (CHP or p22) is co-localized and co-immunoprecipitated with expressed NHE1, NHE2, or NHE3 independently of its myristoylation and Ca2+ binding, and its binding site was identified as the juxtamembrane region within the carboxyl-terminal cytoplasmic domain of exchangers. CHP binding-defective mutations of NHE1-3 or CHP depletion by injection of the competitive CHP-binding region of NHE1 into Xenopus oocytes resulted in a dramatic reduction (>90%) in the Na+/H+ exchange activity. The data suggest that CHP serves as an essential cofactor, which supports the physiological activity of NHE family members.
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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/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CBL10 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/CBL3 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/CLB2 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Calcineurin,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Slc9a2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Hydrogen Antiporter,
http://linkedlifedata.com/resource/pubmed/chemical/calcineurin B-like protein 1...,
http://linkedlifedata.com/resource/pubmed/chemical/calcium binding protein p22, rat,
http://linkedlifedata.com/resource/pubmed/chemical/growth factor-activatable Na-H...,
http://linkedlifedata.com/resource/pubmed/chemical/sodium-hydrogen exchanger 3,
http://linkedlifedata.com/resource/pubmed/chemical/sodium-hydrogen exchanger 5
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
17367-72
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11350981-Amino Acid Sequence,
pubmed-meshheading:11350981-Amino Acid Substitution,
pubmed-meshheading:11350981-Animals,
pubmed-meshheading:11350981-Arabidopsis Proteins,
pubmed-meshheading:11350981-Calcineurin,
pubmed-meshheading:11350981-Calcium-Binding Proteins,
pubmed-meshheading:11350981-Female,
pubmed-meshheading:11350981-Genes, Reporter,
pubmed-meshheading:11350981-Genetic Variation,
pubmed-meshheading:11350981-Green Fluorescent Proteins,
pubmed-meshheading:11350981-Hydrogen-Ion Concentration,
pubmed-meshheading:11350981-Lipoproteins,
pubmed-meshheading:11350981-Luminescent Proteins,
pubmed-meshheading:11350981-Membrane Proteins,
pubmed-meshheading:11350981-Models, Molecular,
pubmed-meshheading:11350981-Molecular Sequence Data,
pubmed-meshheading:11350981-Mutagenesis, Site-Directed,
pubmed-meshheading:11350981-Oocytes,
pubmed-meshheading:11350981-Protein Conformation,
pubmed-meshheading:11350981-Recombinant Proteins,
pubmed-meshheading:11350981-Sodium,
pubmed-meshheading:11350981-Sodium-Hydrogen Antiporter,
pubmed-meshheading:11350981-Transfection,
pubmed-meshheading:11350981-Xenopus laevis
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pubmed:year |
2001
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pubmed:articleTitle |
Calcineurin homologous protein as an essential cofactor for Na+/H+ exchangers.
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pubmed:affiliation |
Department of Molecular Physiology, National Cardiovascular Center Research Institute, Fujishiro-dai 5-7-1, Suita, Osaka 565-8565, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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