Suppressive effect of elongation factor 2 on apoptosis induced by HIV-1 viral protein R

Springer Science and Business Media LLC - Tập 11 Số 3 - Trang 377-388 - 2006
Stanislav Zelivianski1, Dong Liang1, M. Chen1, Bernard L. Mirkin1, Yuqi Zhao2
1Children's Memorial Research Center, Department of Pediatrics, Northwestern University Feinberg School of Medicine, 60614, Chicago, IL, USA
2Departments of Pathology and Microbiology-Immunology, University of Maryland School of Medicine, 10 South Pine Street, MSTF 700A, Baltimore, MD, 21201, USA

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Tài liệu tham khảo

Azad AA. Could Nef and Vpr proteins contribute to disease progression by promoting depletion of bystander cells and prolonged survival of HIV-infected cells?. Biochem Biophys Res Commun 2000; 267(3): 677–685.

Bukrinsky M, Adzhubei A. Viral protein R of HIV-1. Rev Med Virol 1999; 9(1): 39–49.

Emerman M. HIV-1, Vpr and the cell cycle. Curr Biol 1996; 6(9): 1096–1103.

Ferri KF, Kroemer G. Organelle-specific initiation of cell death pathways. Nat Cell Biol 2001; 3(11): E255–E263.

Talapatra S, Thompson CB. Growth factor signaling in cell survival: implications for cancer treatment. J Pharmacol Exp Ther 2001; 298(3): 873–878.

Chen M, Wang J. Initiator caspases in apoptosis signaling pathways. Apoptosis 2002; 7(4): 313–319.

Budihardjo I, Oliver H, Lutter M, Luo X, Wang X. Biochemical pathways of caspase activation during apoptosis. Annu Rev Cell Dev Biol 1999; 15: 269–290.

Li P, Nijhawan D, Budihardjo I, et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997; 91(4): 479–489.

Dejean LM, Martinez-Caballero S, Guo L, et al. Oligomeric, Bax Is a Component of the Putative, Cytochrome c Release Channel, MAC, Mitochondrial, Apoptosis-induced Channel. Mol Biol Cell 2005.

Hajra KM, Liu JR. Apoptosome dysfunction in human cancer. Apoptosis 2004; 9(6): 691–704.

Higuchi M, Proske RJ, Yeh ET. Inhibition of mitochondrial respiratory chain complex I by TNF results in cytochrome c release, membrane permeability transition, and apoptosis. Oncogene 1998; 17(19): 2515–2524.

Ahlemeyer B, Klumpp S, Krieglstein J. Release of cytochrome c into the extracellular space contributes to neuronal apoptosis induced by staurosporine. Brain Res 2002; 934(2): 107–116.

Desagher S, Osen-Sand A, Nichols A, et al. Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. J Cell Biol 1999; 144(5): 891–901.

Tafani M, Cohn JA, Karpinich NO, Rothman RJ, Russo MA, Farber JL. Regulation of intracellular pH mediates Bax activation in HeLa cells treated with staurosporine or tumor necrosis factor-alpha. J Biol Chem 2002; 277(51): 49569–49576.

Zhao RY, Bukrinsky M, Elder RT. HIV-1 Viral Protein R (Vpr) and Host Cellular Responses. Ind J Med Res 2005; 121(4): 270–286.

Zhao Y, Elder RT. Yeast perspectives on HIV-1 Vpr. Frontiers in Bioscience 2000; 5: 905–916.

Macreadie IG, Thorburn DR, Kirby DM, Castelli LA, de Rozario NL, Azad AA. HIV-1 protein Vpr causes gross mitochondrial dysfunction in the yeast Saccharomyces cerevisiae. FEBS Lett 1997; 410(2–3): 145–149.

Macreadie IG, Castelli LA, Hewish DR, Kirkpatrick A, Ward AC, Azad AA. A domain of human immunodeficiency virus type 1 Vpr containing repeated H(S/F)RIG amino acid motifs causes cell growth arrest and structural defects. Proc Natl Acad Sci USA 1995; 92(7): 2770–2774.

Zhao Y, Cao J, O'Gorman MRG, Yu M, Yogev R. Effect of human immunodeficiency virus Type 1 protein R (vpr) gene expression on basic cellular functions of fission yeast Schizosaccharomyces pombe. J Virol 1996; 70: 5821–5826.

Zhao Y, Yu M, Chen M, Elder RT, Yamamoto AJC. Pleiotropic effects of HIV-1 protein R (Vpr) on morphogenesis and cell survival in fission yeast and antagonism by pentoxifylline. Virol 1998a; 246: 266–276.

Elder RT, Yu M, Chen M, Zhu X, Yanagida M, Zhao Y. HIV-1 Vpr induces cell cycle G2 arrest in fission yeast (Schizosaccharomyces pombe) through a pathway involving regulatory and catalytic subunits of PP2A and acting on both Wee1 and Cdc25. Virol 2001; 287(2): 359–370.

Maundrell K. Thiamine-repressible expression vectors pREP and pRIP for fission yeast. Gene 1993; 123(1): 127–130.

Zhao Y, Yu M, Chen M, Elder RT, Yamamoto A, Cao J. Pleiotropic effects of HIV-1 protein R (Vpr) on morphogenesis and cell survival in fission yeast and antagonism by pentoxifylline. Virol 1998; 246: 266–276.

Chen M, Elder RT, Yu M, et al. Mutational analysis of Vpr-induced G2 arrest, nuclear localization, and cell death in fission yeast. J Virol 1999; 73(4): 3236–3245.

Zhao Y, Cao J, O'Gorman MRG, Yu M, Yogev R. Effect of human immunodeficiency virus Type 1 protein R (vpr) gene expression on basic cellular functions of fission yeast Schizosaccharomyces pombe. J Virol 1996; 70: 5821–5826.

Zhao Y, Elder RT, Chen M, Cao J. Fission yeast expression vectors adapted for large scale cloning and GFP fusion with positive screening. BioTechniques 1998; 25: 438–444.

Elder RT, Yu M, Chen M, Zhu X, Yanagida M, Zhao Y. HIV-1 Vpr induces cell cycle G2 arrest in fission yeast (Schizosaccharomyces pombe) through a pathway involving regulatory and catalytic subunits of PP2A and acting on both Wee1 and Cdc25. Virology 2001; 287(2): 359–370.

Benko Z, Liang D, Agbottah E, et al. Anti-Vpr activity of a yeast chaperone protein. J Virol 2004; 78(20): 11016–11029.

Susin SA, Lorenzo HK, Zamzami N, et al. Molecular characterization of mitochondrial apoptosis-inducing factor. Nature 1999; 397(6718): 441–446.

Zhang S, Feng Y, Narayan O, Zhao L. Cytoplasmic retention of HIV-1 regulatory protein Vpr by protein-protein interaction with a novel human cytoplasmic protein VprBP. Gene 2001; 263(1–2): 131–140.

Chowdhury IH, Wang XF, Landau NR, et al. HIV-1 Vpr activates cell cycle inhibitor p21/Waf1/Cip1: a potential mechanism of G2/M cell cycle arrest. Virology 2003; 305(2): 371–377.

Amini S, Saunders M, Kelley K, Khalili K, Sawaya BE. Interplay between HIV-1 Vpr and Sp1 modulates p21(WAF1) gene expression in human astrocytes. J Biol Chem 2004; 279(44): 46046–46056.

Rebbaa A, Chou PM, Emran M, Mirkin BL. Doxorubicin-induced apoptosis in caspase-8-deficient neuroblastoma cells is mediated through direct action on mitochondria. Cancer Chemother Pharmacol 2001; 48(6): 423–428.

Javelaud D, Besancon F. Inactivation of p21WAF1 sensitizes cells to apoptosis via an increase of both p14ARF and p53 levels and an alteration of the Bax/Bcl-2 ratio. J Biol Chem 2002; 277(40): 37949–37954.

Elder RT, Benko Z, Zhao Y. HIV-1 VPR modulates cell cycle G2/M transition through an alternative cellular mechanism other than the classic mitotic checkpoints. Front Biosci 2002; 7: d349–d357.

Zhao Y, Lieberman HB. Schizosaccharomyces pombe: A model for molecular studies of eukaryotic genes. DNA Cell Biol 1995; 14(5): 359–371.

Gogal RM, Jr., Smith BJ, Kalnitsky J, Holladay SD. Analysis of apoptosis of lymphoid cells in fish exposed to immunotoxic compounds. Cytometry 2000; 39(4): 310–318.

Muthumani K, Hwang DS, Desai BM, et al. HIV-1 Vpr induces apoptosis through caspase 9 in T cells and peripheral blood mononuclear cells. J Biol Chem 2002; 277(40): 37820–37831.

Tafani M, Schneider TG, Pastorino JG, Farber JL. Cytochrome c-dependent activation of caspase-3 by tumor necrosis factor requires induction of the mitochondrial permeability transition. Am J Pathol 2000; 156(6): 2111–2121.

Rhoads RE. Signal transduction pathways that regulate eukaryotic protein synthesis. J Biol Chem 1999; 274(43): 30337–30340.

Ryazanov AG, Spirin AS. Phosphorylation of elongation factor 2: A key mechanism regulating gene expression in vertebrates. New Biol 1990; 2(10): 843–850.

Ryazanov AG. Elongation factor-2 kinase and its newly discovered relatives. FEBS Lett 2002; 514(1): 26–29.

Marin P, Nastiuk KL, Daniel N, et al. Glutamate-dependent phosphorylation of elongation factor-2 and inhibition of protein synthesis in neurons. J Neurosci 1997; 17(10): 3445–3454.

Arora S, Yang JM, Kinzy TG, et al. Identification and characterization of an inhibitor of eukaryotic elongation factor 2 kinase against human cancer cell lines. Cancer Res 2003; 63(20): 6894–6899.

Iglewski WJ. Cellular ADP-ribosylation of elongation factor 2. Mol Cell Biochem 1994; 138(1–2):131–133.

Iglewski BH, Liu PV, Kabat D. Mechanism of action of Pseudomonas aeruginosa exotoxin Aiadenosine diphosphate-ribosylation of mammalian elongation factor 2 in vitro and in vivo. Infect Immun 1977; 15(1): 138–144.

Morimoto H, Bonavida B. Diphtheria toxin- and Pseudomonas A toxin-mediated apoptosis. ADP ribosylation of elongation factor-2 is required for DNA fragmentation and cell lysis and synergy with tumor necrosis factor-alpha. J Immunol 1992; 149(6): 2089–2094.

Dorovkov MV, Pavur KS, Petrov AN, Ryazanov AG. Regulation of elongation factor-2 kinase by pH. Biochemistry 2002; 41(45): 13444–13450.

Feuermann M, Francisci S, Rinaldi T, et al. The yeast counterparts of human 'MELAS' mutations cause mitochondrial dysfunction that can be rescued by overexpression of the mitochondrial translation factor EF-Tu. EMBO Rep 2003; 4(1): 53–58.