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Vol. 27, Issue 12, 1415-1422, December 1999
Institut für Toxikologie, Universität Mainz, Mainz,
Germany
The phase I and phase II drug-metabolizing capacity of
freshly isolated and cryopreserved parenchymal cells (PC) from human, rat, and mouse liver held in suspension at 37°C for up to 120 min
after thawing was compared. Although
7-ethoxycoumarin-O-deethylase activity was strongly
reduced in freshly isolated as well as in cryopreserved PC from human,
rat, and mouse liver after 120 min, 7-ethoxyresorufin-O-deethylase activity as well as the
profile and formation rates of hydroxylated testosterone metabolites in general remained constant throughout the 2-h incubation period in
cryopreserved PC from all three species and was similar to that
measured in freshly isolated PC. The activity of glutathione S-transferase (GST) and that of
UDP- glucuronosyltransferase (UDP-GT) toward 4-methylumbelliferone
significantly decreased, whereas the activities of UDP-GT activity
toward 4-hydroxybiphenyl and sulfotransferase in cryopreserved human PC
were similar to those measured in freshly isolated PC. The activities
of GST, UDP-GT toward 4-methylumbelliferone, and sulfotransferase in
cryopreserved rat PC showed a significant decrease when compared with
the activities in freshly isolated PC. The phase II enzyme
activities in cryopreserved mouse PC proved to be far more stable,
being similar to the activities of freshly isolated mouse PC at all
four time points measured with the exception of GST, which showed a
decay from t = 60 min onward. In conclusion, phase
I drug-metabolizing enzyme activities in cryopreserved human, rat, and
mouse PC are very similar to those of freshly isolated PC, whereas
phase II enzyme activities are affected by cryopreservation.
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