From the Research
SULT1A1 Activity and Paracetamol
- The effect of daily paracetamol (acetaminophen) on SULT1A1 activity is not directly addressed in the provided studies.
- However, studies have investigated the inhibition of SULT1A1 by various compounds, including mefenamic acid and salicylic acid 1, 2.
- Quercetin, a flavonoid present in edible fruit, vegetable, and wine, was found to be a potent inhibitor of human liver SULT1A1 and also inhibited the sulfation of paracetamol 2.
- SULT1A1 is involved in the sulfonation of paracetamol, and kinetic parameters of SULT1A1 in catalysing paracetamol sulphation have been determined 3.
- Paracetamol was used as a model substrate to evaluate the enzyme activity of immobilized SULT1A1 on magnetic microparticles 4.
Inhibition of SULT1A1
- Mefenamic acid was found to be a potent and selective inhibitor of human liver SULT1A1, with an IC50 value of 0.02 microM 2.
- Salicylic acid also inhibited SULT1A1, but with a higher IC50 value of 30 +/- 2 microM in adult liver and 25 +/- 1 microM in foetal liver 1.
- 17α-ethinylestradiol was found to be a potent inhibitor of SULT1A1, with a K(i) of 10 nM for inhibiting p-nitrophenol and β-naphthol sulfation 5.
SULT1A1 and Paracetamol Metabolism
- SULT1A1 is one of the major human cytosolic sulfotransferase enzymes responsible for the sulphation of paracetamol 3.
- The sulphation of paracetamol by SULT1A1 occurs in HepG2 human hepatoma cells and Caco-2 human intestinal epithelial cells under metabolic settings 3.
- Liver and intestine cytosols displayed considerably higher acetaminophen-sulphating activity than those of lung and kidney 3.