Abstract
Five distinct organic anion transporter cDNAs, hOAT1-5, were isolated from human liver and kidney. hOAT1, 2, and 3 are homologous to their respective rat orthologues OAT1-3, whereas hOAT4 and 5 are novel clones that have not been identified in other species. hOAT1- and hOAT3-transfected cells showed uptake of p-aminohippurate and fluorescein. Cells expressing hOAT2 showed uptake of p-aminohippurate, methotrexate, cAMP, and alpha-ketoglutarate. Northern blot analysis indicated differential tissue distribution for the transporter transcripts. These results indicate the existence of a family of organic anion transporting proteins in humans distinct from the oatp-like family of transporters.
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Anion Transport Proteins
-
Carrier Proteins / genetics*
-
Carrier Proteins / isolation & purification*
-
Carrier Proteins / metabolism
-
Cell Line
-
Cloning, Molecular
-
Cyclic AMP / metabolism
-
DNA, Complementary / genetics
-
DNA, Complementary / isolation & purification
-
Female
-
Humans
-
In Vitro Techniques
-
Ketoglutaric Acids / metabolism
-
Kidney / metabolism*
-
Liver / metabolism*
-
Methotrexate / metabolism
-
Molecular Sequence Data
-
Oocytes / metabolism
-
Organic Anion Transporters*
-
Organic Anion Transporters, Sodium-Independent*
-
RNA, Messenger / genetics
-
RNA, Messenger / metabolism
-
Rats
-
Sequence Homology, Amino Acid
-
Species Specificity
-
Transfection
-
Xenopus laevis
-
p-Aminohippuric Acid / metabolism
Substances
-
Anion Transport Proteins
-
Carrier Proteins
-
DNA, Complementary
-
Ketoglutaric Acids
-
Organic Anion Transporters
-
Organic Anion Transporters, Sodium-Independent
-
RNA, Messenger
-
SLC22A10 protein, human
-
SLC22A11 protein, human
-
Cyclic AMP
-
p-Aminohippuric Acid
-
Methotrexate