HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Steffgen, J. Articles by Wolff, N. A. Search for Related Content PubMed PubMed Citation Articles by Steffgen, J. Articles by Wolff, N. A. Social Bookmarking                      What's this?

J Biol Chem, Vol. 274, Issue 29, 20191-20196, July 16, 1999

Expression Cloning and Characterization of a Novel Sodium-Dicarboxylate Cotransporter from Winter Flounder Kidney

From the Abteilung Nephrologie und Rheumatologie, Georg-August-Universität Göttingen, Robert-Koch-Strasse 40, D-37075 Göttingen, Germany and the ^§ Abteilung Vegetative Physiologie und Pathophysiologie, Georg-August-Universität Göttingen, Humboldtallee 23, D-37073 Göttingen, Germany

A cDNA coding for a Na⁺-dicarboxylate cotransporter, fNaDC-3, from winter flounder (Pseudopleuronectes americanus) kidney was isolated by functional expression in Xenopus laevis oocytes. The fNaDC-3 cDNA is 2384 nucleotides long and encodes a protein of 601 amino acids with a calculated molecular mass of 66.4 kDa. Secondary structure analysis predicts at least eight membrane-spanning domains. Transport of succinate by fNaDC-3 was sodium-dependent, could be inhibited by lithium, and evoked an inward current. The apparent affinity constant (K_m) of fNaDC-3 for succinate of 30 µM resembles that of Na⁺-dicarboxylate transport in the basolateral membrane of mammalian renal proximal tubules. The substrates specific for the basolateral transporter, 2,3-dimethylsuccinate and cis-aconitate, not only inhibited succinate uptake but also evoked inward currents, proving that they are transported by fNaDC-3. Succinate transport via fNaDC-3 decreased by lowering pH, as did citrate transport, although much more moderately. These characteristics suggest that fNaDC-3 is a new type of Na⁺-dicarboxylate transporter that most likely corresponds to the Na⁺-dicarboxylate cotransporter in the basolateral membrane of mammalian renal proximal tubules.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				X.-Y. Bai, X. Chen, A.-Q. Sun, Z. Feng, K. Hou, and B. Fu Membrane topology structure of human high-affinity, sodium-dependent dicarboxylate transporter FASEB J, August 1, 2007; 21(10): 2409 - 2417. [Abstract] [Full Text] [PDF]

				Y. Hagos, J. Steffgen, A. N. Rizwan, D. Langheit, A. Knoll, G. Burckhardt, and B. C. Burckhardt Functional roles of cationic amino acid residues in the sodium-dicarboxylate cotransporter 3 (NaDC-3) from winter flounder Am J Physiol Renal Physiol, December 1, 2006; 291(6): F1224 - F1231. [Abstract] [Full Text] [PDF]

				J. A. Hall and A. M. Pajor Functional Characterization of a Na+-Coupled Dicarboxylate Carrier Protein from Staphylococcus aureus J. Bacteriol., August 1, 2005; 187(15): 5189 - 5194. [Abstract] [Full Text] [PDF]

				S. H. Wright and W. H. Dantzler Molecular and Cellular Physiology of Renal Organic Cation and Anion Transport Physiol Rev, July 1, 2004; 84(3): 987 - 1049. [Abstract] [Full Text] [PDF]

				S. Aruga, A. M. Pajor, K. Nakamura, L. Liu, O. W. Moe, P. A. Preisig, and R. J. Alpern OKP cells express the Na-dicarboxylate cotransporter NaDC-1 Am J Physiol Cell Physiol, July 1, 2004; 287(1): C64 - C72. [Abstract] [Full Text] [PDF]

				Y. Hagos, B. C. Burckhardt, A. Larsen, C. Mathys, T. Gronow, A. Bahn, N. A. Wolff, G. Burckhardt, and J. Steffgen Regulation of sodium-dicarboxylate cotransporter-3 from winter flounder kidney by protein kinase C Am J Physiol Renal Physiol, January 1, 2004; 286(1): F86 - F93. [Abstract] [Full Text] [PDF]

				N. A. Wolff, K. Thies, N. Kuhnke, G. Reid, B. Friedrich, F. Lang, and G. Burckhardt Protein Kinase C Activation Downregulates Human Organic Anion Transporter 1-Mediated Transport through Carrier Internalization J. Am. Soc. Nephrol., August 1, 2003; 14(8): 1959 - 1968. [Abstract] [Full Text] [PDF]

				B. C. Burckhardt, B. Drinkuth, C. Menzel, A. Konig, J. Steffgen, S. H. Wright, and G. Burckhardt The Renal Na+-Dependent Dicarboxylate Transporter, NaDC-3, Translocates Dimethyl- and Disulfhydryl-Compounds and Contributes to Renal Heavy Metal Detoxification J. Am. Soc. Nephrol., November 1, 2002; 13(11): 2628 - 2638. [Abstract] [Full Text] [PDF]

				F. Knauf, B. Rogina, Z. Jiang, P. S. Aronson, and S. L. Helfand Functional characterization and immunolocalization of the transporter encoded by the life-extending gene Indy PNAS, October 29, 2002; 99(22): 14315 - 14319. [Abstract] [Full Text] [PDF]

				N. A. WOLFF, B. GRUNWALD, B. FRIEDRICH, F. LANG, S. GODEHARDT, and G. BURCKHARDT Cationic Amino Acids Involved in Dicarboxylate Binding of the Flounder Renal Organic Anion Transporter J. Am. Soc. Nephrol., October 1, 2001; 12(10): 2012 - 2018. [Abstract] [Full Text] [PDF]