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Sulfotransferase family, cytosolic, 1C, member 3

male specific sulfotransferase that catalyzes the sulfation of N-hydroxy-2-acetylaminofluorene; plays a role in the bioactivation of N-hydroxyarylamines in the liver [RGD, Feb 2006] (from NCBI)
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Top mentioned proteins: PstI, ACID, estrogen sulfotransferase, HAD, CAN
Papers on SULT1C1
Human sulfotransferases enhance the cytotoxicity of tolvaptan.
Beland et al., United States. In Toxicol Sci, Jan 2016
Of the 12 known human SULTs, no detectable sulfation of tolvaptan was observed with SULT1A1, SULT1A2, SULT1A3, SULT1C2, SULT1C4, SULT4A1, or SULT6B1.
Transcriptional Regulation of Cytosolic Sulfotransferase 1C2 by Intermediates of the Cholesterol Biosynthetic Pathway in Primary Cultured Rat Hepatocytes.
Kocarek et al., Detroit, United States. In J Pharmacol Exp Ther, Dec 2015
Cytosolic sulfotransferase 1C2 (SULT1C2) is expressed in the kidney, stomach, and liver of rats; however, the mechanisms regulating expression of this enzyme are not known.
Toxicogenomics directory of chemically exposed human hepatocytes.
Hengstler et al., Dortmund, Germany. In Arch Toxicol, 2014
Liver disease genes deregulated in cirrhosis, HCC, and NASH that overlap with genes of the aforementioned stereotypical chemical stress response include CYP3A7, normally expressed in fetal liver; the phase II metabolizing enzyme SULT1C2; ALDH8A1, known to generate the ligand of RXR, one of the master regulators of gene expression in the liver; and several genes involved in normal liver functions: CPS1, PCK1, SLC2A2, CYP8B1, CYP4A11, ABCA8, and ADH4.
The co-transplantation of bone marrow derived mesenchymal stem cells reduced inflammation in intramuscular islet transplantation.
Unno et al., Sendai, Japan. In Plos One, 2014
In terms of gene expression, Sult1c2, Gstm1, and Rab37 were significantly upregulated in islets co-cultured with MSCs.
Bleomycin hydrolase and hyperhomocysteinemia modulate the expression of mouse proteins involved in liver homeostasis.
Jakubowski et al., Poznań, Poland. In Amino Acids, 2014
The two up-regulated proteins are involved in nitric oxide generation (Ddah1) and xenobiotic detoxification (Sult1c1).
Regulation of human cytosolic sulfotransferases 1C2 and 1C3 by nuclear signaling pathways in LS180 colorectal adenocarcinoma cells.
Kocarek et al., Detroit, United States. In Drug Metab Dispos, 2014
Treatment with 3-[3-[N-(2-chloro-3-trifluoromethylbenzyl)-(2,2-diphenylethyl)amino]propyloxy]phenylacetic acid hydrochloride [GW3965, liver X receptor (LXR) activator], 3-(2,6-dichlorophenyl)-4-(3'-carboxy-2-chlorostilben-4-yl)oxymethyl-5-isopropylisoxazole [GW4064, farnesoid X receptor (FXR)], or rifampicin [pregnane X receptor (PXR)] moderately (≤2-fold) increased both SULT1C2 and SULT1C3 mRNA levels.
RNA-sequencing quantification of hepatic ontogeny and tissue distribution of mRNAs of phase II enzymes in mice.
Klaassen et al., Syracuse, United States. In Drug Metab Dispos, 2013
Hepatic expression of certain Phase II enzymes peaked during the adolescent stage, such as Ugt1a1, Sult1a1, Sult1c2, Sult1d1, Sult2as, Sult5a1, Tpmt, Glyat, Ugp2, and Mat1a.
Metabolism and pharmacokinetics of mangiferin in conventional rats, pseudo-germ-free rats, and streptozotocin-induced diabetic rats.
Huang et al., Shanghai, China. In Drug Metab Dispos, 2012
The diabetic status induced increased UDP-glucuronosyltransferase (UGT) 1A3, UGT1A8, UGT2B8, and sulfotransferase (SULT) 1A1 mRNA levels and decreased catechol-O-methyltransferase (COMT), UGT2B6, UGT2B12, and SULT1C1 mRNA levels.
Identification of human and murine sulfotransferases able to activate hydroxylated metabolites of methyleugenol to mutagens in Salmonella typhimurium and detection of associated DNA adducts using UPLC-MS/MS methods.
Glatt et al., Potsdam, Germany. In Mutagenesis, 2012
Human SULT1A1 (a form expressed at high levels in many tissues) and SULT1C2 (expressed primarily in foetal tissues) activated all three compounds even at very low substrate concentrations.
Distinct sulfonation activities in resveratrol-sensitive and resveratrol-insensitive human glioblastoma cells.
Liu et al., Dalian, China. In Febs J, 2012
The levels of brain-associated SULT (SULT1A1, SULT1C2, and SULT4A1) expression in U251 cells were lower than those in LN229 cells, suggesting the inverse relationship of SULT-mediated sulfonation activity with high intracellular resveratrol bioavailability and resveratrol sensitivity of human GBM cells.
Hydroxymethyl-substituted furans: mutagenicity in Salmonella typhimurium strains engineered for expression of various human and rodent sulphotransferases.
Meinl et al., Potsdam, Germany. In Mutagenesis, 2012
HMF, 2,5-(bishydroxymethyl)furan (metabolite of HMF), FFA and 5-methyl-FFA were inactive in TA100 but strongly mutagenic when human SULT1C2 was expressed.
Crystal structures of human sulfotransferases SULT1B1 and SULT1C1 complexed with the cofactor product adenosine-3'- 5'-diphosphate (PAP).
Plotnikov et al., Toronto, Canada. In Proteins, 2006
crystal structures of two members of SULT1 family, SULT1B1 and SULT1C1, both in complex with the product of the PAPS cofactor, adenosine-3-5-diphosphate (PAP).
Human sulfotransferase SULT1C1 pharmacogenetics: gene resequencing and functional genomic studies.
Weinshilboum et al., Rochester, United States. In Pharmacogenetics, 2001
gene resequencing and functional genomic studies
On the nature of rat hepatic and mouse olfactory sulfotransferases.
Mikoshiba et al., Tokyo, Japan. In Chem Biol Interact, 1998
It encodes 304 amino acid polypeptide and is 94% identical with rat ST1C1 in amino acid sequences.
Regulation of sulfotransferase mRNA expression in male and female rats of various ages.
Dunn et al., Kansas City, United States. In Chem Biol Interact, 1998
Sulfotransferase SULT1C1 has been implicated in activation of N-hydroxyacetylaminoflourine.
[Multiplicity of sulfotransferases].
Matsui, Tokyo, Japan. In Yakugaku Zasshi, 1997
Mouse olfactory P-ST was present in the cytoplasm of olfactory sustentacular cells and its cloning study revealed that it is 94% identical with rat ST1C1 in amino acid sequences.
Activation and detoxication of carcinogenic arylamines by sulfation.
Kato et al., Tokyo, Japan. In Princess Takamatsu Symp, 1994
A new member of arylsulfotransferase, ST1C1, whose cDNA shows considerable sequence similarity to ST1A1 cDNA, was found to catalyze O-sulfation of N-hydroxy-2-acetylaminofluorence by the cDNA expression in COS-1 cells.
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