研究报告 |
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丝氨酸蛋白酶HtrA2/Omi可参与调节线粒体中的适配蛋白p66Shc |
刘姝1,2, 姜长安1,2 |
1. 四川大学华西第二医院 西部妇幼医学研究院 华西发育与干细胞研究所 成都 610041; 2. 四川大学华西医院 生物治疗国家重点实验室 成都 610041 |
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Serine Protease Omi/HtrA2 Regulates Adaptor Protein p66Shc in Mitochondria |
LIU Shu1,2, JIANG Chang-an 1,2 |
1. West China Development and Stem Cell Institute, West China Institute of Women and Children's Health, West China Second University Hospital, Chengdu 610041, China; 2. State Key Laboratory of Biotherapy, West China Hospital, Chengdu 610041, China |
[1] Pallen M J, Wren B W. The HtrA family of serine proteases. Mol Microbiol, 1997, 26(2): 209-221. [2] Suzuki Y, Imai Y, Nakayama H, et al. A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Molecular Cell, 2001, 8(3): 613-621. [3] Cilenti L, Soundarapandian M M, Kyriazis G A, et al. Regulation of HAX-1 anti-apoptotic protein by Omi/HtrA2 pro tease during cell death. J Biol Chem, 2004, 279(48): 50295-50301. [4] Moisoi N, Klupsch K, Fedele V, et al. Mitochondrial dysfunction triggered by loss of HtrA2 results in the activation of a brain-specific transcriptional stress response. Cell Death and Differentiation, 2009,16(3): 449-464. [5] Martins L M, Morrison A, Klupsch K, et al. Neuroprotective Role of the Reaper-Related Serine Protease HtrA2/Omi Revealed by Targeted Deletion in Mice. Mol Cell Biol, 2004, 24(22): 9848-9862. [6] Jones J M, Datta P, Srinivasula S M, et al. Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice. Nature, 2003, 425(6959): 721-727. [7] Migliaccio E, Giorgio M, Mele S, et al. The p66shc adaptor protein controls oxidative stress response and life span in mammals. Nature, 1999, 402(6759): 309-313. [8] Nemoto S, Finkel T. Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway. Science, 2002, 295(5564): 2450-2452. [9] Trinei M, Giorgio M, Cicalese A, et al. A p53-p66Shc signalling pathway controls intracellular redox status, levels of oxidation-damaged DNA and oxidative stress-induced apoptosis. Oncogene, 2002, 21(24):3872-3878. [10] Napoli C, Martin-Padura I, de Nigris F, et al. Deletion of the p66Shc longevity gene reduces systemic and tissue oxidative stress, vascular cell apoptosis, and early at herogenesis in mice fed a high-fat diet. Proc Natl Acad Sci USA, 2003, 100(4): 2112-2116. [11] Francia P, delli Gatti C, Bachschmid M, et al. Deletion of p66shc gene protects against age-related endothelial dysfunction. Circulation, 2004, 110(18): 2889-2895. [12] Orsini F, Migliaccio E, Moroni M, et al. The lifespan determinant p66Shc localizes tomitochondria where it associates with mtHsp70 and regulates trans-membrane potential. J Biol Chem, 2004, 279(24): 25689-25695. [13] Giorgio M, Migliaccio E, Orsini F, et al. Electron Transfer between Cytochrome c and p66Shc Generates Reactive Oxygen Species that Trigger Mitochondrial Apoptosis. Cell, 2005, 122(2): 221-233. [14] Pinton P, Rimessi A, Marchi S, et al. Protein Kinase C beta and Prolyl Isomerase1 Regulate Mitochondrial Effects of the Life-Span Determinant p66Shc. Science, 2007, 315(5812): 659-663. [15] Kujoth G C, Hiona A, Pugh T D, et al. Mitochondrial DNA Mutations, Oxidative Stress, and Apoptosis in Mammalian Aging. Science, 2005, 309(5733): 481-484. [16] Li B, Hu Q, Wang H, et al. Omi/HtrA2 is a positive regulator of autophagy that facilitates the degradation of mutant proteins involved in neurodegenerative diseases. Cell Death and Differentiation, 2010, 17(11): 1773-1784. [17] Wieckowski M R, Giorgi C, Lebiedzinska M, et al. Isolation of mitochondria-associated membranes and mitochondria from animal tissues and cells. Nature Protocol, 2009, 4(11): 1582-1590. [18] Gonz醠ez-Polo R A, Boya P, Pauleau A L, et al. The apoptosis/autophagy paradox: autophagic vacuolization before apoptotic death. J Cell Sci, 2005, 188(14): 3091-3102. |
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