Disease relevance of SULT1C4

• Induction of differentiation did not generally affect SULT expression, although that of SULT1C2 was reduced after differentiation of the neuroblastoma cell line, NB-1, was induced [1].
• Recombinant human SULT1C sulfotransferases 1 and 2, expressed in Escherichia coli and purified to near electrophoretic homogeneity, were shown to cross-react with the antiserum against the rat liver SULT1C1 sulfotransferase and exhibited sulfonating activities with N-OH-2AAF as substrate [2].

High impact information on SULT1C4

• In the same model, increased relapse risk was associated with SULT1C2 heterozygosity (RR = 4.1; P = .004), FLT3-ITD (RR 3.3; P = .003), and MDR1 variant alleles (RR = 2.4; P = .02) [3].
• Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene [2].
• As there are no isoform-selective substrates for SULTs 1B1 and 1C2 we used immunoblot analysis to show for the first time expression of SULT1B1 at high levels in fetal small intestine, and expression of SULT1C2 in fetal liver, kidney and small intestine [4].
• The amino acid sequence of ratSULT1C2 is 84% identical to the human SULT1C2 and 81% identical to a rabbit SULT1C2 sulfotransferase. ratSULT1C2 and ratSULT1C2A are 92% identical but differ in 22 amino acids [5].
• Activity data showed that P-form (SULT1A1) PST displayed the highest activity toward these compounds, while SULT1C ST #2 also showed considerable activity, indicating that these enzymes may play a more important role in detoxification of environmental xenoestrogens [6].

Biological context of SULT1C4

• The cloning and structural characterization of SULT1C1 and SULT1C2 will now make it possible to perform molecular genetic and pharmacogenomic studies of these sulfate-conjugating enzymes in humans [7].

Other interactions of SULT1C4

• SULT1C1 and SULT1C2 were approximately 21 and 10 kb in length, respectively [7].

Analytical, diagnostic and therapeutic context of SULT1C4

• Finally, human SULT1C1 and SULT1C2 mapped to 2q11.2 by fluorescence in situ hybridization [7].
• In the present study, two novel human sulfotransferases shown to be members of the SULT1C sulfotransferase subfamily based on sequence analysis have been cloned, expressed, and characterized [2].
• Tissue-specific expression of these novel human SULT1C sulfotransferases were examined by employing the Northern blotting technique [2].

References