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RESEARCH PRODUCT

Genomic Structure and in Vivo Expression of the Human Organic Anion Transporter 1 (hOAT1) Gene

Bastian GunawanGerhard BurckhardtGlen ReidNatascha A. WolffAndrew BahnAnnette HillemannHans-jürgen SchultenBernhard ZabelDiana ButtlerDirk PrawittChristian EbbinghausThorsten EnklaarLazlo Füzesi

subject

Gene isoformAnion Transport ProteinsMolecular Sequence DataBiophysicsBiologyBiochemistryExonmedicineHumansGenomic libraryPromoter Regions GeneticMolecular BiologyGeneIn Situ Hybridization FluorescenceDNA PrimersGeneticsBase Sequencemedicine.diagnostic_testReverse Transcriptase Polymerase Chain ReactionChromosomes Human Pair 11Chromosome MappingPromoterDNAExonsCell BiologyTCF4Molecular biologyIntronsDNA binding siteCarrier ProteinsFluorescence in situ hybridization

description

The human organic anion transporter 1 (hOAT1) plays a key role in the secretion of an array of potentially toxic organic anions including many clinically important drugs. Here we report on the genomic cloning of hOAT1. A human genomic library was used for screening of a PAC (P1 artificial chromosome) clone applying PCR techniques. Sequencing of several restriction subclones and of a PCR-generated clone revealed that the hOAT1 gene spans 8.2 kb and is composed of 10 exons divided by 9 introns. RT-PCR studies in a human kidney specimen led to the detection of two new splice variants, hOAT1-3 and hOAT1-4, showing a 132-bp in-frame deletion. Using fluorescence in situ hybridization (FISH) we mapped the hOAT1 gene as a single signal to chromosome 11q13.1-q13.2. Additionally, 600 bp of the 5' flanking region was analyzed, illustrating the probable transcription start site at nt -280, a NF-kappaB-site at nt -397 and several putative transcription factor binding sites.

yearjournalcountryeditionlanguage
2000-08-31Biochemical and Biophysical Research Communications
https://doi.org/10.1006/bbrc.2000.3230