Stress regulation of sulfotransferases in male rat liver
Autor: | Sharon M. Baker, Smarajit Maiti, Shannon Grant, Subramanya Karanth, Carey Pope, Guangping Chen |
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Rok vydání: | 2004 |
Předmět: |
Male
medicine.medical_specialty Sulfotransferase Blotting Western Biophysics Naphthols Biochemistry Gene Expression Regulation Enzymologic Rats Sprague-Dawley chemistry.chemical_compound Cytosol Sulfation Western blot Stress Physiological Physical Conditioning Animal Internal medicine medicine Animals RNA Messenger Sulfhydryl Compounds Molecular Biology Messenger RNA Dose-Response Relationship Drug medicine.diagnostic_test Reverse Transcriptase Polymerase Chain Reaction Cell Biology Glutathione Arylsulfotransferase In vitro Rats Endocrinology Liver chemistry RNA Sulfotransferases Xenobiotic Sulfur Densitometry Hormone |
Zdroj: | Biochemical and Biophysical Research Communications. 323:235-241 |
ISSN: | 0006-291X |
DOI: | 10.1016/j.bbrc.2004.08.074 |
Popis: | Sulfotransferase (SULT) catalyzed sulfation is responsible for hormone regulation and xenobiotic detoxification. Induction of SULTs by various hormones has been reported. Stress regulation of SULTs has not been reported, however. Here we report that rat liver SULTs can be regulated by physical stress (forced running, EX) and chemical stress (the organophosphorus pesticide parathion, PS). Both EX and PS increased rat liver phenol-sulfating SULT1A1 and hydroxysteroid-sulfating SULT2A1 activities. The increase in SULT1A1 activity did not correlate with protein (Western blot) or mRNA (RT-PCR) results but correlated well with increased non-protein soluble thiols. This suggests a possible Cys modification mechanism for stress regulation of SULT1A1. In vitro studies on GSH/GSSG effects on SULT1A1 activity support this conclusion. In contrast, SULT2A1 activity following physical or chemical stress treatments correlated well with protein and mRNA levels. This suggests a stress regulation mechanism of SULT2A1 at the gene transcription level, possibly occurring via hormones. |
Databáze: | OpenAIRE |
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