Ask about this productRelated genes to: SULT1C4 Blocking Peptide
- Gene:
- SULT1C4 NIH gene
- Name:
- sulfotransferase family 1C member 4
- Previous symbol:
- SULT1C2
- Synonyms:
- SULT1C
- Chromosome:
- 2q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 2000-01-21
- Date modifiied:
- 2015-11-06
Related products to: SULT1C4 Blocking Peptide
Related articles to: SULT1C4 Blocking Peptide
- : Glucosinolates, secondary metabolites present in Brassicales, and their breakdown products have demonstrated various biological effects, including anti-carcinogenic activities in some animal models. The active compounds include indole-3-carbinol (I3C) and -methoxyindole-3-carbinol (NI3C). Building on these findings, several synthetic -substituted I3Cs strongly inhibited the growth of human cancer cell lines. This effect was mediated by reactive intermediates formed by sulphotransferase (SULT) 1A1. : We present genotoxicity findings on I3C and N-substituted derivatives, with special consideration given to SULTs. : We review genotoxicity findings with I3C, NI3C and their parental glucosinolates. Then, we present some findings hitherto unpublished. : Neoglucobrassicin and its breakdown product NI3C demonstrated high genotoxic activity in vitro and formed high levels of DNA adducts in animal studies. These effects were strongly enhanced in the presence of SULT1A1. By contrast, glucobrassicin and I3C were weakly mutagenic. New observations include: enhanced activation of NI3C to a mutagen by human SULT1C4 compared to SULT1A1; SULT1A1-dependent genotoxicity of I3C (induction of sister chromatid exchange, SCE); cellular co-localisation of SULT1A1 and DNA adducts formed in the kidneys of NI3C-treated mice. : I3C and NI3C are genotoxic in the presence of an appropriate SULT, but with large quantitative and qualitative differences (I3C required higher concentrations and induced only SCE, virtually no gene mutations). No information is available regarding the genotoxicity of other -substituted I3C derivatives being developed as antineoplastic drugs. We suspect that they may greatly vary in this activity, which in turn might impact clinical effectiveness as well as adverse side-effects. - Source: PubMed
Publication date: 2026/06/05
Glatt HansruediSchumacher Fabian - Capsaicin (CAP), the major pungent component of chili peppers, undergoes sulfation mediated by sulfotransferases (SULTs), an important phase II metabolic pathway influencing its pharmacological properties. In this study, we systematically investigated the sulfation metabolism of CAP and its underlying mechanisms in vitro and in vivo. Five sulfated metabolites were identified in rats with the liver as the primary site. Among them, M3-SO was the most abundant, followed by CAP-SO and M2-SO, while M4-SO was the least abundant. SULT1C4 and SULT1E1 mainly catalyzed CAP and M2 sulfation, whereas SULT1C4 was essential for M3 sulfation. In addition, CAP sulfation occurred in multiple brain regions. Unlike the liver, brain metabolism favored M2-SO over M3-SO, highlighting distinct central versus peripheral sulfation profiles. Brain microdialysis further confirmed this discrepancy. These findings provide a foundation for exploring the pharmacological roles of CAP and its sulfated metabolites, particularly within the central nervous system. - Source: PubMed
Publication date: 2025/11/04
Dou XiaohuanWang ShanZhang QidongMao JianChai GuobiShi QingzhaoZhu YunheFan Wu - Sulfonation is one of drug metabolism reactions affecting homeostasis of estrogens. C-3 aryl substituted 7-hydroxycoumarins are fluorescent estrogen mimetics; i.e., the hydroxyl groups of both estrogens and 7-hydroxycoumarins are conjugated by human sulfotransferases (SULTs). Sulfonation of the 7‑hydroxyl group by SULTs decreases the fluorescence of 7-hydroxycoumarins. Sulfonation of a series of 7-hydroxycoumarins by human SULTs was determined based on this property. SULT subtype-specific binding interactions of 7-hydrocoumarins were assessed against the modelled optimal arrangement needed for sulfonation. 3-(4-Methoxyphenyl)-7-hydroxycoumarin (11) and 3-(4-hydroxyphenyl)-7-hydroxycoumarin (9) were selective substrates for SULT1E1, whereas 3-(1H-1,2,4-triazol-1-yl)-7-hydroxycoumarin (14) was a selective SULT1A1 substrate. Other tested 7-hydroxycoumarin were sulfonated by more than two SULTs. Sulfonation of most 7-hydroxycoumarins by SULT1A1 or SULT1C4 followed Michaelis-Menten kinetics, while substrate inhibition kinetics occurred in sulfonation of several derivatives by SULT1E1. Selective sulfonation of derivatives 9 and 11 by SULT1E1 was due to the enzyme's long and cylindrical active site that assures optimal 7‑hydroxyl group placement in the precursory reaction state. SULT1A1 and SULT1C4 preferred smaller derivatives as substrates than the SULT1E. Estrogens potently inhibited the sulfonation of 3,4-dimethyl-7-hydroxycoumarin (4) by SULT1E1 (IC below 1 µM). SULT1A1 and SULT1C4 were less potently inhibited by the estrogens. Several 7-hydroxycoumarin derivatives share common binding interaction patterns with the estrogens at SULT1E1 and SULT1A1 active sites. Fluorescent 7-hydroxycoumarins could serve as convenient probe substrates for SULTs to evaluate their inhibition by new chemical entities during drug development. 7-Hydroxycoumarins 9 or 11 could be used as selective probe substrates for SULT1E1 and 14 for SULT1A1. - Source: PubMed
Publication date: 2025/08/28
Juvonen Risto OPostila Pekka ASingh Pankaj KumarHuuskonen JuhaniTimonen JuriFashe MulunehHussain RasikhAqip ZaeemaKärkkäinen OlliRaunio HannuPentikäinen Olli T - Rising cases of type 2 diabetes (T2D) in India, especially in metropolitan cities is an increasing concern. The individuals that were most affected are young professionals working in the corporate sector. However, the corporate sector has remained the least explored for T2D risk predisposition. Considering corporate employees' lifestyles and the role of gene-environment interaction in T2D susceptibility, the study aims to find genetic variants associated with T2D predisposition. In this first kind of study, 680 young professionals (284 T2D cases, and 396 controls) were diagnosed and screened for 2658 variants on an array designed explicitly for the CoGsI study. The variant filtering was done at Bonferroni p-value of 0.000028. The genetic data was analysed using PLINK v1.09, SPSS, R programming, VEP tool, and FUMA GWAS tool. Interestingly, 42 variants were associated with the T2D risk. Out of 42, three missense variants (rs1402467, rs6050, and rs713598) in Sulfotransferase family 1 C member 4 (SULT1C4), Fibrinogen Alpha Chain (FGA), and Taste 2 Receptor Member 38 (TAS2R38) and two untranslated region (UTR) variants (rs1063320 and rs6296) in Major Histocompatibility Complex, Class I, G (HLA-G) and 5-Hydroxytryptamine Receptor 1B (HTR1B) were associated with the T2D risk. CoGsI identified potential genomic markers increasing susceptibility to the early onset of T2D. Present findings provide insights into mechanisms underlying T2D manifestation in corporate professionals due to genetics interacting with occupational stress and urban lifestyles. - Source: PubMed
Publication date: 2025/01/02
Husami Shah FahadKaur TavleenGupta LoveRastogi GarimaSingh LakhvinderMeena PoojaSharma InduSingh HemenderSharma Varun - Cytosolic sulfotransferases (SULTs) are cytosolic enzymes that catalyze the transfer of sulfonate group to key endogenous compounds, altering the physiological functions of their substrates. SULT enzymes catalyze the -sulfonation of hydroxy groups or -sulfonation of amino groups of substrate compounds. In this study, we report the discovery of -sulfonation of α,β-unsaturated carbonyl groups mediated by a new SULT enzyme, SULT7A1, and human SULT1C4. Enzymatic assays revealed that SULT7A1 is capable of transferring the sulfonate group from 3'-phosphoadenosine 5'-phosphosulfate to the α-carbon of α,β-unsaturated carbonyl-containing compounds, including cyclopentenone prostaglandins as representative endogenous substrates. Structural analyses of SULT7A1 suggest that the -sulfonation reaction is catalyzed by a novel mechanism mediated by His and Cys residues in the active site. Ligand-activity assays demonstrated that sulfonated 15-deoxy prostaglandin J exhibits antagonist activity against the prostaglandin receptor EP2 and the prostacyclin receptor IP. Modification of α,β-unsaturated carbonyl groups via the new prostaglandin-sulfonating enzyme, SULT7A1, may regulate the physiological function of prostaglandins in the gut. Discovery of -sulfonation of α,β-unsaturated carbonyl groups will broaden the spectrum of potential substrates and physiological functions of SULTs. - Source: PubMed
Publication date: 2024/03/04
Kurogi KatsuhisaSakakibara YoichiHashiguchi TakuyuKakuta YoshimitsuKanekiyo MihoTeramoto TakamasaFukushima TsuyoshiBamba TakeshiMatsumoto JinFukusaki EiichiroKataoka HiroakiSuiko Masahito