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  • Title: Substrate specificity and some properties of phenol sulfotransferase from human intestinal Caco-2 cells.
    Author: Baranczyk-Kuzma A, Garren JA, Hidalgo IJ, Borchardt RT.
    Journal: Life Sci; 1991; 49(16):1197-206. PubMed ID: 1910139.
    Abstract:
    The phase II metabolic reactions, sulfation and glucuronidation, were studied in a human colon carcinoma cell line (Caco-2), which has been developed as a model of intestinal enterocytes. Phenol sulfotransferase (PST, EC 2.4.2.1) was isolated from Caco-2 cells cultured for 7, 14 and 21 days. The enzyme catalyzed the sulfation of both p-nitrophenol and catecholamines (e.g., dopamine) as well as most catecholamine metabolites. The affinity (Km) of PST for dopamine was much higher than for p-nitrophenol, and the specific activity of PST with both substrates increased with the age of the cells. The thermal stability of Caco-2 PST increased with cell age and was not dependent on the acceptor substrate used. The thermolabile PST from 7-day old cells was more sensitive to NEM than was the thermostable enzyme from 21-day old cells. No UDP-glucuronyltransferase (EC 2.4.1.17) activity was detected in 7-, 14- and 21-day old Caco-2 cells with any of the methods used.
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