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Vol. 31, Issue 4, 452-461, April 2003
Department of Chemical Biology, Ernest Mario School of Pharmacy
(H.L., X.M., C.L., J.H., C.S.Y.); Department of Food Science and Center
for Advanced Food Technology (S.Sa., N.B., C-T.H); Department of
Chemistry, Rutgers, the State University of New Jersey, Piscataway, New
Jersey (S.Sh.); Shanghai Institute of Materia Medica, Chinese Academy
of Sciences, Shanghai, China (C.L.); BD Biosciences, Woburn,
Massachusetts (C.P.); and Environmental and Occupational Health
Sciences Institute, Piscataway, New Jersey (B.W., C.S.Y.)
(
)-Epigallocatechin gallate (EGCG) and ()-epigallocatechin
(EGC) are major green tea catechins with antioxidant and anticancer activities. In this study, we characterized the glucuronidation of EGCG
and EGC in human, mouse, and rat microsomes and by nine different human
UGT 1A and 2B isozymes expressed in insect cells. Six EGCG and EGC
glucuronides were biosynthesized, and their structures were identified
for the first time. ()-EGCG-4"-O-glucuronide was the
major EGCG glucuronide formed in all incubations. The catalytic
efficiency
(Vmax/Km) for
()-EGCG-4"-O-glucuronide formation followed the order:
mouse intestine > mouse liver > human liver > rat
liver 
rat small intestine. The UGT-catalyzed glucuronidation of EGC
was much lower than that of EGCG. The
Vmax/Km for
()-EGC-3'-O-glucuronide followed the following order:
mouse liver > human liver > rat liver > rat and mouse
small intestine. Human UGT1A1, 1A8, and 1A9 had high activities with
EGCG. UGT1A8, an intestine-specific UGT, had the highest
Vmax/Km for EGCG
but low activity with EGC. Mice appeared to be more similar to humans
than rats to humans in the glucuronidation of EGCG and EGC. Some of
these catechin glucuronides retained the activities of their parent
compounds in radical scavenging and in inhibiting the release of
arachidonic acid from HT-29 human colon cancer cells. These results
provide foundations for understanding the biotransformation and
biological activities of tea catechins.
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