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* Department of Biochemistry and Molecular Biology in Disease, Atomic Bomb Disease Institute, Nagasaki University School of Medicine, and
Department of Histology and Cell Biology, Nagasaki University School of Medicine, Nagasaki 852-8523, Japan
1Correspondence: Department of Biochemistry and Molecular Biology in Disease, Atomic Bomb Disease Institute, Nagasaki University School of Medicine, Nagasaki, 852-8523, Japan. E-mail: kondo{at}net.nagasaki-u.ac.jp
Glutathione S-transferase (GST) functions in xenobiotic biotransformation and drug metabolism. Increased expression of GST
, an isozyme of GST, has been found in cancer cells resistant to doxorubicin hydrochloride (DOX) or cis-diamminedichloroplatinum (II) (CDDP), and this increase was believed to be correlated with drug resistance of cancer cells. GST is mainly expressed in the cytoplasm; GST in the nucleus has been reported in cancer cells, but the meaning of this result is not known. Here, we studied changes in the amount of nuclear GST after exposure of cancer cells to anticancer drugs, and role of the nuclear GST in drug resistance. We found nuclear GST in cancer cells resistant to DOX, and the amount of nuclear GST was enhanced by treatment of the cancer cells with DOX or CDDP. We also found that a mushroom lectin, an inhibitor of nuclear transport, inhibited the nuclear transfer of GST, suggesting the existence of a specific transport system for the nuclear transfer of GST. Nuclear GST protected DNA against damage by anticancer drugs. These results suggest a possible role of GST in the acquisition of resistance to anticancer drugs by cancer cells. —Goto, S., Ihara, Y., Urata, Y., Izumi, S., Abe, K., Koji, T., Kondo, T. Doxorubicin-induced DNA intercalation and scavenging by nuclear glutathione S-transferase .
Key Words: Glutathione S-transferase • doxorubicin • cisplatin • nuclear transfer • DNA damage
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