|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0003075,
umls-concept:C0005528,
umls-concept:C0020792,
umls-concept:C0023547,
umls-concept:C0033554,
umls-concept:C0034693,
umls-concept:C0034721,
umls-concept:C0087063,
umls-concept:C0205314,
umls-concept:C0596902,
umls-concept:C0679622,
umls-concept:C0747055,
umls-concept:C1521991
|
|
pubmed:issue |
3
|
|
pubmed:dateCreated |
2000-10-19
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
We have isolated a rat novel multispecific organic anion transporter, moat1. The isolated clones were originated by alternative splicing of the moat1 mRNA. The nucleotide sequences predict a protein of 682 amino acids with moderate sequence similarity to LST-1, the oatp family, and the prostaglandin transporter. Northern blot analysis of rat moat1 identified a predominant transcript of 4.4 kilonucleotides in all tissues. Northern blot and in situ hybridization analyses of rat brain further indicated that moat1 mRNA is widely distributed in neuronal cells of the central nervous system, especially in the hippocampus and cerebellum. moat1 transports prostaglandin D(2) (K(m); 35.5 nM), leukotriene C(4) (K(m); 3.2 microM) and taurocholate (K(m); 17.6 microM) in a sodium-independent manner. moat1 also transports prostaglandin E(1), E(2), thromboxane B(2), and iloprost but not dehydroepiandrosterone sulfate and digoxin, of which the substrate specificity is similar, but definitively different from those of any other organic anion transporters.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Sep
|
|
pubmed:issn |
0006-291X
|
|
pubmed:author |
pubmed-author:AbeTT,
pubmed-author:AdachiHH,
pubmed-author:FujiwaraKK,
pubmed-author:IinumaKK,
pubmed-author:ItoSS,
pubmed-author:KondoYY,
pubmed-author:MatsunoSS,
pubmed-author:NakagomiRR,
pubmed-author:NakarMM,
pubmed-author:NishioTT,
pubmed-author:NunokiKK,
pubmed-author:OhtaniHH,
pubmed-author:OkabeMM,
pubmed-author:OnogawaTT,
pubmed-author:SatoEE,
pubmed-author:ShiibaKK,
pubmed-author:SuzukiMM,
pubmed-author:SuzukiTT,
pubmed-author:TanemotoMM,
pubmed-author:TokuiTT,
pubmed-author:UnnoMM
|
|
pubmed:copyrightInfo |
Copyright 2000 Academic Press.
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
7
|
|
pubmed:volume |
275
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
831-8
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:10973807-Alternative Splicing,
pubmed-meshheading:10973807-Amino Acid Sequence,
pubmed-meshheading:10973807-Animals,
pubmed-meshheading:10973807-Anion Transport Proteins,
pubmed-meshheading:10973807-Base Sequence,
pubmed-meshheading:10973807-Biological Transport,
pubmed-meshheading:10973807-Brain,
pubmed-meshheading:10973807-Carrier Proteins,
pubmed-meshheading:10973807-Cloning, Molecular,
pubmed-meshheading:10973807-In Situ Hybridization,
pubmed-meshheading:10973807-Kinetics,
pubmed-meshheading:10973807-Leukotriene C4,
pubmed-meshheading:10973807-Molecular Sequence Data,
pubmed-meshheading:10973807-Oocytes,
pubmed-meshheading:10973807-Phylogeny,
pubmed-meshheading:10973807-Prostaglandin D2,
pubmed-meshheading:10973807-RNA, Messenger,
pubmed-meshheading:10973807-Rats,
pubmed-meshheading:10973807-Substrate Specificity,
pubmed-meshheading:10973807-Taurocholic Acid,
pubmed-meshheading:10973807-Xenopus laevis
|
|
pubmed:year |
2000
|
|
pubmed:articleTitle |
Molecular identification of a rat novel organic anion transporter moat1, which transports prostaglandin D(2), leukotriene C(4), and taurocholate.
|
|
pubmed:affiliation |
Department of Neurophysiology, Tohoku University School of Medicine, Sendai, 980-8575, Japan.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
