| pubmed-article:17442726 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17442726 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:17442726 | lifeskim:mentions | umls-concept:C0034493 | lld:lifeskim |
| pubmed-article:17442726 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:17442726 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:17442726 | lifeskim:mentions | umls-concept:C1853261 | lld:lifeskim |
| pubmed-article:17442726 | lifeskim:mentions | umls-concept:C1853262 | lld:lifeskim |
| pubmed-article:17442726 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:17442726 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:17442726 | pubmed:dateCreated | 2007-7-9 | lld:pubmed |
| pubmed-article:17442726 | pubmed:abstractText | An electroneutral organic cation (OC)/proton exchanger in the apical membrane of proximal tubules mediates the final step of renal OC excretion. Two members of the multidrug and toxin extrusion family, MATE1 and MATE2-K, were recently identified in human and rodent kidney and proposed to be the molecular basis of renal OC/H(+) exchange. To take advantage of the comparative value of the large database on the kinetic and selectivity characteristics of OC/H(+) exchange that exists for rabbit kidney, we cloned rbMATE1 and rbMATE2-K. The rabbit homologs have 75% (MATE1) and 74% (MATE2-K) amino acid identity to their human counterparts (and 51% identity with each other). rbMATE1 and rbMATE2-K exhibited H(+) gradient-dependent uptake and efflux of tetraethylammonium (TEA) when expressed in Chinese hamster ovary cells. Both transporters displayed similar affinities for selected compounds [IC(50) values within 2-fold for TEA, 1-methyl-4-phenylpyridinium, and quinidine] and very different affinities for others (IC(50) values differing by 8- to 80-fold for choline and cimetidine, respectively). These results indicate that rbMATE1 and rbMATE2-K are multispecific OC/H(+) exchangers with similar, but distinct, functional characteristics. Overall, the selectivity of MATE1 and MATE2-K correlated closely with that observed in rabbit renal brush-border membrane vesicles. | lld:pubmed |
| pubmed-article:17442726 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17442726 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17442726 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17442726 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17442726 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17442726 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17442726 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17442726 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17442726 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:17442726 | pubmed:issn | 1931-857X | lld:pubmed |
| pubmed-article:17442726 | pubmed:author | pubmed-author:CherringtonNa... | lld:pubmed |
| pubmed-article:17442726 | pubmed:author | pubmed-author:ZhangXiaohong... | lld:pubmed |
| pubmed-article:17442726 | pubmed:author | pubmed-author:WrightStephen... | lld:pubmed |
| pubmed-article:17442726 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17442726 | pubmed:volume | 293 | lld:pubmed |
| pubmed-article:17442726 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17442726 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17442726 | pubmed:pagination | F360-70 | lld:pubmed |
| pubmed-article:17442726 | pubmed:dateRevised | 2011-4-28 | lld:pubmed |
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| pubmed-article:17442726 | pubmed:meshHeading | pubmed-meshheading:17442726... | lld:pubmed |
| pubmed-article:17442726 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17442726 | pubmed:articleTitle | Molecular identification and functional characterization of rabbit MATE1 and MATE2-K. | lld:pubmed |
| pubmed-article:17442726 | pubmed:affiliation | Dept. of Physiology, College of Medicine, University of Arizona, Tucson, AZ 85724, USA. | lld:pubmed |
| pubmed-article:17442726 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17442726 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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