Fenamates and the potent inhibition of human liver phenol sulphotransferase

M. Vietri, C. De Santi, A. Pietrabissa, F. Mosca, G. M. Pacifici

Research output: Contribution to journalArticle

Abstract

1. The inhibition of the human liver phenol sulphotransferase (HL-PST) and catechol sulphotransferase (HL-CST) by five fenamates has been studied and the activities of HL-PST and HL-CST were measured with 4-nitrophenol and dopamine as substrates, respectively. 2. The IC50 for inhibition of HL-PST were 0.02 μM (mefenamic acid); 0.12 μM (tolfenamic acid); 0.28 μM (niflumic acid); 0.87 μM (meclofenamic acid) and 1.50 μM (flufenamic acid). 3. HL-CST was less susceptible than HL-PST to the inhibition by fenamates and the IC50 for HL-CST were 36 μM (tolfenamic acid); 70 μM (flufenamic acid); 76 μM (mefenamic acid); 180 μM (niflumic acid) and 185 μM (meclofenamic acid). 4. The ratios of the IC50 for HL-CST:HL-PST were drug-dependent and ranged from 47 (flufenamic acid) to 3800 (mefenamic acid). Mefenamic acid is a relatively potent and selective inhibitor of HL-PST. 5. The IC50 for HL-PST obtained with mefenamic acid was three orders of magnitude lower than the peak plasma concentration of this drug after an oral dose of 0.5 g. Accordingly, mefenamic acid should impair sulphation in vivo.

Original languageEnglish
Pages (from-to)111-116
Number of pages6
JournalXenobiotica
Volume30
Issue number2
Publication statusPublished - 2000

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Health, Toxicology and Mutagenesis
  • Pharmacology
  • Toxicology

Fingerprint Dive into the research topics of 'Fenamates and the potent inhibition of human liver phenol sulphotransferase'. Together they form a unique fingerprint.

  • Cite this

    Vietri, M., De Santi, C., Pietrabissa, A., Mosca, F., & Pacifici, G. M. (2000). Fenamates and the potent inhibition of human liver phenol sulphotransferase. Xenobiotica, 30(2), 111-116.