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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2011.1
- 수록면
- 189 - 196 (8page)
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Ornithine decarboxylase (ODC) is the rate-limiting enzyme in polyamine biosynthesis and a target for chemoprevention. Hydroxydibenzoylmethane (HDB),a derivative of dibenzoylmethane of licorice, is a promising chemopreventive agent. In this paper, we investigated whether HDB would inhibit the ODC pathway to enhance apoptosis in human promyelocytic leukemia HL-60 cells. We found ODC enzyme activity was reduced during HDB treatment. Overexpression of ODC in HL-60 parental cells could reduce HDB-induced apoptosis, which leads to loss of mitochondrial membrane potential (Δψ m), through lessening intracellular ROS. Furthermore, ODC overexpression protected cytochrome c release and the activation of caspase-3 following HDB treatment. The results demonstrated HDB-induced apoptosis was through a mechanism of down-regulation of ODC and occurred along a ROS-dependent mitochondria-mediated pathway.
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참고문헌 (23)
참고문헌 신청
Amer J / 2003 / Flow cytometric measurement of reactive oxygen species production by normal and thalassaemic red blood cells / Eur J Haematol 70 : 84 ~ 90
Asher G / 2005 / A mechanism of ubiquitin-independent proteasomal degradation of the tumor suppressors p53 and p73 / Genes Dev 19 : 316 ~ 321
Auvinen M / 1992 / Ornithine decarboxylase activity is critical for cell transformation / Nature 360 : 355 ~ 358
Carter WO / 1994 / Intracellular hydrogen peroxide and superoxide anion detection in endothelial cells / J Leukoc Biol 55 : 253 ~ 258
Casero RA / 2009 / Polyamine catabolism and disease / Biochem J 421 : 323 ~ 338
Asher G / 2005 / A mechanism of ubiquitin-independent proteasomal degradation of the tumor suppressors p53 and p73 / Genes Dev 19 : 316 ~ 321
Auvinen M / 1992 / Ornithine decarboxylase activity is critical for cell transformation / Nature 360 : 355 ~ 358
Carter WO / 1994 / Intracellular hydrogen peroxide and superoxide anion detection in endothelial cells / J Leukoc Biol 55 : 253 ~ 258
Casero RA / 2009 / Polyamine catabolism and disease / Biochem J 421 : 323 ~ 338
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