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KMID : 0620920020340010032
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Experimental & Molecular Medicine
2002 Volume.34 No. 1 p.32 ~ p.37
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D4-GDI is cleaved by caspase-3 during daunorubicin-induced apoptosis in HL-60 cells
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Byung Hyun Park/Kang Beom Kwon
Eun Kyung Park/Do Gon Ryu/Byung Hyun Park
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Abstract
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Daunorubicin, an anti-cancer drug, is known to induce apoptosis in HL-60 cells in a dose-dependent manner through the activation of caspase-3 (CPP32). Caspase-3 selective inhibitor, Ac-DEVD-CHO, prevented both the activation of caspase-3 and cleavage of poly(ADP-ribose) polymerase (PARP). D4-GDI is a GDP dissociation inhibitor for the Ras-related Rho family GTPase in hematopoietic cells. Here we report that D4-GDI is a substrate for the caspase-3. D4-GDI was cleaved to a 23 kDa fragment by daunorubicin treatment in HL-60 cells with kinetics that parallel the onset of apoptosis. D4-GDI cleavage as well as DNA fragmentation was inhibited by treatment with Ac-DEVD-CHO but not with Ac-YVAD-CHO, a caspase-1 inhibitor. These data suggest that D4-GDI of Rho family GTPase may be regulated during apoptosis through the caspase-3 mediated cleavage of the GDI protein.
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KEYWORD
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daunorubicin, caspase-3, D4-GDI, poly(ADP-ribose) polymerase, apoptosis,
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