QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: jpet.104.065532v1 310/2/808    most recent Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Shimada, M. Articles by Yamazoe, Y. Search for Related Content PubMed PubMed Citation Articles by Shimada, M. Articles by Yamazoe, Y.

ABSORPTION, DISTRIBUTION, METABOLISM, AND EXCRETION

Unique Properties of a Renal Sulfotransferase, St1d1, in Dopamine Metabolism

Division of Drug Metabolism and Molecular Toxicology, Graduate School of Pharmaceutical Sciences, Tohoku University, Aramaki Aoba, Aoba-ku, Sendai, Japan

Although catecholamine sulfation is higher in the kidney than in the liver of mice, no detectable amounts of previously reported sulfotransferases (STs) such as St1a, St1b, St1c, and St1e were expressed in mouse kidney cytosols. A new sulfotransferase (St1d1) cDNA was isolated from kidney cDNA library of BALB/c strain by reverse transcription-polymerase chain reaction (RTPCR) using information from expressed sequence tags (EST) database. The cDNA sequence resembled that of cDNA reported previously (AA238910) (Sakakibara et al., 1998) but differed in two amino acids, ²⁰⁶Q/K and ²¹⁶Y/F, in the deduced amino acid sequence. The St1d1 expressed had unique substrate specificities for catecholamine derivatives, which preferred their deaminated metabolites rather than their parent amines. St1d1 showed the highest activity toward 3,4-dihydroxyphenylacetic acid (230.2 ± 2.69 nmol/mg/min) among the examined substrate. St1d1 protein was abundant in kidney, followed by liver, lung, and uterus. Furthermore, an addition of anti-St1d1 serum in the cytosolic reaction mixture resulted in complete inhibition of the sulfotransferase activity suggesting a major role of St1d1 on catecholamine sulfations. No human ST1D ortholog was detected at both mRNA and protein levels, although ST1A5 selectively catalyzing parent amine sulfation was detected in human kidney. These results indicate the functional basis of sulfation and the clear species difference on renal catecholamine metabolisms in mice and humans.

Address correspondence to: Dr. Miki Shimada, Division of Drug Metabolism and Molecular Toxicology, Graduate School of Pharmaceutical Sciences, Tohoku University, Aramaki Aoba, Aoba-ku, Sendai, 980-8578, Japan. E-mail: shimada{at}mail.pharm.tohoku.ac.jp.

This article has been cited by other articles:

				L. Senggunprai, K. Yoshinari, M. Shimada, and Y. Yamazoe Involvement of ST1B Subfamily of Cytosolic Sulfotransferase in Kynurenine Metabolism to Form Natriuretic Xanthurenic Acid Sulfate J. Pharmacol. Exp. Ther., December 1, 2008; 327(3): 789 - 798. [Abstract] [Full Text] [PDF]

				Y. Alnouti and C. D. Klaassen Tissue Distribution and Ontogeny of Sulfotransferase Enzymes in Mice Toxicol. Sci., October 1, 2006; 93(2): 242 - 255. [Abstract] [Full Text] [PDF]

				A. L. Niklaus and J. W. Pollard Mining the Mouse Transcriptome of Receptive Endometrium Reveals Distinct Molecular Signatures for the Luminal and Glandular Epithelium Endocrinology, July 1, 2006; 147(7): 3375 - 3390. [Abstract] [Full Text] [PDF]