Heat-induced drug resistance is associated with increased expression of Bcl-2 in HL60.
HL60 cells underwent apoptosis with heat treatment, i.e. exposure to 42 degrees C for 120 minutes. Cells exposed to the same temperature for 30 minutes became resistant to subsequent, otherwise lethal, heat shock. These thermotolerant cells also acquired resistance to anti-cancer drugs including daunorubicin and VP16. We found that mild heat shock upregulates not only HSP70 but also BCL-2, though BCL-2 has not previously been recognized as a heat-inducible protein. Expression of BCL-2 closely paralleled resistance to subsequent exposure to anticancer drugs. The present results suggest that BCL-2 may play a role in heat-induced drug resistance.
Inoue
Y
Y
Third Department of Internal Medicine, Yamaguchi University School of Medicine, Japan.
Sato
Y
Y
Nishimura
M
M
Seguchi
M
M
Zaitsu
Y
Y
Yamada
K
K
Oka
Y
Y
D000903:Antibiotics, Antineoplastic / Q000494:pharmacology; D000972:Antineoplastic Agents, Phytogenic / Q000494:pharmacology; D017209:Apoptosis; D015153:Blotting, Western; D053938:DNA Fragmentation / Q000187:drug effects; D003630:Daunorubicin / Q000494:pharmacology; D019008:Drug Resistance, Neoplasm; D005047:Etoposide / Q000494:pharmacology; D018922:HL-60 Cells; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D006801:Humans; D019253:Proto-Oncogene Proteins c-bcl-2 / Q000235:genetics / Q000378:metabolism*; D013696:Temperature; D013997:Time Factors; D015854:Up-Regulation / Q000187:drug effects / Q000235:genetics
D000903:Antibiotics, Antineoplastic; D000972:Antineoplastic Agents, Phytogenic; D018840:HSP70 Heat-Shock Proteins; D019253:Proto-Oncogene Proteins c-bcl-2; D005047:Etoposide; D003630:Daunorubicin