We reported previously that
NSC606985, a
camptothecin analogue, induces apoptosis of
acute myeloid leukemia (AML) cells through proteolytic activation of
protein kinase Cdelta. Here, we analyzed
protein expression profiles of fractionated nuclei, mitochondria, raw endoplasmic reticula, and cytosols of NSC606985-induced apoptotic AML cell line NB4 cells by two-dimensional electrophoresis combined with MALDI-TOF/TOF tandem mass spectrometry. In total, 90 unique deregulated
proteins, including 16 compartment-compartment translocated ones, were identified. They contributed to multiple functional activities such as DNA damage repairing, chromosome assembly,
mRNA processing, biosynthesis, modification, and degradation of
proteins. More interestingly, several increased oxidative stress-related
proteins mainly presented in mitochondria, while upregulated glycolysis
proteins mainly occurred in the nuclei. With their functional analyses, the possible roles of these deregulated
proteins in NSC606985-induced apoptosis were discussed. Collectively, these discoveries would shed new insights for systematically understanding the mechanisms of the
camptothecin-induced apoptosis.