Ethanol up-regulates phenol sulfotransferase (SULT1A1) and hydroxysteroid sulfotransferase (SULT2A1) in rat liver and intestine
被引:16
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作者:
Maiti, Smarajit
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机构:
Oklahoma State Univ, Ctr Vet Hlth Sci, Dept Physiol Sci, Stillwater, OK 74078 USA
Agricure Biotech Res Soc, Midnapore, W Bengal, IndiaOklahoma State Univ, Ctr Vet Hlth Sci, Dept Physiol Sci, Stillwater, OK 74078 USA
Maiti, Smarajit
[1
,2
]
Chen, Guangping
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机构:
Oklahoma State Univ, Ctr Vet Hlth Sci, Dept Physiol Sci, Stillwater, OK 74078 USAOklahoma State Univ, Ctr Vet Hlth Sci, Dept Physiol Sci, Stillwater, OK 74078 USA
Chen, Guangping
[1
]
机构:
[1] Oklahoma State Univ, Ctr Vet Hlth Sci, Dept Physiol Sci, Stillwater, OK 74078 USA
[2] Agricure Biotech Res Soc, Midnapore, W Bengal, India
Ethanol regulation;
Hep G2 cells;
protein expression;
rat liver and intestine;
sulfotransferases;
HUMAN CYTOSOLIC SULFOTRANSFERASES;
INDUCIBLE STEROID SULFOTRANSFERASE;
X-RECEPTOR PXR;
RETINOIC ACID;
ALCOHOL-CONSUMPTION;
NUCLEAR RECEPTOR;
IN-VITRO;
DEHYDROEPIANDROSTERONE SULFOTRANSFERASE;
METABOLIC SYNDROME;
BRASSICA-NAPUS;
D O I:
10.3109/13813455.2014.992440
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
Ethanol-consumption impairs physiological-efficiency/endurance, expedites senescence. Impaired-regulations of steroids/biomolecules link these processes. Steroids are catabolized by cytosolic-sulfotransferases (SULTs). Ethanol-induction of eukaryotic-SULTs-expression is scanty. Plant (Brassica-napus) steroid-sulfotransferase; BNST3/BNST4 (gene/BNST) is highly ethanol-inducible (protein/mRNA). Resembling mammalian-SULTs catalytic-mechanism BNSTs show broad substrate-specificities (mammalian-steroids; estradiol/dehydroepiandrosterone/pregnanolone). Recently, ethanol-regulation of SULTs-expression is verified in rat liver/intestine/cultured human-hepatocarcinoma (Hep-G2) cells at enzyme-activity/protein-expression (Western-blot) level. Here, two week's ethanol ingestion by male rat significantly increased SULT2A1 in their liver/intestine (p<0.05-p<0.001) and phenol-sulfotransferase (SULT1A1) in intestine (p<0.001) at enzyme-activity/protein levels. In human cells, ethanol significantly (2-fold) increased hSULT1A1/hSULT1E (2-3 fold) protein expressions paralleling their enzymatic-activities (p<0.05-p<0.01). The earlier finding of alcohol-association to the physiological impairment may be corroborated by our present findings. Inductions of SULT-expressions by ethanol have significant physiological/pharmacological consequences.
机构:
Alma Coll, Dept Biochem, 614 W Super St, Alma, MI 48801 USAAlma Coll, Dept Biochem, 614 W Super St, Alma, MI 48801 USA
Beckmann, Joe D.
Chodavarapu, Sundari
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Alma Coll, Dept Biochem, 614 W Super St, Alma, MI 48801 USA
Nivagen Pharmaceut Inc, 1920 5th St, Davis, CA 95616 USAAlma Coll, Dept Biochem, 614 W Super St, Alma, MI 48801 USA
Chodavarapu, Sundari
Doyle, Brian
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机构:
Alma Coll, Dept Biochem, 614 W Super St, Alma, MI 48801 USAAlma Coll, Dept Biochem, 614 W Super St, Alma, MI 48801 USA
机构:
Dept. Mole. Pharmacol./Exper. Ther., Mayo Medical School-Mayo, Clinic-Mayo Foundation, RochesterDept. Mole. Pharmacol./Exper. Ther., Mayo Medical School-Mayo, Clinic-Mayo Foundation, Rochester
Thomae B.A.
Eckloff B.W.
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机构:
Dept. Mole. Pharmacol./Exper. Ther., Mayo Medical School-Mayo, Clinic-Mayo Foundation, RochesterDept. Mole. Pharmacol./Exper. Ther., Mayo Medical School-Mayo, Clinic-Mayo Foundation, Rochester
Eckloff B.W.
Freimuth R.R.
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Dept. Mole. Pharmacol./Exper. Ther., Mayo Medical School-Mayo, Clinic-Mayo Foundation, RochesterDept. Mole. Pharmacol./Exper. Ther., Mayo Medical School-Mayo, Clinic-Mayo Foundation, Rochester
Freimuth R.R.
Wieben E.D.
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Dept. Mole. Pharmacol./Exper. Ther., Mayo Medical School-Mayo, Clinic-Mayo Foundation, RochesterDept. Mole. Pharmacol./Exper. Ther., Mayo Medical School-Mayo, Clinic-Mayo Foundation, Rochester
Wieben E.D.
Weinshilboum R.M.
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机构:
Dept. Mole. Pharmacol./Exper. Ther., Mayo Medical School-Mayo, Clinic-Mayo Foundation, RochesterDept. Mole. Pharmacol./Exper. Ther., Mayo Medical School-Mayo, Clinic-Mayo Foundation, Rochester