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Decreased sulfotransferase SULT1C2 gene expression in DPT-induced polycystic kidney

Kazunobu Sugimura1, Tomoaki Tanaka, Yoshihiko Tanaka

  • 1Department of Urology, Osaka City University Medical School, 1-4-3 Asahi-machi, Abeno-ku, Osaka 545-8585, Japan. ksugimura@msic.med.osaka-cu.ac.jp

Kidney International
|August 8, 2002
PubMed
Abstract

Insights

Down-regulation of mouse sulfotransferase SULT1C2 in acquired polycystic kidney disease (PKD) may contribute to tubular changes. This study identified SULT1C2's role in a rat model, revealing its decreased expression in affected kidneys.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Polycystic kidney disease (PKD) pathogenesis remains unclear, even with identified causative genes for hereditary forms.
  • This study explores gene expression alterations in an acquired PKD model induced by 2-amino-4,5-diphenylthiazole (DPT).

Purpose of the Study:

  • To investigate gene expression changes in a DPT-induced acquired polycystic kidney disease (PKD) model.
  • To identify specific genes involved in the pathogenesis of acquired PKD.

Main Methods:

  • Utilized RT-PCR differential display to compare kidney mRNA from DPT-fed rats and control rats.
  • Confirmed differential gene expression using Northern blot analysis and screened a mouse kidney cDNA library.
  • Successfully expressed and characterized the recombinant mouse SULT1C2 protein in E. coli.

Main Results:

  • Identified a 1.5-kb cDNA as the mouse ortholog of rat SULT1C2 sulfotransferase (GenBank Accession No. AY005469).
  • Found mouse SULT1C2 mRNA abundant in normal kidney and stomach tissues.
  • Observed decreased SULT1C2 mRNA expression in the DPT-treated rat kidney but not in the stomach.
  • Demonstrated the recombinant SULT1C2 protein's sulfotransferase activity on p-nitrophenol.

Conclusions:

  • Down-regulation of SULT1C2 in the kidney may contribute to tubular cystic changes in acquired PKD.
  • This decrease could result from reduced sulfation of tubular basement membrane components.
  • Further research is needed to elucidate the physiological substrate and precise function of SULT1C2.

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