Cloning, functional characterization and localization of a rat renal na+-dicarboxylate transporter. Sekine, Takashi, Seok Ho Ch, Makoto Hosoyamada, Yoshikatsu Kanai, Nobuaki Watanabe, Yoshitake Furuta, Kuniaki Fukuda, Takashi Igarashi, and Hitoshi Endou. Kyorin University School of Medicine, Department of Pharmacology and Toxicology, Mitaka, Tokyo 181, Japan, Department of Pharmacology, Catholic University Medical College, Banpo-dong 505, Seocho-gu, Seoul 137-701, Korea, Sankyo Co., Ltd., Drug Metabolism & Pharmacokinetics IV Analytical and Metabolic Research Laboratories, Shinagawa-ku, Tokyo 140, Japan, University of Tokyo Mejirodai Campus, Department of Paediatrics, Bunkyo-ku, Tokyo 112, Japan
APStracts 5:0085F, 1998.
We report here the isolation, functional characterization, tissue distribution and membrane localization of rat renal Na+-dicarboxylate transporter (rNaDC-1). rNaDC-1 consists of 2245 nucleotides and the deduced amino acid sequence showed 73 % and 75 % identity to rabbit and human NaDC-1, respectively. When expressed in Xenopus laevis oocytes, rNaDC-1 mediated sodium-dependent uptake of di- and tri -carboxylates. Substrates of rNaDC-1 evoked inward currents in oocytes expressed with rNaDC-1; succinate, [alpha]-ketoglutarate and glutarate were relatively high affinity substrates and citrate was a low affinity substrate of rNaDC-1. The coupling ratio of citrate to charge was determined to be 1:1 at pH 7.4; influx of one positive charge per citrate molecule suggests a symport of three Na+ with a divalent citrate. Expression of rNaDC-1 mRNA was detected in the the kidney and the small and large intestines. Immunohistochemistry using polyclonal antibodies raised against the 14 amino acids at the C -terminus of rNaDC-1 revealed that rNaDC-1 is localized exclusively in the luminal membrane of S2 and S3.

Received 11 February 1998; accepted in final form 8 April 1998.
APS Manuscript Number F30-8.
Article publication pending Am. J. Physiol. (Renal Physiology).
ISSN 1080-4757 Copyright 1998 The American Physiological Society.
Published in APStracts on 24 April 1998