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Volumn 20, Issue 3, 2010, Pages 314-331

S100A8/A9 induces autophagy and apoptosis via ROS-mediated cross-talk between mitochondria and lysosomes that involves BNIP3

Author keywords

Beclin 1; BNIP3; Calprotectin; Lysosomal activation; Mitochondrial membrane potential; S100A8 A9

Indexed keywords

3 METHYLADENINE; 3-METHYLADENINE; ADENINE; ATG12 PROTEIN, HUMAN; ATG5 PROTEIN, HUMAN; BAFILOMYCIN A1; BNIP3 PROTEIN, HUMAN; CALGRANULIN A; CALGRANULIN B; DRUG DERIVATIVE; MACROLIDE; MEMBRANE PROTEIN; MICROTUBULE ASSOCIATED PROTEIN; ONCOPROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REACTIVE OXYGEN METABOLITE; SUMO PROTEIN;

EID: 77949270765     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2009.129     Document Type: Article
Times cited : (204)

References (76)
  • 1
    • 0034948738 scopus 로고    scopus 로고
    • The autophagosomal-lysosomal compartment in programmed cell death
    • Bursch W. The autophagosomal-lysosomal compartment in programmed cell death. Cell Death Differ 2001; 8:569-581.
    • (2001) Cell Death Differ , vol.8 , pp. 569-581
    • Bursch, W.1
  • 2
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: From caspases to alternative mechanisms
    • Leist M, Jaattela M. Four deaths and a funeral: from caspases to alternative mechanisms. Nat Rev Mol Cell Biol 2001; 2:589-598.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 589-598
    • Leist, M.1    Jaattela, M.2
  • 3
    • 0142027948 scopus 로고    scopus 로고
    • Ways of dying: Multiple pathways to apoptosis
    • Adams JM. Ways of dying: multiple pathways to apoptosis. Genes Dev 2003; 17:2481-2495.
    • (2003) Genes Dev , vol.17 , pp. 2481-2495
    • Adams, J.M.1
  • 4
    • 68049143304 scopus 로고    scopus 로고
    • Apoptosis and cancer: Mutations within caspase genes
    • Ghavami S, Hashemi M, Ande SR, et al. Apoptosis and cancer: mutations within caspase genes. J Med Genet 2009; 46:497-510.
    • (2009) J Med Genet , vol.46 , pp. 497-510
    • Ghavami, S.1    Hashemi, M.2    Ande, S.R.3
  • 5
    • 33846396238 scopus 로고    scopus 로고
    • Cytotoxic effects of intra and extracellular zinc chelation on human breast cancer cells
    • Hashemi M, Ghavami S, Eshraghi M, Booy EP, Los M. Cytotoxic effects of intra and extracellular zinc chelation on human breast cancer cells. Eur J Pharmacol 2007; 557:9-19.
    • (2007) Eur J Pharmacol , vol.557 , pp. 9-19
    • Hashemi, M.1    Ghavami, S.2    Eshraghi, M.3    Booy, E.P.4    Los, M.5
  • 6
    • 28144454326 scopus 로고    scopus 로고
    • Apoptosis in liver diseases - Detection and therapeutic applications
    • Ghavami S, Hashemi M, Kadkhoda K, et al. Apoptosis in liver diseases - detection and therapeutic applications. Med Sci Monit 2005; 11:RA337-RA345.
    • (2005) Med Sci Monit , vol.11
    • Ghavami, S.1    Hashemi, M.2    Kadkhoda, K.3
  • 7
    • 34247371033 scopus 로고    scopus 로고
    • Cell survival, cell death and cell cycle pathways are interconnected: Implications for cancer therapy
    • Maddika S, Ande SR, Panigrahi S, et al. Cell survival, cell death and cell cycle pathways are interconnected: Implications for cancer therapy. Drug Resist Updat 2007; 10:13-29.
    • (2007) Drug Resist Updat , vol.10 , pp. 13-29
    • Maddika, S.1    Ande, S.R.2    Panigrahi, S.3
  • 8
    • 33947658447 scopus 로고    scopus 로고
    • Therapeutic targets in the mitochondrial apoptotic pathway
    • Hacker G, Paschen SA. Therapeutic targets in the mitochondrial apoptotic pathway. Expert Opin Ther Targets 2007; 11:515-526.
    • (2007) Expert Opin Ther Targets , vol.11 , pp. 515-526
    • Hacker, G.1    Paschen, S.A.2
  • 9
    • 38349040141 scopus 로고    scopus 로고
    • S100A8/9 induces cell death via a novel, RAGE-independent pathway that involves selective release of Smac/DIABLO and Omi/HtrA2
    • Ghavami S, Kerkhoff C, Chazin WJ, et al. S100A8/9 induces cell death via a novel, RAGE-independent pathway that involves selective release of Smac/DIABLO and Omi/HtrA2. Biochim Biophys Acta 2008; 1783:297-311.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 297-311
    • Ghavami, S.1    Kerkhoff, C.2    Chazin, W.J.3
  • 10
    • 0037636369 scopus 로고    scopus 로고
    • Mitochondrial membrane potential regulates matrix configuration and cytochrome c release during apoptosis
    • Gottlieb E, Armour SM, Harris MH, Thompson CB. Mitochondrial membrane potential regulates matrix configuration and cytochrome c release during apoptosis. Cell Death Differ 2003; 10:709-717.
    • (2003) Cell Death Differ , vol.10 , pp. 709-717
    • Gottlieb, E.1    Armour, S.M.2    Harris, M.H.3    Thompson, C.B.4
  • 11
    • 46549086527 scopus 로고    scopus 로고
    • Mitochondrial death pathways in yeast and mammalian cells
    • Cheng WC, Leach KM, Hardwick JM. Mitochondrial death pathways in yeast and mammalian cells. Biochim Biophys Acta 2008; 1783:1272-1279.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 1272-1279
    • Cheng, W.C.1    Leach, K.M.2    Hardwick, J.M.3
  • 12
    • 3042740431 scopus 로고    scopus 로고
    • Mechanism of apoptosis induced by S100A8/A9 in colon cancer cell lines: The role of ROS and the effect of metal ions
    • Ghavami S, Kerkhoff C, Los M, et al. Mechanism of apoptosis induced by S100A8/A9 in colon cancer cell lines: the role of ROS and the effect of metal ions. J Leukoc Biol 2004; 76:169-175.
    • (2004) J Leukoc Biol , vol.76 , pp. 169-175
    • Ghavami, S.1    Kerkhoff, C.2    Los, M.3
  • 13
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • Klionsky DJ, Emr SD. Autophagy as a regulated pathway of cellular degradation. Science 2000; 290:1717-1721.
    • (2000) Science , vol.290 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 14
    • 0347626252 scopus 로고    scopus 로고
    • Autophagy: A regulated bulk degradation process inside cells
    • Yoshimori T. Autophagy: a regulated bulk degradation process inside cells. Biochem Biophys Res Commun 2004; 313:453-458.
    • (2004) Biochem Biophys Res Commun , vol.313 , pp. 453-458
    • Yoshimori, T.1
  • 15
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N, Levine B, Cuervo AM, Klionsky DJ. Autophagy fights disease through cellular self-digestion. Nature 2008; 451:1069-1075.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 16
    • 0031036896 scopus 로고    scopus 로고
    • Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease
    • Anglade P, Vyas S, Javoy-Agid F, et al. Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease. Histol Histopathol 1997; 12:25-31.
    • (1997) Histol Histopathol , vol.12 , pp. 25-31
    • Anglade, P.1    Vyas, S.2    Javoy-Agid, F.3
  • 17
    • 0034304390 scopus 로고    scopus 로고
    • The endosomal-lysosomal system of neurons in Alzheimer's disease pathogenesis: A review
    • Nixon RA, Cataldo AM, Mathews PM. The endosomal-lysosomal system of neurons in Alzheimer's disease pathogenesis: a review. Neurochem Res 2000; 25:1161-1172.
    • (2000) Neurochem Res , vol.25 , pp. 1161-1172
    • Nixon, R.A.1    Cataldo, A.M.2    Mathews, P.M.3
  • 19
    • 33845868493 scopus 로고    scopus 로고
    • S100 proteins expressed in phagocytes: A novel group of damage-associated molecular pattern molecules
    • Foell D, Wittkowski H, Vogl T, Roth J. S100 proteins expressed in phagocytes: a novel group of damage-associated molecular pattern molecules. J Leukoc Biol 2007; 81:28-37.
    • (2007) J Leukoc Biol , vol.81 , pp. 28-37
    • Foell, D.1    Wittkowski, H.2    Vogl, T.3    Roth, J.4
  • 20
    • 0032435515 scopus 로고    scopus 로고
    • Novel insights into structure and function of MRP8 (S100A8) and MRP14 (S100A9)
    • Kerkhoff C, Klempt M, Sorg C. Novel insights into structure and function of MRP8 (S100A8) and MRP14 (S100A9). Biochim Biophys Acta 1998; 1448:200-211.
    • (1998) Biochim Biophys Acta , vol.1448 , pp. 200-211
    • Kerkhoff, C.1    Klempt, M.2    Sorg, C.3
  • 21
    • 0025143194 scopus 로고
    • Antimicrobial actions of calcium binding leucocyte L1 protein, calprotectin
    • Steinbakk M, Naess-Andresen CF, Lingaas E, et al. Antimicrobial actions of calcium binding leucocyte L1 protein, calprotectin. Lancet 1990; 336:763-765.
    • (1990) Lancet , vol.336 , pp. 763-765
    • Steinbakk, M.1    Naess-Andresen, C.F.2    Lingaas, E.3
  • 22
    • 14644404879 scopus 로고    scopus 로고
    • The arachidonic acid-binding protein S100A8/A9 promotes NADPH oxidase activation by interaction with p67phox and Rac-2
    • Kerkhoff C, Nacken W, Benedyk M, et al. The arachidonic acid-binding protein S100A8/A9 promotes NADPH oxidase activation by interaction with p67phox and Rac-2. FASEB J 2005; 19:467-469.
    • (2005) FASEB J , vol.19 , pp. 467-469
    • Kerkhoff, C.1    Nacken, W.2    Benedyk, M.3
  • 23
    • 38349052450 scopus 로고    scopus 로고
    • S100A8/A9 at low concentration promotes tumor cell growth via RAGE ligation and MAP kinase-dependent pathway
    • Ghavami S, Rashedi I, Dattilo BM, et al. S100A8/A9 at low concentration promotes tumor cell growth via RAGE ligation and MAP kinase-dependent pathway. J Leukoc Biol 2008; 83:1484-1492.
    • (2008) J Leukoc Biol , vol.83 , pp. 1484-1492
    • Ghavami, S.1    Rashedi, I.2    Dattilo, B.M.3
  • 24
    • 0034704068 scopus 로고    scopus 로고
    • Coregulation of neurite outgrowth and cell survival by amphoterin and S100 proteins through receptor for advanced glycation end products (RAGE) activation
    • Huttunen HJ, Kuja-Panula J, Sorci G, et al. Coregulation of neurite outgrowth and cell survival by amphoterin and S100 proteins through receptor for advanced glycation end products (RAGE) activation. J Biol Chem 2000; 275:40096-40105.
    • (2000) J Biol Chem , vol.275 , pp. 40096-40105
    • Huttunen, H.J.1    Kuja-Panula, J.2    Sorci, G.3
  • 25
    • 1842421190 scopus 로고    scopus 로고
    • S100B causes apoptosis in a myoblast cell line in a RAGEindependent manner
    • Sorci G, Riuzzi F, Agneletti AL, Marchetti C, Donato R. S100B causes apoptosis in a myoblast cell line in a RAGEindependent manner. J Cell Physiol 2004; 199:274-283.
    • (2004) J Cell Physiol , vol.199 , pp. 274-283
    • Sorci, G.1    Riuzzi, F.2    Agneletti, A.L.3    Marchetti, C.4    Donato, R.5
  • 26
    • 19944434059 scopus 로고    scopus 로고
    • Inhibition of macroautophagy triggers apoptosis
    • Boya P, Gonzalez-Polo RA, Casares N, et al. Inhibition of macroautophagy triggers apoptosis. Mol Cell Biol 2005; 25:1025-1040.
    • (2005) Mol Cell Biol , vol.25 , pp. 1025-1040
    • Boya, P.1    Gonzalez-Polo, R.A.2    Casares, N.3
  • 27
    • 34249798692 scopus 로고    scopus 로고
    • Autophagic and apoptotic response to stress signals in mammalian cells
    • Ferraro E, Cecconi F. Autophagic and apoptotic response to stress signals in mammalian cells. Arch Biochem Biophys 2007; 462:210-219.
    • (2007) Arch Biochem Biophys , vol.462 , pp. 210-219
    • Ferraro, E.1    Cecconi, F.2
  • 28
    • 0037946767 scopus 로고    scopus 로고
    • Messengers of cell death: Apoptotic signaling in health and disease
    • Rossi D, Gaidano G. Messengers of cell death: apoptotic signaling in health and disease. Haematologica 2003; 88:212-218.
    • (2003) Haematologica , vol.88 , pp. 212-218
    • Rossi, D.1    Gaidano, G.2
  • 29
    • 0025726216 scopus 로고
    • A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry
    • Nicoletti I, Migliorati G, Pagliacci MC, Grignani F, Riccardi C. A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry. J Immunol Methods 1991; 139:271-279.
    • (1991) J Immunol Methods , vol.139 , pp. 271-279
    • Nicoletti, I.1    Migliorati, G.2    Pagliacci, M.C.3    Grignani, F.4    Riccardi, C.5
  • 30
    • 33645237577 scopus 로고    scopus 로고
    • Caspase-7 is directly activated by the approximately 700-kDa apoptosome complex and is released as a stable XIAP-caspase-7 approximately 200-kDa complex
    • Twiddy D, Cohen GM, Macfarlane M, Cain K. Caspase-7 is directly activated by the approximately 700-kDa apoptosome complex and is released as a stable XIAP-caspase-7 approximately 200-kDa complex. J Biol Chem 2006; 281:3876-3888.
    • (2006) J Biol Chem , vol.281 , pp. 3876-3888
    • Twiddy, D.1    Cohen, G.M.2    MacFarlane, M.3    Cain, K.4
  • 31
    • 0030044012 scopus 로고    scopus 로고
    • Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32
    • Lippke JA, Gu Y, Sarnecki C, Caron PR, Su MS. Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32. J Biol Chem 1996; 271:1825-1828.
    • (1996) J Biol Chem , vol.271 , pp. 1825-1828
    • Lippke, J.A.1    Gu, Y.2    Sarnecki, C.3    Caron, P.R.4    Su, M.S.5
  • 32
    • 3242806104 scopus 로고    scopus 로고
    • Caspases and cancer: Mechanisms of inactivation and new treatment modalities
    • Philchenkov A, Zavelevich M, Kroczak TJ, Los M. Caspases and cancer: mechanisms of inactivation and new treatment modalities. Exp Oncol 2004; 26:82-97.
    • (2004) Exp Oncol , vol.26 , pp. 82-97
    • Philchenkov, A.1    Zavelevich, M.2    Kroczak, T.J.3    Los, M.4
  • 33
    • 0035933619 scopus 로고    scopus 로고
    • Cleaved caspase-3, caspase-7 and poly (ADP-ribose) polymerase are complementarily but differentially expressed in human medulloblastomas
    • Puig B, Tortosa A, Ferrer I. Cleaved caspase-3, caspase-7 and poly (ADP-ribose) polymerase are complementarily but differentially expressed in human medulloblastomas. Neurosci Lett 2001; 306:85-88.
    • (2001) Neurosci Lett , vol.306 , pp. 85-88
    • Puig, B.1    Tortosa, A.2    Ferrer, I.3
  • 34
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • Levine B, Klionsky DJ. Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev Cell 2004; 6:463-477.
    • (2004) Dev Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 35
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: A double-edged sword
    • Shintani T, Klionsky DJ. Autophagy in health and disease: a double-edged sword. Science 2004; 306:990-995.
    • (2004) Science , vol.306 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 36
    • 0037166241 scopus 로고    scopus 로고
    • Formation of the approximately 350-kDa Apg12-Apg5.Apg16 multimeric complex, mediated by Apg16 oligomerization, is essential for autophagy in yeast
    • Kuma A, Mizushima N, Ishihara N, Ohsumi Y. Formation of the approximately 350-kDa Apg12-Apg5.Apg16 multimeric complex, mediated by Apg16 oligomerization, is essential for autophagy in yeast. J Biol Chem 2002; 277:18619-18625.
    • (2002) J Biol Chem , vol.277 , pp. 18619-18625
    • Kuma, A.1    Mizushima, N.2    Ishihara, N.3    Ohsumi, Y.4
  • 37
    • 0035911162 scopus 로고    scopus 로고
    • Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells
    • Mizushima N, Yamamoto A, Hatano M, et al. Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells. J Cell Biol 2001; 152:657-668.
    • (2001) J Cell Biol , vol.152 , pp. 657-668
    • Mizushima, N.1    Yamamoto, A.2    Hatano, M.3
  • 38
    • 0141960205 scopus 로고    scopus 로고
    • The mouse APG10 homolog, an E2-like enzyme for Apg12p conjugation, facilitates MAP-LC3 modification
    • Nemoto T, Tanida I, Tanida-Miyake E, et al. The mouse APG10 homolog, an E2-like enzyme for Apg12p conjugation, facilitates MAP-LC3 modification. J Biol Chem 2003; 278:39517-39526.
    • (2003) J Biol Chem , vol.278 , pp. 39517-39526
    • Nemoto, T.1    Tanida, I.2    Tanida-Miyake, E.3
  • 39
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homolog of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya Y, Mizushima N, Ueno T, et al. LC3, a mammalian homolog of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 2000; 19:5720-5728.
    • (2000) EMBO J , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3
  • 40
    • 0032701984 scopus 로고    scopus 로고
    • Formation process of autophagosome is traced with Apg8/Aut7p in yeast
    • Kirisako T, Baba M, Ishihara N, et al. Formation process of autophagosome is traced with Apg8/Aut7p in yeast. J Cell Biol 1999; 147:435-446.
    • (1999) J Cell Biol , vol.147 , pp. 435-446
    • Kirisako, T.1    Baba, M.2    Ishihara, N.3
  • 41
    • 0035809160 scopus 로고    scopus 로고
    • Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase y sorting in Saccharomyces cerevisiae
    • Kihara A, Noda T, Ishihara N, Ohsumi Y. Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae. J Cell Biol 2001; 152:519-530.
    • (2001) J Cell Biol , vol.152 , pp. 519-530
    • Kihara, A.1    Noda, T.2    Ishihara, N.3    Ohsumi, Y.4
  • 42
    • 0000906170 scopus 로고    scopus 로고
    • Induction of autophagy and inhibition of tumorigenesis by Beclin 1
    • Liang XH, Jackson S, Seaman M, et al. Induction of autophagy and inhibition of tumorigenesis by Beclin 1. Nature 1999; 402:672-676.
    • (1999) Nature , vol.402 , pp. 672-676
    • Liang, X.H.1    Jackson, S.2    Seaman, M.3
  • 43
    • 0347986620 scopus 로고    scopus 로고
    • Class III phosphoinositide 3-kinase-Beclin1 complex mediates the amino acid-dependent regulation of autophagy in C2C12 myotubes
    • Tassa A, Roux MP, Attaix D, Bechet DM. Class III phosphoinositide 3-kinase-Beclin1 complex mediates the amino acid-dependent regulation of autophagy in C2C12 myotubes. Biochem J 2003; 376 (Part 3):577-586.
    • (2003) Biochem J , vol.376 , Issue.PART 3 , pp. 577-586
    • Tassa, A.1    Roux, M.P.2    Attaix, D.3    Bechet, D.M.4
  • 44
    • 36248987708 scopus 로고    scopus 로고
    • Akt is transferred to the nucleus of cells treated with apoptin, and it participates in apoptin-induced cell death
    • Maddika S, Bay GH, Kroczak TJ, et al. Akt is transferred to the nucleus of cells treated with apoptin, and it participates in apoptin-induced cell death. Cell Prolif 2007; 40:835-848.
    • (2007) Cell Prolif , vol.40 , pp. 835-848
    • Maddika, S.1    Bay, G.H.2    Kroczak, T.J.3
  • 45
    • 43449130891 scopus 로고    scopus 로고
    • Interaction with PI3- kinase contributes to the cytotoxic activity of apoptin
    • Maddika S, Wiechec E, Ande SR, et al. Interaction with PI3- kinase contributes to the cytotoxic activity of apoptin. Oncogene 2008; 27:3060-3065.
    • (2008) Oncogene , vol.27 , pp. 3060-3065
    • Maddika, S.1    Wiechec, E.2    Ande, S.R.3
  • 46
    • 0033791650 scopus 로고    scopus 로고
    • Autophagy, cytoplasm-to-vacuole targeting pathway, and pexophagy in yeast and mammalian cells
    • Kim J, Klionsky DJ. Autophagy, cytoplasm-to-vacuole targeting pathway, and pexophagy in yeast and mammalian cells. Annu Rev Biochem 2000; 69:303-342.
    • (2000) Annu Rev Biochem , vol.69 , pp. 303-342
    • Kim, J.1    Klionsky, D.J.2
  • 47
    • 27644494779 scopus 로고    scopus 로고
    • Regulation of S100A8/A9 (calprotectin) binding to tumor cells by zinc ion and its implication for apoptosis-inducing activity
    • Nakatani Y, Yamazaki M, Chazin WJ, Yui S. Regulation of S100A8/A9 (calprotectin) binding to tumor cells by zinc ion and its implication for apoptosis-inducing activity. Mediators Inflamm 2005; 2005:280-292.
    • (2005) Mediators Inflamm , vol.2005 , pp. 280-292
    • Nakatani, Y.1    Yamazaki, M.2    Chazin, W.J.3    Yui, S.4
  • 48
    • 0035999163 scopus 로고    scopus 로고
    • Implication of extracellular zinc exclusion by recombinant human calprotectin (MRP8 and MRP14) from target cells in its apoptosis-inducing activity
    • Yui S, Nakatani Y, Hunter MJ, Chazin WJ, Yamazaki M. Implication of extracellular zinc exclusion by recombinant human calprotectin (MRP8 and MRP14) from target cells in its apoptosis-inducing activity. Mediators Inflamm 2002; 11:165-172.
    • (2002) Mediators Inflamm , vol.11 , pp. 165-172
    • Yui, S.1    Nakatani, Y.2    Hunter, M.J.3    Chazin, W.J.4    Yamazaki, M.5
  • 49
    • 0036661021 scopus 로고    scopus 로고
    • Apoptotic pathways: Involvement of lysosomal proteases
    • Turk B, Stoka V, Rozman-Pungercar J, et al. Apoptotic pathways: involvement of lysosomal proteases. Biol Chem 2002; 383:1035-1044.
    • (2002) Biol Chem , vol.383 , pp. 1035-1044
    • Turk, B.1    Stoka, V.2    Rozman-Pungercar, J.3
  • 50
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: More than scavengers
    • Turk B, Turk D, Turk V. Lysosomal cysteine proteases: more than scavengers. Biochim Biophys Acta 2000; 1477:98-111.
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 51
    • 44149121946 scopus 로고    scopus 로고
    • Brevinin-2R(1) semi-selectively kills cancer cells by a distinct mechanism, which involves the lysosomal-mitochondrial death pathway
    • Ghavami S, Asoodeh A, Klonisch T, et al. Brevinin-2R(1) semi-selectively kills cancer cells by a distinct mechanism, which involves the lysosomal-mitochondrial death pathway. J Cell Mol Med 2008; 12:1005-1022.
    • (2008) J Cell Mol Med , vol.12 , pp. 1005-1022
    • Ghavami, S.1    Asoodeh, A.2    Klonisch, T.3
  • 52
    • 0033984094 scopus 로고    scopus 로고
    • BNIP3 heterodimerizes with Bcl-2/Bcl-X(L) and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites
    • Ray R, Chen G, Vande Velde C, et al. BNIP3 heterodimerizes with Bcl-2/Bcl-X(L) and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites. J Biol Chem 2000; 275:1439-1448.
    • (2000) J Biol Chem , vol.275 , pp. 1439-1448
    • Ray, R.1    Chen, G.2    Vande Velde, C.3
  • 53
    • 34249886312 scopus 로고    scopus 로고
    • HIF-1alpha activation by a redoxsensitive pathway mediates cyanide-induced BNIP3 upregulation and mitochondrial-dependent cell death
    • Zhang L, Li L, Liu H, et al. HIF-1alpha activation by a redoxsensitive pathway mediates cyanide-induced BNIP3 upregulation and mitochondrial-dependent cell death. Free Radic Biol Med 2007; 43:117-127.
    • (2007) Free Radic Biol Med , vol.43 , pp. 117-127
    • Zhang, L.1    Li, L.2    Liu, H.3
  • 54
    • 60549109843 scopus 로고    scopus 로고
    • Role of BNIP3 in TNF-induced cell death-TNF upregulates BNIP3 expression
    • Ghavami S, Eshraghi M, Kadkhoda K, et al. Role of BNIP3 in TNF-induced cell death-TNF upregulates BNIP3 expression. Biochim Biophys Acta 2009; 1793:546-560.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 546-560
    • Ghavami, S.1    Eshraghi, M.2    Kadkhoda, K.3
  • 55
    • 0038267444 scopus 로고    scopus 로고
    • CD47 and the 19 kDa interacting protein-3 (BNIP3) in T cell apoptosis
    • Lamy L, Ticchioni M, Rouquette-Jazdanian AK, et al. CD47 and the 19 kDa interacting protein-3 (BNIP3) in T cell apoptosis. J Biol Chem 2003; 278:23915-23921.
    • (2003) J Biol Chem , vol.278 , pp. 23915-23921
    • Lamy, L.1    Ticchioni, M.2    Rouquette-Jazdanian, A.K.3
  • 56
    • 34848920863 scopus 로고    scopus 로고
    • ROS, mitochondria and the regulation of autophagy
    • Scherz-Shouval R, Elazar Z. ROS, mitochondria and the regulation of autophagy. Trends Cell Biol 2007; 17:422-427.
    • (2007) Trends Cell Biol , vol.17 , pp. 422-427
    • Scherz-Shouval, R.1    Elazar, Z.2
  • 57
    • 34250825929 scopus 로고    scopus 로고
    • Oxidation as a posttranslational modification that regulates autophagy
    • Scherz-Shouval R, Shvets E, Elazar Z. Oxidation as a posttranslational modification that regulates autophagy. Autophagy 2007; 3:371-373.
    • (2007) Autophagy , vol.3 , pp. 371-373
    • Scherz-Shouval, R.1    Shvets, E.2    Elazar, Z.3
  • 58
    • 65249176434 scopus 로고    scopus 로고
    • BNIP3 (Bcl-2 19 kDa interacting protein) acts as transcriptional repressor of apoptosis- inducing factor expression preventing cell death in human malignant gliomas
    • Burton TR, Eisenstat DD, Gibson SB. BNIP3 (Bcl-2 19 kDa interacting protein) acts as transcriptional repressor of apoptosis- inducing factor expression preventing cell death in human malignant gliomas. J Neurosci 2009; 29:4189-4199.
    • (2009) J Neurosci , vol.29 , pp. 4189-4199
    • Burton, T.R.1    Eisenstat, D.D.2    Gibson, S.B.3
  • 59
    • 62849105988 scopus 로고    scopus 로고
    • The role of Bcl-2 family member BNIP3 in cell death and disease: NIPping at the heels of cell death
    • Burton TR, Gibson SB. The role of Bcl-2 family member BNIP3 in cell death and disease: NIPping at the heels of cell death. Cell Death Differ 2009; 16:515-523.
    • (2009) Cell Death Differ , vol.16 , pp. 515-523
    • Burton, T.R.1    Gibson, S.B.2
  • 60
    • 0035814933 scopus 로고    scopus 로고
    • Mitochondria are selectively eliminated from eukaryotic cells after blockade of caspases during apoptosis
    • Xue L, Fletcher GC, Tolkovsky AM. Mitochondria are selectively eliminated from eukaryotic cells after blockade of caspases during apoptosis. Curr Biol 2001; 11:361-365.
    • (2001) Curr Biol , vol.11 , pp. 361-365
    • Xue, L.1    Fletcher, G.C.2    Tolkovsky, A.M.3
  • 61
    • 0034849783 scopus 로고    scopus 로고
    • Autophagic cell death and its execution by lysosomal cathepsins
    • Uchiyama Y. Autophagic cell death and its execution by lysosomal cathepsins. Arch Histol Cytol 2001; 64:233-246.
    • (2001) Arch Histol Cytol , vol.64 , pp. 233-246
    • Uchiyama, Y.1
  • 62
    • 2642553881 scopus 로고    scopus 로고
    • Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8
    • Yu L, Alva A, Su H, et al. Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8. Science 2004; 304:1500-1502.
    • (2004) Science , vol.304 , pp. 1500-1502
    • Yu, L.1    Alva, A.2    Su, H.3
  • 63
    • 10344262564 scopus 로고    scopus 로고
    • Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes
    • Shimizu S, Kanaseki T, Mizushima N, et al. Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes. Nat Cell Biol 2004; 6:1221-1228.
    • (2004) Nat Cell Biol , vol.6 , pp. 1221-1228
    • Shimizu, S.1    Kanaseki, T.2    Mizushima, N.3
  • 64
    • 25144457455 scopus 로고    scopus 로고
    • Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy
    • Pattingre S, Tassa A, Qu X, et al. Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy. Cell 2005; 122:927-939.
    • (2005) Cell , vol.122 , pp. 927-939
    • Pattingre, S.1    Tassa, A.2    Qu, X.3
  • 65
  • 66
    • 34547471625 scopus 로고    scopus 로고
    • Bnip3 mediates mitochondrial dysfunction and cell death through Bax and Bak
    • Kubli DA, Ycaza JE, Gustafsson AB. Bnip3 mediates mitochondrial dysfunction and cell death through Bax and Bak. Biochem J 2007; 405:407-415.
    • (2007) Biochem J , vol.405 , pp. 407-415
    • Kubli, D.A.1    Ycaza, J.E.2    Gustafsson, A.B.3
  • 67
    • 0038239701 scopus 로고    scopus 로고
    • Selective degradation of oxidatively modified protein substrates by the proteasome
    • Grune T, Merker K, Sandig G, Davies KJ. Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem Biophys Res Commun 2003; 305:709-718.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 709-718
    • Grune, T.1    Merker, K.2    Sandig, G.3    Davies, K.J.4
  • 69
    • 0030045552 scopus 로고    scopus 로고
    • Properties of the endosomal-lysosomal system in the human central nervous system: Disturbances mark most neurons in populations at risk to degenerate in Alzheimer's disease
    • Cataldo AM, Hamilton DJ, Barnett JL, Paskevich PA, Nixon RA. Properties of the endosomal-lysosomal system in the human central nervous system: disturbances mark most neurons in populations at risk to degenerate in Alzheimer's disease. J Neurosci 1996; 16:186-199.
    • (1996) J Neurosci , vol.16 , pp. 186-199
    • Cataldo, A.M.1    Hamilton, D.J.2    Barnett, J.L.3    Paskevich, P.A.4    Nixon, R.A.5
  • 70
    • 2442643788 scopus 로고    scopus 로고
    • Suppression of chaperone-mediated autophagy in the renal cortex during acute diabetes mellitus
    • Sooparb S, Price SR, Shaoguang J, Franch HA. Suppression of chaperone-mediated autophagy in the renal cortex during acute diabetes mellitus. Kidney Int 2004; 65:2135-2144.
    • (2004) Kidney Int , vol.65 , pp. 2135-2144
    • Sooparb, S.1    Price, S.R.2    Shaoguang, J.3    Franch, H.A.4
  • 71
    • 0031943314 scopus 로고    scopus 로고
    • Kinetical analysis of tumor cell death-inducing mechanism by polymorphonuclear leukocyte- derived calprotectin: Involvement of protein synthesis and generation of reactive oxygen species in target cells
    • Mikami M, Yamazaki M, Yui S. Kinetical analysis of tumor cell death-inducing mechanism by polymorphonuclear leukocyte- derived calprotectin: involvement of protein synthesis and generation of reactive oxygen species in target cells. Microbiol Immunol 1998; 42:211-221.
    • (1998) Microbiol Immunol , vol.42 , pp. 211-221
    • Mikami, M.1    Yamazaki, M.2    Yui, S.3
  • 72
    • 0032701911 scopus 로고    scopus 로고
    • The two calciumbinding proteins, S100A8 and S100A9, are involved in the metabolism of arachidonic acid in human neutrophils
    • Kerkhoff C, Klempt M, Kaever V, Sorg C. The two calciumbinding proteins, S100A8 and S100A9, are involved in the metabolism of arachidonic acid in human neutrophils. J Biol Chem 1999; 274:32672-32679.
    • (1999) J Biol Chem , vol.274 , pp. 32672-32679
    • Kerkhoff, C.1    Klempt, M.2    Kaever, V.3    Sorg, C.4
  • 73
    • 0032524649 scopus 로고    scopus 로고
    • High level expression and dimer characterization of the S100 EF-hand proteins, migration inhibitory factor-related proteins 8 and 14
    • Hunter MJ, Chazin WJ. High level expression and dimer characterization of the S100 EF-hand proteins, migration inhibitory factor-related proteins 8 and 14. J Biol Chem 1998; 273:12427-12435.
    • (1998) J Biol Chem , vol.273 , pp. 12427-12435
    • Hunter, M.J.1    Chazin, W.J.2
  • 74
    • 27144508384 scopus 로고    scopus 로고
    • Monitoring of programmed cell death in vivo and in vitro-new and old methods of cancer therapy assessment
    • Los M, Gibson SB, edsNew York: Springer Science+Business Media Inc
    • Ghavami S, Barczyk K, Maddika S, et al. Monitoring of programmed cell death in vivo and in vitro-new and old methods of cancer therapy assessment. In: Los M, Gibson SB, eds. Apoptotic Pathways as Target for Novel Therapies in Cancer and Other Diseases. New York: Springer Science+Business Media Inc., 2005:323-341.
    • (2005) Apoptotic Pathways As Target for Novel Therapies in Cancer and Other Diseases , pp. 323-341
    • Ghavami, S.1    Barczyk, K.2    Maddika, S.3
  • 75
    • 61749088475 scopus 로고    scopus 로고
    • Unscheduled Akttriggered activation of cyclin-dependent kinase 2 as a key effector mechanism of apoptin's anticancer toxicity
    • Maddika S, Panigrahi S, Wiechec E, et al. Unscheduled Akttriggered activation of cyclin-dependent kinase 2 as a key effector mechanism of apoptin's anticancer toxicity. Mol Cell Biol 2009; 29:1235-1248.
    • (2009) Mol Cell Biol , vol.29 , pp. 1235-1248
    • Maddika, S.1    Panigrahi, S.2    Wiechec, E.3
  • 76
    • 43149102480 scopus 로고    scopus 로고
    • Akt-mediated phosphorylation of CDK2 regulates its dual role in cell cycle progression and apoptosis
    • Maddika S, Ande SR, Wiechec E, et al. Akt-mediated phosphorylation of CDK2 regulates its dual role in cell cycle progression and apoptosis. J Cell Sci 2008; 121 (Part 7):979-988.
    • (2008) J Cell Sci , vol.121 , Issue.PART 7 , pp. 979-988
    • Maddika, S.1    Ande, S.R.2    Wiechec, E.3


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