Ethanol Sulfation by the Human Cytosolic Sulfotransferases: A Systematic Analysis

Kurogi, Katsuhisa; Davidson, Garrett; Mohammed, Yasir I.; Williams, Frederick; Liu, Ming‐Yih; Sakakibara, Yoichi; Suiko, Masahito; Liu, Ming‐Cheh

doi:10.1248/bpb.b12-00547

Cited by 18 publications

(9 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Altogether, these results would suggest that UGTs have higher metabolic activity towards ethanol than SULTs both in vivo and in the in vitro models of hepatocytes used in this study. SULT1A1 and SULT2A1 are the main SULT isoforms expressed in liver (Riches et al, 2009;Kurogi et al, 2012;Stachel and Skopp 2016). Here, we confirmed that SULT1A1 and SULT2A1 mRNA are expressed at comparable levels between HepaRG and HH.…”

Section: Discussionsupporting

confidence: 80%

Non-oxidative ethanol metabolism in human hepatic cells in vitro: Involvement of uridine diphospho-glucuronosyltransferase 1A9 in ethylglucuronide production

Hugbart

Verres²,

Daré

et al. 2020

Toxicology in Vitro

View full text Add to dashboard Cite

show abstract

Section: Discussionsupporting

confidence: 80%

Non-oxidative ethanol metabolism in human hepatic cells in vitro: Involvement of uridine diphospho-glucuronosyltransferase 1A9 in ethylglucuronide production

Hugbart

Verres²,

Daré

et al. 2020

Toxicology in Vitro

View full text Add to dashboard Cite

show abstract

“…For example, the expression of SULT1A3 was found to be induced by its prototype substrate, dopamine, via ERK pathway in SK-N-MC and SH-SY5Y human neuroblastoma cells. 65) Ethanol has been shown to induce ethanol-sulfating SULTs, 66,67) SULT1A1 and SULT1E1, in cultured HepG2 human hepatoma cells. 68) Interestingly, 17β-estradiol, a substrate for SULT1A1 and SULT1E1, was demonstrated to be capable of inducing SULT2A1, implying that the sulfation of androgens, which are estrogen precursors, is regulated by 17β-estradiol.…”

Section: Regulation Of Sult Expression and Activitymentioning

confidence: 99%

Updated perspectives on the cytosolic sulfotransferases (SULTs) and SULT-mediated sulfation

Suiko

Kurogi

Hashiguchi

et al. 2017

Bioscience, Biotechnology, and Biochemistry

Self Cite

View full text Add to dashboard Cite

The cytosolic sulfotransferases (SULTs) are Phase II detoxifying enzymes that mediate the sulfate conjugation of numerous xenobiotic molecules. While the research on the SULTs has lagged behind the research on Phase I cytochrome P-450 enzymes and other Phase II conjugating enzymes, it has gained more momentum in recent years. This review aims to summarize information obtained in several fronts of the research on the SULTs, including the range of the SULTs in different life forms, concerted actions of the SULTs and other Phase II enzymes, insights into the structure-function relationships of the SULTs, regulation of SULT expression and activity, developmental expression of SULTs, as well as the use of a zebrafish model for studying the developmental pharmacology/toxicology.

show abstract

“…EtS is another minor, direct alcohol metabolite, produced through conjugation with sulfate. This reaction is carried out by cytosolic sulfotransferase enzymes [ 84 ]. EtG is primarily used to detect heavy alcohol use.…”

Section: Breath Testmentioning

confidence: 99%

Biomolecules and Biomarkers Used in Diagnosis of Alcohol Drinking and in Monitoring Therapeutic Interventions

Nanau

Neuman

2015

Biomolecules

View full text Add to dashboard Cite

Background: The quantitative, measurable detection of drinking is important for the successful treatment of alcohol misuse in transplantation of patients with alcohol disorders, people living with human immunodeficiency virus that need to adhere to medication, and special occupational hazard offenders, many of whom continually deny drinking. Their initial misconduct usually leads to medical problems associated with drinking, impulsive social behavior, and drunk driving. The accurate identification of alcohol consumption via biochemical tests contributes significantly to the monitoring of drinking behavior. Methods: A systematic review of the current methods used to measure biomarkers of alcohol consumption was conducted using PubMed and Google Scholar databases (2010–2015). The names of the tests have been identified. The methods and publications that correlate between the social instruments and the biochemical tests were further investigated. There is a clear need for assays standardization to ensure the use of these biochemical tests as routine biomarkers. Findings: Alcohol ingestion can be measured using a breath test. Because alcohol is rapidly eliminated from the circulation, the time for detection by this analysis is in the range of hours. Alcohol consumption can alternatively be detected by direct measurement of ethanol concentration in blood or urine. Several markers have been proposed to extend the interval and sensitivities of detection, including ethyl glucuronide and ethyl sulfate in urine, phosphatidylethanol in blood, and ethyl glucuronide and fatty acid ethyl esters in hair, among others. Moreover, there is a need to correlate the indirect biomarker carbohydrate deficient transferrin, which reflects longer lasting consumption of higher amounts of alcohol, with serum γ-glutamyl transpeptidase, another long term indirect biomarker that is routinely used and standardized in laboratory medicine.

show abstract

Ethanol Sulfation by the Human Cytosolic Sulfotransferases: A Systematic Analysis

Cited by 18 publications

References 43 publications

Non-oxidative ethanol metabolism in human hepatic cells in vitro: Involvement of uridine diphospho-glucuronosyltransferase 1A9 in ethylglucuronide production

Non-oxidative ethanol metabolism in human hepatic cells in vitro: Involvement of uridine diphospho-glucuronosyltransferase 1A9 in ethylglucuronide production

Updated perspectives on the cytosolic sulfotransferases (SULTs) and SULT-mediated sulfation

Biomolecules and Biomarkers Used in Diagnosis of Alcohol Drinking and in Monitoring Therapeutic Interventions

Contact Info

Product

Resources

About