Human sulfotransferase (SULT) 1C1: Functional genomics of common polymorphisms

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SULT1C1 catalyzes the sulfation of planar phenols, thyroid hormones and the chemical procarcinogen N-OH-2-acetylaminofluorene in a step required for the metabolic activation of that compound. We recently cloned the human SULT1C1 gene and resequenced it using DNA from 89 Caucasian subjects. A total of 31 polymorphisms were found, including 7 nonsynonymous cSNPs, 4 of which had allele frequencies greater than 1%. To study the effects of these cSNPs on enzyme activity and/or quantity of immunoreactive protein, expression constructs were created, and those constructs were used to transfect COS-1 cells. With 4-nitrophenol as a substrate, Asp60Ala and Arg73Gln had only about 15% of the activity of the wild type (WT) enzyme. Ser111Phe had no detectable enzyme activity, and Phe193Leu had approximately 40% of that of the WT sequence. Functional genomic characterization of cSNPs for SULT1C1 will now make it possible to use these pharmacogenomic data to test clinically relevant hypotheses.

Original languageEnglish (US)
Pages (from-to)P32
JournalClinical pharmacology and therapeutics
Issue number2
StatePublished - 2001

ASJC Scopus subject areas

  • Pharmacology
  • Pharmacology (medical)


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