Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-12-10
pubmed:abstractText
The human multidrug resistance protein (MRP) gene encodes a membrane protein involved in the ATP-dependent transport of hydrophobic compounds. We previously isolated a canalicular multispecific organic anion transporter, cMOAT1/MRP2, that belongs to the ATP binding cassette (ABC) superfamily, which is specifically expressed in liver, and cMOAT1/MRP2 is responsible for the defects in hyperbilirubinemia II/Dubin-Johnson syndrome. In this study, we isolated a new cDNA of the ABC superfamily designated cMOAT2/MRP3 that is homologous to human MRP1 and cMOAT1/MRP2: cMOAT2/MRP3 is 56% identical to MRP1 and 45% identical to cMOAT1/MRP2, respectively. Fluorescence in situ hybridization demonstrated the chromosomal locus of this gene on chromosome 17q22. The human cMOAT2 cDNA hybridized to a 6.5-kb mRNA that was mainly expressed in liver and to a lesser extent in colon, small intestine, and prostate. The cMOAT2/MRP3 gene was not overexpressed in cisplatin-resistant cell lines with increased ATP-dependent transport of cisplatin over their parental counterparts derived from human head and neck cancer and human prostatic cancer cell lines. The human cMOAT2/MRP3, a novel member of the ABC superfamily, may function as a membrane transporter in liver, colon, and prostate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 1998 Academic Press.
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
252
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
103-10
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9813153-Adenosine Triphosphate, pubmed-meshheading:9813153-Amino Acid Sequence, pubmed-meshheading:9813153-Anion Transport Proteins, pubmed-meshheading:9813153-Base Sequence, pubmed-meshheading:9813153-Carrier Proteins, pubmed-meshheading:9813153-Cisplatin, pubmed-meshheading:9813153-DNA-Binding Proteins, pubmed-meshheading:9813153-Drug Resistance, Neoplasm, pubmed-meshheading:9813153-Female, pubmed-meshheading:9813153-Humans, pubmed-meshheading:9813153-KB Cells, pubmed-meshheading:9813153-Male, pubmed-meshheading:9813153-Molecular Sequence Data, pubmed-meshheading:9813153-Multidrug Resistance-Associated Proteins, pubmed-meshheading:9813153-Organ Specificity, pubmed-meshheading:9813153-Pregnancy, pubmed-meshheading:9813153-Prostatic Neoplasms, pubmed-meshheading:9813153-Sequence Alignment, pubmed-meshheading:9813153-Sequence Homology, Amino Acid, pubmed-meshheading:9813153-Transcription, Genetic, pubmed-meshheading:9813153-Tumor Cells, Cultured
pubmed:year
1998
pubmed:articleTitle
Isolation of a novel human canalicular multispecific organic anion transporter, cMOAT2/MRP3, and its expression in cisplatin-resistant cancer cells with decreased ATP-dependent drug transport.
pubmed:affiliation
Department of Biochemistry, Kyushu University School of Medicine, Fukuoka, Maidashi, 812-8582, USA. uchiumi@biochem1.med.kyushu-u.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't