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논문 기본 정보

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학술저널
저자정보
Fasanmade, Adedigbo A. (Department of Pharmaceutics and Pharmacodynamics, Center for Pasrmaceutical Biotechnology, College of Pharmacy Centocor Biotechnology Inc.) Owuor, Edward D. (Department of Pharmaceutics and Pharmacodynamics, Center for Pasrmaceutical Biotechnology, College of Pharmacy, Department of Pharmaceutics, College of Pharmacy, Rutgers University, E) Ee, Rachel P.L. (Department of Pharmaceutics and Pharmacodynamics, Center for Pasrmaceutical Biotechnology, College of Pharmacy) Qato, Dima (Department of Pharmaceutics and Pharmacodynamics, Center for Pasrmaceutical Biotechnology, College of Pharmacy) Heller, Mark (Centocor Biotechnologies Inc.,) Kong, Ah Ng Tony (Department of Pharmaceutics and Pharmacodynamics, Center for Pasrmaceutical Biotechnology, College of Pharmacy, Department of Pharmaceutics, College of Pharmacy, Rutgers University, E)
저널정보
대한약학회 Archives of pharmacal research : a publication of the Pharmaceutical Society of Korea Archives of pharmacal research : a publication of the Pharmaceutical Society of Korea 제24권 제2호
발행연도
2001.1
수록면
126 - 135 (10page)

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Quinacrine (QU), a phospholipase-A2 (PLA-2) inhibitor has been used clinically as a chemotherapeutic adjuvant. To understand the mechanisms leading to its chemotherapeutic effect, we have investigated QU-induced apoptotic signaling pathways in human cervical squamous carcinoma HeLa cells. In this study, we found that QU induced cytochrome c-dependent apoptotic signaling. The release of pro-apoptotic cytochrome c was QU concentration- and time-dependent, and preceded activation of caspase-9 and -3. Flow cytometric FACScan analysis using fluorescence intensities of $DiOC_6$/ demonstrated that QU-induced cytochrome c release was independent of mitochondrial permeability transition (MPT), since the concentrations of QU that induced cytochrome c release did not alter mitochondrial membrane potential (${\blacktriangle}{\Psi}_m$). Moreover, kinetic analysis of caspase activities showed that cytochrome c release led to the activation of caspase-9 and downstream death effector caspase-3, Caspase-3 inhibitor (Ac-DEVD-CHO) partially blocked QU-induced apoptosis, suggesting the importance of caspase-3 in this apoptotic signaling mechanism. Supplementation with arachidonic acid (AA) sustained caspase-3 activation induced by QU. Using inhibitors against cellular arachidonate metabolism of lipooxygenase (Nordihydroxyguaiaretic Acid, NDGA) and cyclooxygenase (5,8,11,14-Eicosatetraynoic Acid, ETYA) demonstrated that QU-induced apoptotic signaling may be dependent on its role as a PLA-2 inhibitor. Interestingly, NDCA attenuated QU-induced cytochrome c release, caspase activity as well as apoptotic cell death. The blockade of cytochrome c release by NDCA was much more effective than that attained with cyclosporin A (CsA), a MPT inhibitor. ETYA was not effective in blocking cytochrome c release, except under very high concentrations. Caspase inhibitor z-VAD blocked the release of cytochrome c suggesting that this signaling event is caspase dependent, and caspase-8 activation may be upstream of the mitochondrial events. In summary, we report that QU induced cytochrome c-dependent apoptotic signaling cascade, which may be dependent on its role as a PLA-2 inhibitor. This apoptotic mechanism induced by QU may contribute to its known chemotherapeutic effects.
#Quinacrine #Cytochrome c #Caspase-3 #Phospholipase-A-2 #Cervical Carcinoma #Apoptosis

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