pubmed-article:17475902 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17475902 | lifeskim:mentions | umls-concept:C1512977 | lld:lifeskim |
pubmed-article:17475902 | lifeskim:mentions | umls-concept:C1171362 | lld:lifeskim |
pubmed-article:17475902 | lifeskim:mentions | umls-concept:C1420117 | lld:lifeskim |
pubmed-article:17475902 | lifeskim:mentions | umls-concept:C1968832 | lld:lifeskim |
pubmed-article:17475902 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
pubmed-article:17475902 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:17475902 | lifeskim:mentions | umls-concept:C1515670 | lld:lifeskim |
pubmed-article:17475902 | lifeskim:mentions | umls-concept:C1612271 | lld:lifeskim |
pubmed-article:17475902 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:17475902 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:17475902 | pubmed:dateCreated | 2007-7-20 | lld:pubmed |
pubmed-article:17475902 | pubmed:abstractText | The functional characteristics of human proton coupled folate transporter (hPCFT)/heme carrier protein (HCP) 1 were investigated. hPCFT/HCP1 expressed transiently in human embryonic kidney 293 cells mediated the transport of folate at an acidic extracellular pH of 5.5 in a manner independent of Na(+) and insensitive to membrane potential, but its transport activity was absent at near-neutral pH. Folate transport mediated by hPCFT/hHCP1 at pH 5.5 was saturable with a K(m) of 1.67 microM and extensively inhibited by reduced folates, such as folinate, 5-methyltetrahydrofolate, and methotrexate (MTX). Sulfobro-mophthalein and 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid were also found to be potent inhibitors of hPCFT/hHCP1, but hemin was found to exhibit only minimal inhibitory effect. When expressed stably as a protein fused with green fluorescent protein (GFP-hPCFT/HCP1) in MDCKII cells, GFP-hPCFT/HCP1 was mainly localized at the apical membrane, and the cellular accumulation of MTX was higher from the apical side than from the basal side. These functional features of hPCFT/HCP1 are consistent with those of the well characterized carrier-mediated folate transport system in the small intestine, suggesting that hPCFT/HCP1 is responsible for the intestinal absorption of folate and also MTX. We also found that sulfasalazine is a potent inhibitor of hPCFT/HCP1, which would interfere with the intestinal absorption of MTX when coadministered in therapy for rheumatoid arthritis as well as folate. | lld:pubmed |
pubmed-article:17475902 | pubmed:language | eng | lld:pubmed |
pubmed-article:17475902 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17475902 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17475902 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17475902 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17475902 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17475902 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17475902 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17475902 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17475902 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17475902 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17475902 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17475902 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17475902 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17475902 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17475902 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17475902 | pubmed:month | Aug | lld:pubmed |
pubmed-article:17475902 | pubmed:issn | 0022-3565 | lld:pubmed |
pubmed-article:17475902 | pubmed:author | pubmed-author:HayashiYayoiY | lld:pubmed |
pubmed-article:17475902 | pubmed:author | pubmed-author:OtagiriMasaki... | lld:pubmed |
pubmed-article:17475902 | pubmed:author | pubmed-author:YuasaHiroakiH | lld:pubmed |
pubmed-article:17475902 | pubmed:author | pubmed-author:InoueKatsuhis... | lld:pubmed |
pubmed-article:17475902 | pubmed:author | pubmed-author:AbeNaokiN | lld:pubmed |
pubmed-article:17475902 | pubmed:author | pubmed-author:NakaiYasuhiro... | lld:pubmed |
pubmed-article:17475902 | pubmed:author | pubmed-author:HatakeyamaMai... | lld:pubmed |
pubmed-article:17475902 | pubmed:author | pubmed-author:OhtaKin-yaKY | lld:pubmed |
pubmed-article:17475902 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17475902 | pubmed:volume | 322 | lld:pubmed |
pubmed-article:17475902 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17475902 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17475902 | pubmed:pagination | 469-76 | lld:pubmed |
pubmed-article:17475902 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:17475902 | pubmed:meshHeading | pubmed-meshheading:17475902... | lld:pubmed |
pubmed-article:17475902 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17475902 | pubmed:articleTitle | Functional characterization of human proton-coupled folate transporter/heme carrier protein 1 heterologously expressed in mammalian cells as a folate transporter. | lld:pubmed |
pubmed-article:17475902 | pubmed:affiliation | Department of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan. | lld:pubmed |
pubmed-article:17475902 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17475902 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
literatureCitation:1650_174... | literatureCitation:pubmed | pubmed-article:17475902 | lld:drugbank |
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