Molecular cloning and characterization of two novel human renal organic anion transporters (hOAT1 and hOAT3)

Joanne E. Race, Steven M. Grassl, William J. Williams, Eli J. Holtzman*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

The cloned organic anion transporters from rat, mouse, and winter flounder (rOAT1, mOAT1, fROAT) mediate the coupled exchange of α-ketoglutarate with multiple organic anions, including p-aminohippurate (PAH). We have isolated two novel gene products from human kidney which bear significant homology to the known OATs and belong to the amphiphilic solute facilitator (ASF) family. The cDNAs, hOAT1 and hOAT3, encode for 550- and 568-amino-acid residue proteins, respectively. hOAT1 and hOAT3 mRNAs are expressed strongly in kidney and weakly in brain. Both genes map to chromosome 11 region q11.7. PAH uptake by Xenopus laevis oocytes injected with hOAT1 mRNA is increased 100-fold compared to water-injected oocytes. PAH uptake is chloride dependent and is not further increased by preincubation of oocytes in 5 mM glutarate. Uptake of PAH is inhibited by probenicid, α-ketoglutarate, bumetanide, furosemide, and losartan, but not by salicylate, urate, choline, amilioride, and hydrochlorothiazide.

Original languageEnglish
Pages (from-to)508-514
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume255
Issue number2
DOIs
StatePublished - 16 Feb 1999
Externally publishedYes

Funding

FundersFunder number
American Heart Association, New York State Affiliate
Dialysis Clinics, Inc.

    Keywords

    • Homology cloning
    • Kidney
    • Organic anion transport
    • P-amino-hippurate

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