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Blood, Vol. 95 No. 10 (May 15), 2000:
pp. 3214-3218
Glyoxalase I is involved in resistance of human leukemia cells
to antitumor agent-induced apoptosis
Hiroshi Sakamoto,
Tetsuo Mashima,
Atsuo Kizaki,
Shingo Dan,
Yuichi Hashimoto,
Mikihiko Naito, and
Takashi Tsuruo
From the Cancer Chemotherapy Center, Japanese Foundation for Cancer
Research, Tokyo, and the Institute of Molecular and Cellular
Biosciences, The University of Tokyo, Tokyo, Japan.
Abnormality in the machinery of apoptosis is associated with a
resistant phenotype of the tumor cell to chemotherapy. To determine the
molecular basis of resistance to antitumor agent-induced apoptosis, we
performed a complementary DNA (cDNA) subtractive hybridization with
messenger RNA (mRNA) from human monocytic leukemia U937 and its variant
UK711, which is resistant to apoptosis induced by antitumor agents. We
found that glyoxalase I (GLO1), an enzyme that
detoxifies methylglyoxal, is selectively overexpressed in the
apoptosis-resistant UK711 cells. The GLO1 enzyme activity was
significantly elevated in UK711 and UK110 cells, another drug-resistant mutant, as well as in K562/ADM, adriamycin-resistant leukemia cells,
compared with their parental cells. When overexpressed in human Jurkat
cells, GLO1 inhibited etoposide- and adriamycin-induced caspase
activation and apoptosis, indicating the involvement of GLO1 in
apoptosis suppression caused by these drugs. Moreover, cotreatment with
S-p-bromobenzylglutathione cyclopentyl diester (BBGC),
a cell-permeable inhibitor of GLO1, enhanced etoposide-induced apoptosis in resistant UK711 cells but not in parental U937 cells. Taken together, these results indicate that GLO1 is a resistant factor
to antitumor agent-induced apoptosis in human leukemia cells and that
the GLO1 inhibitor could be a drug resistance-reversing agent.
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