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Volumn 58, Issue 3, 2009, Pages 431-442

Mechanisms regulating cytochrome c release in pancreatic mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CHOLECYSTOKININ OCTAPEPTIDE; CYTOCHROME C; REACTIVE OXYGEN METABOLITE;

EID: 61649090733     PISSN: 00175749     EISSN: 14683288     Source Type: Journal    
DOI: 10.1136/gut.2007.147207     Document Type: Article
Times cited : (63)

References (66)
  • 1
    • 11844301338 scopus 로고    scopus 로고
    • Cell death pathways in pancreatitis and pancreatic cancer
    • Gukovskaya AS, Pandol SJ. Cell death pathways in pancreatitis and pancreatic cancer. Pancreatology 2004;4:567-86.
    • (2004) Pancreatology , vol.4 , pp. 567-586
    • Gukovskaya, A.S.1    Pandol, S.J.2
  • 2
    • 14644408674 scopus 로고    scopus 로고
    • Early events in acute pancreatitis
    • Halangk W, Lerch MM. Early events in acute pancreatitis. Clin Lab Med 2005;25:1-15.
    • (2005) Clin Lab Med , vol.25 , pp. 1-15
    • Halangk, W.1    Lerch, M.M.2
  • 3
    • 0028783295 scopus 로고
    • Relationship between severity, necrosis, and apoptosis in five models of experimental acute pancreatitis
    • Kaiser AM, Saluja AK, Sengupta A, et al. Relationship between severity, necrosis, and apoptosis in five models of experimental acute pancreatitis. Am J Physiol Cell Physiol 1995;269:C1295-304.
    • (1995) Am J Physiol Cell Physiol , vol.269
    • Kaiser, A.M.1    Saluja, A.K.2    Sengupta, A.3
  • 4
    • 0030025675 scopus 로고    scopus 로고
    • Mechanisms of cell death after pancreatic duct obstruction in the opossum and the rat
    • Gukovskaya AS, Perkins P, Zaninovic V, et al. Mechanisms of cell death after pancreatic duct obstruction in the opossum and the rat. Gastroenterology 1996;110:875-84.
    • (1996) Gastroenterology , vol.110 , pp. 875-884
    • Gukovskaya, A.S.1    Perkins, P.2    Zaninovic, V.3
  • 5
    • 0029841658 scopus 로고    scopus 로고
    • The role of neutrophils and platelet-activating factor in mediating experimental pancreatis
    • Sandoval D, Gukovskaya A, Reavey P, et al. The role of neutrophils and platelet-activating factor in mediating experimental pancreatis. Gastroenterology 1996;111:1081-91.
    • (1996) Gastroenterology , vol.111 , pp. 1081-1091
    • Sandoval, D.1    Gukovskaya, A.2    Reavey, P.3
  • 8
    • 33645640921 scopus 로고    scopus 로고
    • Cell death in pancreatitis: Caspases protect from necrotizing pancreatitis
    • Mareninova OA, Sung KF, Hong P, et al. Cell death in pancreatitis: caspases protect from necrotizing pancreatitis. J Biol Chem 2006;281:3370-81.
    • (2006) J Biol Chem , vol.281 , pp. 3370-3381
    • Mareninova, O.A.1    Sung, K.F.2    Hong, P.3
  • 9
    • 0037151017 scopus 로고    scopus 로고
    • Cholecystokinin induces caspase activation and mitochondrial dysfunction in pancreatic acinar cells. Roles in cell injury processes of pancreatitis
    • Gukovskaya AS, Gukovsky I, Jung Y, et al. Cholecystokinin induces caspase activation and mitochondrial dysfunction in pancreatic acinar cells. Roles in cell injury processes of pancreatitis. J Biol Chem 2002;277:22595-604.
    • (2002) J Biol Chem , vol.277 , pp. 22595-22604
    • Gukovskaya, A.S.1    Gukovsky, I.2    Jung, Y.3
  • 10
    • 0029971046 scopus 로고    scopus 로고
    • Induction of apoptosis reduces the severity of caerulein-induced pancreatitis in mice
    • Saluja A, Hofbauer B, Yamaguchi Y, et al. Induction of apoptosis reduces the severity of caerulein-induced pancreatitis in mice. Biochem Biophys Res Commun 1996;220:875-8.
    • (1996) Biochem Biophys Res Commun , vol.220 , pp. 875-878
    • Saluja, A.1    Hofbauer, B.2    Yamaguchi, Y.3
  • 11
    • 0032546484 scopus 로고    scopus 로고
    • Induction of apoptosis in pancreatic acinar cells reduces the severity of acute pancreatitis
    • Bhatia M, Wallig MA, Hofbauer B, et al. Induction of apoptosis in pancreatic acinar cells reduces the severity of acute pancreatitis. Biochem Biophys Res Commun 1998;246:476-83.
    • (1998) Biochem Biophys Res Commun , vol.246 , pp. 476-483
    • Bhatia, M.1    Wallig, M.A.2    Hofbauer, B.3
  • 12
    • 0033576675 scopus 로고    scopus 로고
    • More than one way to die: Apoptosis, necrosis and reactive oxygen damage
    • Fiers W, Beyaert R, Declercq W, et al. More than one way to die: apoptosis, necrosis and reactive oxygen damage. Oncogene 1999;18:7719-30.
    • (1999) Oncogene , vol.18 , pp. 7719-7730
    • Fiers, W.1    Beyaert, R.2    Declercq, W.3
  • 13
    • 7744235672 scopus 로고    scopus 로고
    • Death by design: Apoptosis, necrosis and autophagy
    • Edinger AL, Thompson CB. Death by design: apoptosis, necrosis and autophagy. Curr Opin Cell Biol 2004;16:663-9.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 663-669
    • Edinger, A.L.1    Thompson, C.B.2
  • 14
    • 33846018602 scopus 로고    scopus 로고
    • Cell death by necrosis: Towards a molecular definition
    • Golstein P, Kroemer G. Cell death by necrosis: towards a molecular definition. Trends Biochem Sci 2007;32:37-43.
    • (2007) Trends Biochem Sci , vol.32 , pp. 37-43
    • Golstein, P.1    Kroemer, G.2
  • 15
    • 33645420460 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization: The sine qua non for cell death
    • Armstrong JS. Mitochondrial membrane permeabilization: the sine qua non for cell death. Bioessays 2006;28:253-60.
    • (2006) Bioessays , vol.28 , pp. 253-260
    • Armstrong, J.S.1
  • 16
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green DR, Kroemer G. The pathophysiology of mitochondrial cell death. Science 2004;305:626-9.
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 17
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer G, Galluzzi L, Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol Rev 2007;87:99-163.
    • (2007) Physiol Rev , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 18
    • 0030592172 scopus 로고    scopus 로고
    • The permeability transition pore. Control points of a cyclosporin A-sensitive mitochondrial channel involved in cell death
    • Bernardi P. The permeability transition pore. Control points of a cyclosporin A-sensitive mitochondrial channel involved in cell death. Biochim Biophys Acta 1996;1275:5-9.
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 5-9
    • Bernardi, P.1
  • 19
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M. The mitochondrial permeability transition pore and its role in cell death. Biochem J 1999;341:233-49.
    • (1999) Biochem J , vol.341 , pp. 233-249
    • Crompton, M.1
  • 20
    • 0032504709 scopus 로고    scopus 로고
    • Elucidating the molecular mechanism of the permeability transition pore and its role in reperfusion injury of the heart
    • Halestrap AP, Kerr PM, Javadov S, et al. Elucidating the molecular mechanism of the permeability transition pore and its role in reperfusion injury of the heart. Biochim Biophys Acta 1998;1366:79-94.
    • (1998) Biochim Biophys Acta , vol.1366 , pp. 79-94
    • Halestrap, A.P.1    Kerr, P.M.2    Javadov, S.3
  • 21
    • 15844375853 scopus 로고    scopus 로고
    • Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
    • Baines CP, Kaiser RA, Purcell NH, et al. Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 2005;434:658-62.
    • (2005) Nature , vol.434 , pp. 658-662
    • Baines, C.P.1    Kaiser, R.A.2    Purcell, N.H.3
  • 22
    • 15844407874 scopus 로고    scopus 로고
    • Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
    • Nakagawa T, Shimizu S, Watanabe T, et al. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 2005;434:652-8.
    • (2005) Nature , vol.434 , pp. 652-658
    • Nakagawa, T.1    Shimizu, S.2    Watanabe, T.3
  • 23
    • 0035876483 scopus 로고    scopus 로고
    • BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak
    • Zong WX, Lindsten T, Ross AJ, et al. BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes Dev 2001;15:1481-6.
    • (2001) Genes Dev , vol.15 , pp. 1481-1486
    • Zong, W.X.1    Lindsten, T.2    Ross, A.J.3
  • 24
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death
    • Wei MC, Zong WX, Cheng EH, et al. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 2001;292:727-30.
    • (2001) Science , vol.292 , pp. 727-730
    • Wei, M.C.1    Zong, W.X.2    Cheng, E.H.3
  • 25
    • 1342333658 scopus 로고    scopus 로고
    • Signal transduction, calcium and acute pancreatitis
    • Sutton R, Criddle D, Raraty MG, et al. Signal transduction, calcium and acute pancreatitis. Pancreatology 2003;3:497-505.
    • (2003) Pancreatology , vol.3 , pp. 497-505
    • Sutton, R.1    Criddle, D.2    Raraty, M.G.3
  • 26
    • 3042572722 scopus 로고    scopus 로고
    • Acute pancreatitis and organ failure: Pathophysiology, natural history, and management strategies
    • Raraty MG, Connor S, Criddle DN, et al. Acute pancreatitis and organ failure: pathophysiology, natural history, and management strategies. Curr Gastroenterol Rep 2004;6:99-103.
    • (2004) Curr Gastroenterol Rep , vol.6 , pp. 99-103
    • Raraty, M.G.1    Connor, S.2    Criddle, D.N.3
  • 27
    • 0033027090 scopus 로고    scopus 로고
    • Role of oxidative stress in the pathogenesis of caerulein-induced acute pancreatitis
    • Dabrowski A, Konturek SJ, Konturek JW, et al. Role of oxidative stress in the pathogenesis of caerulein-induced acute pancreatitis. Eur J Pharmacol 1999;377:1-11.
    • (1999) Eur J Pharmacol , vol.377 , pp. 1-11
    • Dabrowski, A.1    Konturek, S.J.2    Konturek, J.W.3
  • 28
    • 0032918583 scopus 로고    scopus 로고
    • Oxidative stress affects pancreatic proteins during the early pathogenesis of rat caerulein pancreatitis
    • Reinheckel T, Prause J, Nedelev B, et al. Oxidative stress affects pancreatic proteins during the early pathogenesis of rat caerulein pancreatitis. Digestion 1999;60:56-62.
    • (1999) Digestion , vol.60 , pp. 56-62
    • Reinheckel, T.1    Prause, J.2    Nedelev, B.3
  • 30
    • 46149138125 scopus 로고
    • New technique for the isolation of functional rat pancreatic mitochondria and its application to models of pancreatic injury
    • Wilson JS, Korsten MA, Leo MA, et al. New technique for the isolation of functional rat pancreatic mitochondria and its application to models of pancreatic injury. J Lab Clin Med 1986;107:51-8.
    • (1986) J Lab Clin Med , vol.107 , pp. 51-58
    • Wilson, J.S.1    Korsten, M.A.2    Leo, M.A.3
  • 31
    • 0033011746 scopus 로고    scopus 로고
    • Induction of permeability transition in pancreatic mitochondria by cerulein in rats
    • Schild L, Matthias R, Stanarius A, et al. Induction of permeability transition in pancreatic mitochondria by cerulein in rats. Mol Cell Biochem 1999;195:191-7.
    • (1999) Mol Cell Biochem , vol.195 , pp. 191-197
    • Schild, L.1    Matthias, R.2    Stanarius, A.3
  • 32
    • 0030923560 scopus 로고    scopus 로고
    • Pancreatic acinar cells produce, release, and respond to tumor necrosis factor-alpha. Role in regulating cell death and pancreatitis
    • Gukovskaya AS, Gukovsky I, Zaninovic V, et al. Pancreatic acinar cells produce, release, and respond to tumor necrosis factor-alpha. Role in regulating cell death and pancreatitis. J Clin Invest 1997;100:1853-62.
    • (1997) J Clin Invest , vol.100 , pp. 1853-1862
    • Gukovskaya, A.S.1    Gukovsky, I.2    Zaninovic, V.3
  • 33
    • 0018665167 scopus 로고
    • Membrane potential of mitochondria measured with an electrode sensitive to tetraphenyl phosphonium and relationship between proton electrochemical potential and phosphorylation potential in steady state
    • Kamo N, Muratsugu M, Hongoh R, et al. Membrane potential of mitochondria measured with an electrode sensitive to tetraphenyl phosphonium and relationship between proton electrochemical potential and phosphorylation potential in steady state. J Membr Biol 1979;49:105-21.
    • (1979) J Membr Biol , vol.49 , pp. 105-121
    • Kamo, N.1    Muratsugu, M.2    Hongoh, R.3
  • 34
    • 0345120940 scopus 로고    scopus 로고
    • Measurement of mitochondrial membrane potential using fluorescent rhodamine derivatives
    • Scaduto RCJ, Grotyohann LW. Measurement of mitochondrial membrane potential using fluorescent rhodamine derivatives. Biophys J 1999;76:469-77.
    • (1999) Biophys J , vol.76 , pp. 469-477
    • Scaduto, R.C.J.1    Grotyohann, L.W.2
  • 35
    • 0035051416 scopus 로고    scopus 로고
    • + exchange inhibitor, on the ion transport of myocardial mitochondria
    • + exchange inhibitor, on the ion transport of myocardial mitochondria. Mol Cell Biochem 2001;219:83-90.
    • (2001) Mol Cell Biochem , vol.219 , pp. 83-90
    • Hotta, Y.1    Ishikawa, N.2    Ohashi, N.3
  • 36
    • 0022402287 scopus 로고
    • Swelling and contraction of the mitochondrial matrix. I. A structural interpretation of the relationship between light scattering and matrix volume
    • Beavis AD, Brannan RD, Garlid KD. Swelling and contraction of the mitochondrial matrix. I. A structural interpretation of the relationship between light scattering and matrix volume. J Biol Chem 1985;260:13424- 33.
    • (1985) J Biol Chem , vol.260 , pp. 13424-13433
    • Beavis, A.D.1    Brannan, R.D.2    Garlid, K.D.3
  • 37
    • 0031573401 scopus 로고    scopus 로고
    • A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: Applications in detecting the activity of phagocyte NADPH oxidase and other oxidases
    • Zhou M, Diwu Z, Panchuk-Voloshina N, et al. A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases. Anal Biochem 1997;253:162-8.
    • (1997) Anal Biochem , vol.253 , pp. 162-168
    • Zhou, M.1    Diwu, Z.2    Panchuk-Voloshina, N.3
  • 38
    • 1442349824 scopus 로고    scopus 로고
    • Investigations of phagosomes, mitochondria, and acidic granules in human neutrophils using fluorescent probes
    • Bassoe CF, Li N, Ragheb K, et al. Investigations of phagosomes, mitochondria, and acidic granules in human neutrophils using fluorescent probes. Cytometry B Clin Cytom 2003;51:21-9.
    • (2003) Cytometry B Clin Cytom , vol.51 , pp. 21-29
    • Bassoe, C.F.1    Li, N.2    Ragheb, K.3
  • 39
    • 1342289237 scopus 로고    scopus 로고
    • Methods for detection of reactive metabolites of oxygen and nitrogen: In vitro and in vivo considerations
    • Tarpey MM, Wink DA, Grisham MB. Methods for detection of reactive metabolites of oxygen and nitrogen: in vitro and in vivo considerations. Am J Physiol Regul Integr Comp Physiol 2004;286:R431-R444.
    • (2004) Am J Physiol Regul Integr Comp Physiol , vol.286
    • Tarpey, M.M.1    Wink, D.A.2    Grisham, M.B.3
  • 40
    • 4544250814 scopus 로고    scopus 로고
    • Reactive oxygen species produced by NAD(P)H oxidase inhibit apoptosis in pancreatic cancer cells
    • Vaquero EC, Edderkaoui M, Pandol SJ, et al. Reactive oxygen species produced by NAD(P)H oxidase inhibit apoptosis in pancreatic cancer cells. J Biol Chem 2004;279:34643-54.
    • (2004) J Biol Chem , vol.279 , pp. 34643-34654
    • Vaquero, E.C.1    Edderkaoui, M.2    Pandol, S.J.3
  • 41
    • 0032827410 scopus 로고    scopus 로고
    • Mitochondrial transport of cations: Channels, exchangers, and permeability transition
    • Bernardi P. Mitochondrial transport of cations: channels, exchangers, and permeability transition. Physiol Rev 1999;79:1127- 55.
    • (1999) Physiol Rev , vol.79 , pp. 1127-1155
    • Bernardi, P.1
  • 42
    • 11144300815 scopus 로고    scopus 로고
    • Mitochondrial permeability transitions: How many doors to the house?
    • Zoratti M, Szabo I, De Marchi U. Mitochondrial permeability transitions: how many doors to the house? Biochim Biophys Acta 2005;1706:40-52.
    • (2005) Biochim Biophys Acta , vol.1706 , pp. 40-52
    • Zoratti, M.1    Szabo, I.2    De Marchi, U.3
  • 43
    • 0031918742 scopus 로고    scopus 로고
    • The mitochondrial death/life regulator in apoptosis and necrosis
    • Kroemer G, Dallaporta B, Resche-Rigon M. The mitochondrial death/life regulator in apoptosis and necrosis. Annu Rev Physiol 1998;60:619-42.
    • (1998) Annu Rev Physiol , vol.60 , pp. 619-642
    • Kroemer, G.1    Dallaporta, B.2    Resche-Rigon, M.3
  • 44
    • 1642498301 scopus 로고    scopus 로고
    • Ethanol differentially regulates NFkappaB activation in pancreatic acinar cells through calcium and protein kinase C pathways
    • Gukovskaya AS, Hosseini S, Satoh A, et al. Ethanol differentially regulates NFkappaB activation in pancreatic acinar cells through calcium and protein kinase C pathways. Am J Physiol Gastrointest Liver Physiol 2004;286:G204-13.
    • (2004) Am J Physiol Gastrointest Liver Physiol , vol.286
    • Gukovskaya, A.S.1    Hosseini, S.2    Satoh, A.3
  • 45
    • 11144234843 scopus 로고    scopus 로고
    • 2+-induced reactive oxygen species production promotes cytochrome c release from rat liver mitochondria via mitochondrial permeability transition (MPT)-dependent and MPT-independent mechanisms: Role of cardiolipin
    • 2+-induced reactive oxygen species production promotes cytochrome c release from rat liver mitochondria via mitochondrial permeability transition (MPT)-dependent and MPT-independent mechanisms: role of cardiolipin. J Biol Chem 2004;279:53103-8.
    • (2004) J Biol Chem , vol.279 , pp. 53103-53108
    • Petrosillo, G.1    Ruggiero, F.M.2    Pistolese, M.3
  • 46
    • 0037022352 scopus 로고    scopus 로고
    • Cytochrome c release from mitochondria proceeds by a two-step process
    • Ott M, Robertson JD, Gogvadze V, et al. Cytochrome c release from mitochondria proceeds by a two-step process. Proc Natl Acad Sci U S A 2002;99:1259-63.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 1259-1263
    • Ott, M.1    Robertson, J.D.2    Gogvadze, V.3
  • 49
    • 0345529917 scopus 로고    scopus 로고
    • Role of reactive oxygen species and cardiolipin in the release of cytochrome c from mitochondria
    • Petrosillo G, Ruggiero FM, Paradies G. Role of reactive oxygen species and cardiolipin in the release of cytochrome c from mitochondria. FASEB J 2003;17:2202-8.
    • (2003) FASEB J , vol.17 , pp. 2202-2208
    • Petrosillo, G.1    Ruggiero, F.M.2    Paradies, G.3
  • 51
    • 0034740585 scopus 로고    scopus 로고
    • DeltaPsi(m)-Dependent and -independent production of reactive oxygen species by rat brain mitochondria
    • Votyakova TV, Reynolds IJ. DeltaPsi(m)-Dependent and -independent production of reactive oxygen species by rat brain mitochondria. J Neurochem 2001;79:266-77.
    • (2001) J Neurochem , vol.79 , pp. 266-277
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 53
    • 0032957613 scopus 로고    scopus 로고
    • Secretagogue-induced digestive enzyme activation and cell injury in rat pancreatic acini
    • Saluja AK, Bhagat L, Lee HS, et al. Secretagogue-induced digestive enzyme activation and cell injury in rat pancreatic acini. Am J Physiol Gastrointest Liver Physiol 1999;276:G835-42.
    • (1999) Am J Physiol Gastrointest Liver Physiol , vol.276
    • Saluja, A.K.1    Bhagat, L.2    Lee, H.S.3
  • 54
    • 1842610571 scopus 로고    scopus 로고
    • Generation of ROS in response to CCK-8 stimulation in mouse pancreatic acinar cells
    • Granados MP, Salido GM, Pariente JA, et al. Generation of ROS in response to CCK-8 stimulation in mouse pancreatic acinar cells. Mitochondrion 2004;3:285-96.
    • (2004) Mitochondrion , vol.3 , pp. 285-296
    • Granados, M.P.1    Salido, G.M.2    Pariente, J.A.3
  • 55
    • 0038389668 scopus 로고    scopus 로고
    • Mitochondrial mechanisms of neural cell death and neuroprotective interventions in Parkinson's disease
    • Fiskum G, Starkov A, Polster BM, et al. Mitochondrial mechanisms of neural cell death and neuroprotective interventions in Parkinson's disease. Ann N Y Acad Sci 2003;991:111-9.
    • (2003) Ann N Y Acad Sci , vol.991 , pp. 111-119
    • Fiskum, G.1    Starkov, A.2    Polster, B.M.3
  • 56
    • 0037424245 scopus 로고    scopus 로고
    • Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production
    • Li N, Ragheb K, Lawler G, et al. Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production. J Biol Chem 2003;278:8516-25.
    • (2003) J Biol Chem , vol.278 , pp. 8516-8525
    • Li, N.1    Ragheb, K.2    Lawler, G.3
  • 57
    • 0036472502 scopus 로고    scopus 로고
    • Menadione-induced apoptosis: Roles of cytosolic Ca(2+) elevations and the mitochondrial permeability transition pore
    • Gerasimenko JV, Gerasimenko OV, Palejwala A, et al. Menadione-induced apoptosis: roles of cytosolic Ca(2+) elevations and the mitochondrial permeability transition pore. J Cell Sci 2002;115:485-97.
    • (2002) J Cell Sci , vol.115 , pp. 485-497
    • Gerasimenko, J.V.1    Gerasimenko, O.V.2    Palejwala, A.3
  • 58
    • 33845992232 scopus 로고    scopus 로고
    • Menadione-induced reactive oxygen species generation via redox cycling promotes apoptosis of murine pancreatic acinar cells
    • Criddle DN, Gillies S, Baumgartner-Wilson HK, et al. Menadione-induced reactive oxygen species generation via redox cycling promotes apoptosis of murine pancreatic acinar cells. J Biol Chem 2006;281:40485-92.
    • (2006) J Biol Chem , vol.281 , pp. 40485-40492
    • Criddle, D.N.1    Gillies, S.2    Baumgartner-Wilson, H.K.3
  • 59
    • 3042637611 scopus 로고    scopus 로고
    • Effects of secretagogues and bile acids on mitochondrial membrane potential of pancreatic acinar cells: Comparison of different modes of evaluating DeltaPsim
    • Voronina SG, Barrow SL, Gerasimenko OV, et al. Effects of secretagogues and bile acids on mitochondrial membrane potential of pancreatic acinar cells: comparison of different modes of evaluating DeltaPsim. J Biol Chem 2004;279:27327-38.
    • (2004) J Biol Chem , vol.279 , pp. 27327-27338
    • Voronina, S.G.1    Barrow, S.L.2    Gerasimenko, O.V.3
  • 60
    • 0034912358 scopus 로고    scopus 로고
    • 1,2-bis(2-Aminophenoxy) ethane-N,N,N′,N′-tetraacetic acid induces caspase-mediated apoptosis and reactive oxygen species-mediated necrosis in cultured cortical neurons
    • Han KS, Kang HJ, Kim EY, et al. 1,2-bis(2-Aminophenoxy) ethane-N,N,N′,N′-tetraacetic acid induces caspase-mediated apoptosis and reactive oxygen species-mediated necrosis in cultured cortical neurons. J Neurochem 2001;78:230-9.
    • (2001) J Neurochem , vol.78 , pp. 230-239
    • Han, K.S.1    Kang, H.J.2    Kim, E.Y.3
  • 61
    • 0034762086 scopus 로고    scopus 로고
    • BAPTA/AM, an intracellular calcium chelator, induces delayed necrosis by lipoxygenase-mediated free radicals in mouse cortical cultures
    • Wie MB, Koh JY, Won MH, et al. BAPTA/AM, an intracellular calcium chelator, induces delayed necrosis by lipoxygenase-mediated free radicals in mouse cortical cultures. Prog Neuropsychopharm Biol Psychiatry 2001;25:1641-59.
    • (2001) Prog Neuropsychopharm Biol Psychiatry , vol.25 , pp. 1641-1659
    • Wie, M.B.1    Koh, J.Y.2    Won, M.H.3
  • 62
    • 0034700135 scopus 로고    scopus 로고
    • Calcium-dependent enzyme activation and vacuole formation in the apical granular region of pancreatic acinar cells
    • Raraty M, Ward J, Erdemli G, et al. Calcium-dependent enzyme activation and vacuole formation in the apical granular region of pancreatic acinar cells. Proc Natl Acad Sci U S A 2000;97:13126- 31.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 13126-13131
    • Raraty, M.1    Ward, J.2    Erdemli, G.3
  • 63
    • 33745265721 scopus 로고    scopus 로고
    • Free radicals and the pancreatic acinar cells: Role in physiology and pathology
    • Chvanov M, Petersen OH, Tepikin A. Free radicals and the pancreatic acinar cells: role in physiology and pathology. Phil Trans R Soc Lond B Biol Sci 2005;360:2273-84.
    • (2005) Phil Trans R Soc Lond B Biol Sci , vol.360 , pp. 2273-2284
    • Chvanov, M.1    Petersen, O.H.2    Tepikin, A.3
  • 64
    • 0036788941 scopus 로고    scopus 로고
    • Regulation of hydrogen peroxide production by brain mitochondria by calcium and Bax
    • Starkov AA, Polster BM, Fiskum G. Regulation of hydrogen peroxide production by brain mitochondria by calcium and Bax. J Neurochem 2002;83:220-8.
    • (2002) J Neurochem , vol.83 , pp. 220-228
    • Starkov, A.A.1    Polster, B.M.2    Fiskum, G.3
  • 65
    • 33744492597 scopus 로고    scopus 로고
    • 2+ transport, permeability transition and oxidative stress in cell death: Implications in cardiotoxicity, neurodegeneration and dyslipidemias
    • 2+ transport, permeability transition and oxidative stress in cell death: implications in cardiotoxicity, neurodegeneration and dyslipidemias. Front Biosci 2006;11:2554-64.
    • (2006) Front Biosci , vol.11 , pp. 2554-2564
    • Vercesi, A.E.1    Kowaltowski, A.J.2    Oliveira, H.C.3
  • 66
    • 33745591102 scopus 로고    scopus 로고
    • Multiple pathways of cytochrome c release from mitochondria in apoptosis
    • Gogvadze V, Orrenius S, Zhivotovsky B. Multiple pathways of cytochrome c release from mitochondria in apoptosis. Biochim Biophys Acta 2006;1757:639-47.
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 639-647
    • Gogvadze, V.1    Orrenius, S.2    Zhivotovsky, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.