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J S Hernández’s research while affiliated with Mayo Clinic – Rochester – Minnesota – USA
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Publications (5)
Sulfation of estrone and 17β-estradiol in human liver: Catalysis by thermostable phenol sulfotransferase and by dehydroepiandrosterone sulfotransferase Article
Sulfation is a major pathway in humans for the biotransformation of estrogens. However, the nature of the enzymes that catalyze the sulfation of estrone (E1) and 17 beta-estradiol (E2) in human liver is unclear. Human liver contains at least three well-characterized cytoplasmic sulfotransferases, the thermostable (TS) and thermolabile (TL) forms of…Cite Request full-text Human liver arylamine N-sulfotransferase activity. Thermostable phenol sulfotransferase catalyzes the N-sulfation of 2-naphthylamine Article
Our experiments were performed to determine whether human liver, like that of other mammals, could catalyze the N-sulfation of an arylamine, 2-naphthylamine (2-NA) and, if so, whether this reaction might be catalyzed by one or both of the two known forms of human phenol sulfotransferase (PST). One form of PST is thermostable (TS) and catalyzes the…Cite Request full-text Thiopurine methyltransferase regulation in rat kidney: Immunoprecipitation studies Article
1. Thiopurine methyltransferase (TPMT) catalyses the S-methylation of thiopurine drugs. TPMT activity in the kidneys of male Sprague-Dawley (S-D) rats is approximately twice that present in the kidneys of female S-D rats, and this difference is testosterone-dependent. Renal TPMT activities in these animals also increase dramatically during growth a…Cite Request full-text Human liver estrone (E1), Estradiol (E2) and dehydroepiandrosterone (DHEA) sulfotransferases (STs): Comparison with thermostable (TS) and thermolabile (TL) phenol sulfotransferase (PST) activities Article
Sulfation plays an important role in the metabolism of E1, E2 and DHEA in humans. The relationship between the enzymes that catalyze the sulfation of E1, E2 and DHEA and TS and TL PST is unclear. The authors compared thermal stability, sensitivity to inhibition by 2,6-dichloro-4-nitrophenol (DCNP) and individual variation in the regulation of these…Cite Request full-text Mouse thiopurine methyltransferase pharmacogenetics: Correlation of immunoreactive protein and enzymatic activity Article
Thiopurine methyltransferase (TPMT) catalyzes the S-methylation of aromatic and heterocyclic sulfhydryl compounds including thiopurine drugs such as 6-mercaptopurine. Genetic polymorphisms control levels of TPMT enzymatic activity in both humans and inbred mice. AKR/J (AK) and C57BL/6J (B6) mice have genetically low, whereas DBA/2J (D2) mice have g…Cite Request full-text
Citations
… However, differential cell counts performed on bone marrow smears from AZA-treated mice (Table 5) did not show a reduced number of erythroid cells. TPMT genetic polymorphisms which play a role in the development of bone marrow injury following AZA treatment in man also occur in some strains of mouse (Hernandez et al. 1990 ). It is possible that if the present studies had been conducted with a strain of mouse that is known to have a genetically low TMPT activity (for example, the C57BL ⁄ 6J or AKR ⁄ J strains) a more acute bone marrow injury may have been observed involving all haemopoietic cell lineages. …Reference: The haemotoxicity of azathioprine in repeat dose studies in the female CD‐1 mouse Mouse thiopurine methyltransferase pharmacogenetics: Correlation of immunoreactive protein and enzymatic activity Citing article
View … Most, if not all, cellular effects of estrogens are mediated by the nuclear receptors estrogen receptor alpha (ERα) and -beta (ERß) with a high ligand-receptor binding affinity (Kd˜1nM) [27][28][29]. Although estrogens have been reported to be the substrates of multiple SULTs including SULT1A1 and SULT2A1 [30] , SULT1E1 exhibits the highest affinity for these hormones, especially the 3-hydroxyl position of E 2 [5,29], to which it binds with a Michaelis-Menten constant (Km) of 0.27 nM and with a turnover number (kcat) of 10s −1 x10 3 /nM respectively [31,32]. This sulfoconjugation of estrogens can be reversed by the deconjugation reaction catalyzed by the steroid sulfatase (STS) [33]. …Reference: Hepatic Estrogen Sulfotransferase Distantly Sensitizes Mice to Hemorrhagic Shock-Induced Acute Lung Injury Sulfation of estrone and 17β-estradiol in human liver: Catalysis by thermostable phenol sulfotransferase and by dehydroepiandrosterone sulfotransferase Citing article
View … In human liver, the N-sulfonation of various alicyclic amines is mediated primarily by SULT2A1 (Shiraga et al. 1999a). SULT1A1 appears to be the major enzyme catalyzing the sulfonation of 2-naphthylamine (Hernandez et al. 1991) . …Reference: Pharmacogenetics of soluble sulfotransferases (SULTs). Naunyn Schmiedebergs Arch Pharmacol Human liver arylamine N-sulfotransferase activity. Thermostable phenol sulfotransferase catalyzes the N-sulfation of 2-naphthylamine Citing article
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Top co-authors (7)
Richard Weinshilboum
Mayo Foundation for Medical Education and Research
Thomas C Wood
Mayo Foundation for Medical Education and Research
Jon A. Van Loon
D M Otterness
R. W. G. Watson
S P Powers
Roberto Guerciolini
Top journals
Drug Metabolism and Disposition: the Biological Fate of Chemicals (2) Xenobiotica (1) Journal of Pharmacology and Experimental Therapeutics (1) The FASEB Journal (1)
Affiliations
Mayo Clinic – Rochester Department
Department of Molecular Pharmacology and Experimental Therapeutics
Disciplines
Biology Topic
Chemistry Topic
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Fuente: https://www.researchgate.net/scientific-contributions/J-S-Hernandez-39289797