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Molecular cloning, functional characterization and genomic organization of four alternatively spliced isoforms of the human organic cation transporter 1 ( hOCT1 / SLC22A1 )
Author(s) -
HAYER M.,
BÖNISCH H.,
BRÜSS M.
Publication year - 1999
Publication title -
annals of human genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.537
H-Index - 77
eISSN - 1469-1809
pISSN - 0003-4800
DOI - 10.1046/j.1469-1809.2000.6430267.x
Subject(s) - complementary dna , gene isoform , exon , organic cation transport proteins , microbiology and biotechnology , molecular cloning , gene , cloning (programming) , tandem exon duplication , biology , hek 293 cells , intron , exon trapping , alternative splicing , genetics , transporter , computer science , programming language
In this study we report the cloning of four human OCT1 ( hOCT1 / SLC22A1 ) isoforms: a long form, hOCT1G/L554, and three shorter forms (hOCT1G/L506, hOCT1G483 and hOCT1G353). All four variants could be identified in the human glioma cell line SK‐MG‐1, whereas only two isoforms (hOCT1G/L554 and hOCT1G/L506) were found in human liver cDNA. The hOCT1G/L554 represents the full length hOCT1 since the sequence of this clone is more than 99% identical to previously cloned hOCT1 cDNAs. Elucidation of the gene structure of human OCT1 demonstrated that the other isolated isoforms are alternatively spliced variants. The hOCT1 gene consists of 7 exons and 6 introns. When stably expressed in human embryonic kidney (HEK293) cells, only the full length hOCT1 cDNA mediated decynium‐22 (D22)‐sensitive uptake of tritiated 1‐methyl‐4‐phenylpyridinium ([ 3 H]‐MPP + ).