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Eur J Clin Pharmacol. 1991;41(4):345-50.

Distribution of UDP-glucuronosyltransferase and its endogenous substrate uridine 5'-diphosphoglucuronic acid in human tissues.

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Department of Biomedicine, Medical School, University of Pisa, Italy.


The activity of UDP-glucuronosyltransferase (UDPGT) and the concentration of its endogenous substrate, 5'-diphosphoglucuronic acid (UDPGA), have been measured in human liver, kidney, lung and intestinal mucosa. The activity of UDPGT was tissue- and substrate-dependent. The liver/kidney and liver/intestine ratios for UDPGT varied over one order of magnitude with three substrates. The highest activity of UDGPT in extrahepatic tissues was in the kidney, with 1-naphthol as substrate; it was about half of the hepatic activity. The concentration ( of UDPGA was 279 (liver), 17.4 (kidney), 19.3 (intestinal mucosa) and 17.2 (lung), it was at least 15-fold higher in liver than the other tissues, and the concentration in kidney, lung and intestinal mucosa was similar. The kinetics of UDPGT in a liver homogenate at varying concentrations of UDPGA and fixed concentration of 1-naphthol, ethinyloestradiol, and morphine was also measured. The apparent kM for UDPGT depended upon the chemical nature of the UDPGA-acceptor substrate; average values of kM were 63, 300, and 700 mumol.l-1 for 1-naphthol, ethinyloestradiol and morphine respectively. These values are, respectively, lower, similar to and higher than the hepatic concentration of UDPGA. Under certain circumstances UDPGA may be the limiting factor in the in vivo glucuronidation of drugs by extrahepatic tissues.

[Indexed for MEDLINE]

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