Decreased sulfotransferase SULT1C2 gene expression in DPT-induced polycystic kidney

Decreased sulfotransferase SULT1C2 gene expression in DPT-induced polycystic kidney. The pathogenesis of polycystic kidney disease (PKD) remains unclear despite the identification of the genes responsible for hereditary PKD. In this study, we investigated the alteration of gene expressions in an acq...

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Bibliographic Details
Published in:Kidney international 2002-09, Vol.62 (3), p.757-762
Main Authors: Sugimura, Kazunobu, Tanaka, Tomoaki, Tanaka, Yoshihiko, Takano, Haruna, Kanagawa, Kenji, Sakamoto, Nobuyoshi, Ikemoto, Shin-Ichi, Kawashima, Hidenori, Nakatani, Tatsuya
Format: Article
Language:English
Subjects:
2-amino-4,5-diphenylthiazole
Animals
Base Sequence
Biological and medical sciences
DNA, Complementary
DPT
Gene Expression Profiling
Kidneys
Male
Medical sciences
Mice
Molecular Sequence Data
Nephrology. Urinary tract diseases
polycystic kidney disease
Polycystic Kidney Diseases - chemically induced
Polycystic Kidney Diseases - enzymology
Polycystic Kidney Diseases - genetics
Rats
Rats, Sprague-Dawley
Sulfotransferases - genetics
SULT1C2 sulfotransferase
Thiazoles
Tumors of the urinary system
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Summary:Decreased sulfotransferase SULT1C2 gene expression in DPT-induced polycystic kidney. The pathogenesis of polycystic kidney disease (PKD) remains unclear despite the identification of the genes responsible for hereditary PKD. In this study, we investigated the alteration of gene expressions in an acquired PKD model induced by 2-amino-4,5-diphenylthiazole (DPT) using the differential display method. Kidney mRNA from a Sprague-Dawley rat fed with 1% DPT for 4 days and from a control rat was compared by the RT-PCR differential display method. Differentially expressed bands were re-amplified and subcloned. Using these subclones as probes, the changes in gene expressions were confirmed by Northern blot analysis. Subsequently, mouse kidney cDNA library was screened. The isolated 1.5-kb cDNA contained an open reading frame encoding 296 amino acids, which shared 94.3% identity with rat SULT1C2 sulfotransferase, and was considered to be its mouse ortholog (GenBank Accession No. AY005469). Mouse SULT1C2 mRNA was abundant in the kidney and stomach among normal mouse tissues. The expression of SULT1C2 mRNA was decreased in the rat kidney after DPT feeding but not in the stomach. Mouse SULT1C2 was expressed successfully using pET plasmid vector and E. coli. The recombinant 34-kD protein was capable of catalyzing the sulfation of p-nitrophenol at a Km of 3.1 mmol/L, by utilizing 3′-phosphoadenosine 5′-phosphosulfate (PAPS) as the sulfate donor. Although the physiological substrate and function of SULT1C2 have yet to be elucidated, its down-regulation could be involved in the cystic changes of tubules by decreasing the sulfation of the tubular basement membrane components.
ISSN:0085-2538
1523-1755
DOI:10.1046/j.1523-1755.2002.00512.x