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Volumn 8, Issue 3, 2013, Pages

Free Fatty Acid Induces Endoplasmic Reticulum Stress and Apoptosis of β-cells by Ca2+/Calpain-2 Pathways

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 6; CALCIUM ION; CALCIUM RELEASE ACTIVATED CALCIUM CHANNEL 1; CALPAIN 2; CASPASE 12; CASPASE 3; FATTY ACID; GLUCOSE REGULATED PROTEIN 78; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; PROTEIN IRE1; STROMAL INTERACTION MOLECULE 1;

EID: 84875151418     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0059921     Document Type: Article
Times cited : (72)

References (51)
  • 2
    • 78650826465 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperon tauroursodeoxycholic acid alleviates obesity-induced myocardial contractile dysfunction
    • Ceylan-Isik AF, Sreejayan N, Ren J, (2011) Endoplasmic reticulum chaperon tauroursodeoxycholic acid alleviates obesity-induced myocardial contractile dysfunction. J Mol Cell Cardiol 50: 107-116.
    • (2011) J Mol Cell Cardiol , vol.50 , pp. 107-116
    • Ceylan-Isik, A.F.1    Sreejayan, N.2    Ren, J.3
  • 3
    • 41149178575 scopus 로고    scopus 로고
    • Ex vivo transcriptional profiling of human pancreatic islets following chronic exposure to monounsaturated fatty acids
    • Bikopoulos G, da Silva Pimenta A, Lee SC, Lakey JR, Der SD, et al. (2008) Ex vivo transcriptional profiling of human pancreatic islets following chronic exposure to monounsaturated fatty acids. J Endocrinol 196: 455-464.
    • (2008) J Endocrinol , vol.196 , pp. 455-464
    • Bikopoulos, G.1    da Silva Pimenta, A.2    Lee, S.C.3    Lakey, J.R.4    Der, S.D.5
  • 4
    • 77951158889 scopus 로고    scopus 로고
    • Involvement of microRNAs in the cytotoxic effects exerted by proinflammatory cytokines on pancreatic beta-cells
    • Roggli E, Britan A, Gattesco S, Lin-Marq N, Abderrahmani A, et al. (2010) Involvement of microRNAs in the cytotoxic effects exerted by proinflammatory cytokines on pancreatic beta-cells. Diabetes 59: 978-986.
    • (2010) Diabetes , vol.59 , pp. 978-986
    • Roggli, E.1    Britan, A.2    Gattesco, S.3    Lin-Marq, N.4    Abderrahmani, A.5
  • 5
    • 0028268936 scopus 로고
    • Long-term exposure of rat pancreatic islets to fatty acids inhibits glucose-induced insulin secretion and biosynthesis through a glucose fatty acid cycle
    • Zhou YP, Grill VE, (1994) Long-term exposure of rat pancreatic islets to fatty acids inhibits glucose-induced insulin secretion and biosynthesis through a glucose fatty acid cycle. J Clin Invest 93: 870-876.
    • (1994) J Clin Invest , vol.93 , pp. 870-876
    • Zhou, Y.P.1    Grill, V.E.2
  • 6
    • 0029036835 scopus 로고
    • Long term exposure to fatty acids and ketones inhibits B-cell functions in human pancreatic islets of Langerhans
    • Zhou YP, Grill VE, (1995) Long term exposure to fatty acids and ketones inhibits B-cell functions in human pancreatic islets of Langerhans. J Clin Endocrinol Metab 80: 1584-1590.
    • (1995) J Clin Endocrinol Metab , vol.80 , pp. 1584-1590
    • Zhou, Y.P.1    Grill, V.E.2
  • 7
    • 84871009308 scopus 로고    scopus 로고
    • CD147 induces UPR to inhibit apoptosis and chemosensitivity by increasing the transcription of Bip in hepatocellular carcinoma
    • Tang J, Guo YS, Zhang Y, Yu XL, Li L, et al. (2012) CD147 induces UPR to inhibit apoptosis and chemosensitivity by increasing the transcription of Bip in hepatocellular carcinoma. Cell Death Differ 19: 1779-1790.
    • (2012) Cell Death Differ , vol.19 , pp. 1779-1790
    • Tang, J.1    Guo, Y.S.2    Zhang, Y.3    Yu, X.L.4    Li, L.5
  • 8
    • 33646576875 scopus 로고    scopus 로고
    • A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function
    • Feske S, Gwack Y, Prakriya M, Srikanth S, Puppel SH, et al. (2006) A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function. Nature 441: 179-185.
    • (2006) Nature , vol.441 , pp. 179-185
    • Feske, S.1    Gwack, Y.2    Prakriya, M.3    Srikanth, S.4    Puppel, S.H.5
  • 9
    • 61349137530 scopus 로고    scopus 로고
    • STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1
    • Park CY, Hoover PJ, Mullins FM, Bachhawat P, Covington ED, et al. (2009) STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1. Cell 136: 876-890.
    • (2009) Cell , vol.136 , pp. 876-890
    • Park, C.Y.1    Hoover, P.J.2    Mullins, F.M.3    Bachhawat, P.4    Covington, E.D.5
  • 10
    • 66749085475 scopus 로고    scopus 로고
    • A cytosolic homomerization and a modulatory domain within STIM1 C-terminus determine coupling to ORAI1 channels
    • Muik M, Fahrner M, Derler I, Schindl R, Bergsmann J, et al. (2009) A cytosolic homomerization and a modulatory domain within STIM1 C-terminus determine coupling to ORAI1 channels. J Biol Chem 284: 8421-8426.
    • (2009) J Biol Chem , vol.284 , pp. 8421-8426
    • Muik, M.1    Fahrner, M.2    Derler, I.3    Schindl, R.4    Bergsmann, J.5
  • 11
    • 84859735442 scopus 로고    scopus 로고
    • SARAF inactivates the store operated calcium entry machinery to prevent excess calcium refilling
    • Palty R, Raveh A, Kaminsky I, Meller R, Reuveny E, (2012) SARAF inactivates the store operated calcium entry machinery to prevent excess calcium refilling. Cell 149: 425-438.
    • (2012) Cell , vol.149 , pp. 425-438
    • Palty, R.1    Raveh, A.2    Kaminsky, I.3    Meller, R.4    Reuveny, E.5
  • 12
    • 0027474051 scopus 로고
    • Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration
    • Saito K, Elce JS, Hamos JE, Nixon RA, (1993) Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration. Proc Natl Acad Sci U S A 90: 2628-2632.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2628-2632
    • Saito, K.1    Elce, J.S.2    Hamos, J.E.3    Nixon, R.A.4
  • 13
    • 41149174763 scopus 로고    scopus 로고
    • Mechanistic role of calpains in postischemic neurodegeneration
    • Bevers MB, Neumar RW, (2008) Mechanistic role of calpains in postischemic neurodegeneration. J Cereb Blood Flow Metab 28: 655-673.
    • (2008) J Cereb Blood Flow Metab , vol.28 , pp. 655-673
    • Bevers, M.B.1    Neumar, R.W.2
  • 14
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro A, Mina E, Kayed R, Milton SC, Parker I, et al. (2005) Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem 280: 17294-17300.
    • (2005) J Biol Chem , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5
  • 15
    • 0037112117 scopus 로고    scopus 로고
    • Activation of calpain in cultured neurons overexpressing Alzheimer amyloid precursor protein
    • Kuwako K, Nishimura I, Uetsuki T, Saido TC, Yoshikawa K, (2002) Activation of calpain in cultured neurons overexpressing Alzheimer amyloid precursor protein. Brain Res Mol Brain Res 107: 166-175.
    • (2002) Brain Res Mol Brain Res , vol.107 , pp. 166-175
    • Kuwako, K.1    Nishimura, I.2    Uetsuki, T.3    Saido, T.C.4    Yoshikawa, K.5
  • 16
    • 56349169766 scopus 로고    scopus 로고
    • An increase in intracellular Ca2+ is required for the activation of mitochondrial calpain to release AIF during cell death
    • Norberg E, Gogvadze V, Ott M, Horn M, Uhlén P, et al. (2008) An increase in intracellular Ca2+ is required for the activation of mitochondrial calpain to release AIF during cell death. Cell Death Differ 15: 1857-1864.
    • (2008) Cell Death Differ , vol.15 , pp. 1857-1864
    • Norberg, E.1    Gogvadze, V.2    Ott, M.3    Horn, M.4    Uhlén, P.5
  • 17
    • 35748969099 scopus 로고    scopus 로고
    • Common genetic variation in calpain-10 gene (CAPN10) and diabetes risk in a multi-ethnic cohort of American postmenopausal women
    • Song Y, You NC, Hsu YH, Sul J, Wang L, et al. (2007) Common genetic variation in calpain-10 gene (CAPN10) and diabetes risk in a multi-ethnic cohort of American postmenopausal women. Hum Mol Genet 16: 2960-2971.
    • (2007) Hum Mol Genet , vol.16 , pp. 2960-2971
    • Song, Y.1    You, N.C.2    Hsu, Y.H.3    Sul, J.4    Wang, L.5
  • 18
    • 0035957929 scopus 로고    scopus 로고
    • Activation of caspase-12, an endoplasmic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress
    • Yoneda T, Imaizumi K, Oono K, Yui D, Gomi F, et al. (2001) Activation of caspase-12, an endoplasmic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J Biol Chem 276: 13935-13940.
    • (2001) J Biol Chem , vol.276 , pp. 13935-13940
    • Yoneda, T.1    Imaizumi, K.2    Oono, K.3    Yui, D.4    Gomi, F.5
  • 19
    • 77950860036 scopus 로고    scopus 로고
    • Intracellular Ca2+ storage in health and disease: a dynamic equilibrium
    • Sammels E, Parys JB, Missiaen L, De Smedt H, Bultynck G, (2010) Intracellular Ca2+ storage in health and disease: a dynamic equilibrium. Cell Calcium 47: 297-314.
    • (2010) Cell Calcium , vol.47 , pp. 297-314
    • Sammels, E.1    Parys, J.B.2    Missiaen, L.3    De Smedt, H.4    Bultynck, G.5
  • 20
    • 84865125412 scopus 로고    scopus 로고
    • Calpain 2 activated through N-Methyl-D-Aspartic acid receptor signaling cleaves CPEB3 and abrogates CPEB3-repressed translation in neurons
    • Wang CF, Huang YS, (2012) Calpain 2 activated through N-Methyl-D-Aspartic acid receptor signaling cleaves CPEB3 and abrogates CPEB3-repressed translation in neurons. Mol Cell Biol 32: 3321-3332.
    • (2012) Mol Cell Biol , vol.32 , pp. 3321-3332
    • Wang, C.F.1    Huang, Y.S.2
  • 21
    • 43549108142 scopus 로고    scopus 로고
    • Glucolipotoxicity: fuel excess and beta-cell dysfunction
    • Poitout V, Robertson RP, (2008) Glucolipotoxicity: fuel excess and beta-cell dysfunction. Endocr Rev 29: 351-366.
    • (2008) Endocr Rev , vol.29 , pp. 351-366
    • Poitout, V.1    Robertson, R.P.2
  • 22
    • 50549202600 scopus 로고
    • The glucose fatty-acid cycle. Its role in insulin sensitivity and the metabolic disturbances of diabetes mellitus
    • Randle PJ, Garland PB, Hales CN, Newsholme EA, (1963) The glucose fatty-acid cycle. Its role in insulin sensitivity and the metabolic disturbances of diabetes mellitus. Lancet 1: 785-789.
    • (1963) Lancet , vol.1 , pp. 785-789
    • Randle, P.J.1    Garland, P.B.2    Hales, C.N.3    Newsholme, E.A.4
  • 23
    • 0024995157 scopus 로고
    • A 48-hour lipid infusion in the rat time-dependently inhibits glucose-induced insulin secretion and B cell oxidation through a process likely coupled to fatty acid oxidation
    • Sako Y, Grill VE, (1990) A 48-hour lipid infusion in the rat time-dependently inhibits glucose-induced insulin secretion and B cell oxidation through a process likely coupled to fatty acid oxidation. Endocrinology 127: 1580-1589.
    • (1990) Endocrinology , vol.127 , pp. 1580-1589
    • Sako, Y.1    Grill, V.E.2
  • 24
    • 0027303165 scopus 로고
    • Chronic perifusion of rat islets with palmitate suppresses glucose-stimulated insulin release
    • Elks ML, (1993) Chronic perifusion of rat islets with palmitate suppresses glucose-stimulated insulin release. Endocrinology 133: 208-214.
    • (1993) Endocrinology , vol.133 , pp. 208-214
    • Elks, M.L.1
  • 25
    • 0033042342 scopus 로고    scopus 로고
    • Prolonged elevation of plasma free fatty acids desensitizes the insulin secretory response to glucose in vivo in rats
    • Mason TM, Goh T, Tchipashvili V, Sandhu H, Gupta N, et al. (1999) Prolonged elevation of plasma free fatty acids desensitizes the insulin secretory response to glucose in vivo in rats. Diabetes 48: 524-530.
    • (1999) Diabetes , vol.48 , pp. 524-530
    • Mason, T.M.1    Goh, T.2    Tchipashvili, V.3    Sandhu, H.4    Gupta, N.5
  • 26
    • 0028849148 scopus 로고
    • Opposite effects of short- and long-term fatty acid infusion on insulin secretion in healthy subjects
    • Paolisso G, Gambardella A, Amato L, Tortoriello R, D'Amore A, et al. (1995) Opposite effects of short- and long-term fatty acid infusion on insulin secretion in healthy subjects. Diabetologia 38: 1295-1299.
    • (1995) Diabetologia , vol.38 , pp. 1295-1299
    • Paolisso, G.1    Gambardella, A.2    Amato, L.3    Tortoriello, R.4    D'Amore, A.5
  • 27
    • 0030731946 scopus 로고    scopus 로고
    • Fatty acids decrease IDX-1 expression in rat pancreatic islets and reduce GLUT2, glucokinase, insulin, and somatostatin levels
    • Gremlich S, Bonny C, Waeber G, Thorens B, (1997) Fatty acids decrease IDX-1 expression in rat pancreatic islets and reduce GLUT2, glucokinase, insulin, and somatostatin levels. J Biol Chem 272: 30261-30269.
    • (1997) J Biol Chem , vol.272 , pp. 30261-30269
    • Gremlich, S.1    Bonny, C.2    Waeber, G.3    Thorens, B.4
  • 28
    • 0033304970 scopus 로고    scopus 로고
    • Glucose-induced preproinsulin gene expression is inhibited by the free fatty acid palmitate
    • Ritz-Laser B, Meda P, Constant I, Klages N, Charollais A, et al. (1999) Glucose-induced preproinsulin gene expression is inhibited by the free fatty acid palmitate. Endocrinology 140: 4005-4014.
    • (1999) Endocrinology , vol.140 , pp. 4005-4014
    • Ritz-Laser, B.1    Meda, P.2    Constant, I.3    Klages, N.4    Charollais, A.5
  • 29
    • 0034033180 scopus 로고    scopus 로고
    • Inhibition of insulin gene expression by long-term exposure of pancreatic beta cells to palmitate is dependent on the presence of a stimulatory glucose concentration
    • Jacqueminet S, Briaud I, Rouault C, Reach G, Poitout V, (2000) Inhibition of insulin gene expression by long-term exposure of pancreatic beta cells to palmitate is dependent on the presence of a stimulatory glucose concentration. Metabolism 49: 532-536.
    • (2000) Metabolism , vol.49 , pp. 532-536
    • Jacqueminet, S.1    Briaud, I.2    Rouault, C.3    Reach, G.4    Poitout, V.5
  • 30
    • 0035145780 scopus 로고    scopus 로고
    • Lipotoxicity of the pancreatic beta-cell is associated with glucose-dependent esterification of fatty acids into neutral lipids
    • Briaud I, Harmon JS, Kelpe CL, Segu VB, Poitout V, (2001) Lipotoxicity of the pancreatic beta-cell is associated with glucose-dependent esterification of fatty acids into neutral lipids. Diabetes 50: 315-321.
    • (2001) Diabetes , vol.50 , pp. 315-321
    • Briaud, I.1    Harmon, J.S.2    Kelpe, C.L.3    Segu, V.B.4    Poitout, V.5
  • 31
    • 0042531617 scopus 로고    scopus 로고
    • Palmitate inhibition of insulin gene expression is mediated at the transcriptional level via ceramide synthesis
    • Kelpe CL, Moore PC, Parazzoli SD, Wicksteed B, Rhodes CJ, et al. (2003) Palmitate inhibition of insulin gene expression is mediated at the transcriptional level via ceramide synthesis. J Biol Chem 278: 30015-30021.
    • (2003) J Biol Chem , vol.278 , pp. 30015-30021
    • Kelpe, C.L.1    Moore, P.C.2    Parazzoli, S.D.3    Wicksteed, B.4    Rhodes, C.J.5
  • 32
    • 25444480496 scopus 로고    scopus 로고
    • Palmitate inhibits insulin gene expression by altering PDX-1 nuclear localization and reducing MafA expression in isolated rat islets of Langerhans
    • Hagman DK, Hays LB, Parazzoli SD, Poitout V, (2005) Palmitate inhibits insulin gene expression by altering PDX-1 nuclear localization and reducing MafA expression in isolated rat islets of Langerhans. J Biol Chem 280: 32413-32418.
    • (2005) J Biol Chem , vol.280 , pp. 32413-32418
    • Hagman, D.K.1    Hays, L.B.2    Parazzoli, S.D.3    Poitout, V.4
  • 33
    • 0036315888 scopus 로고    scopus 로고
    • Prolonged exposure to free fatty acids has cytostatic and pro-apoptotic effects on human pancreatic islets: evidence that beta-cell death is caspase mediated, partially dependent on ceramide pathway, and Bcl-2 regulated
    • Lupi R, Dotta F, Marselli L, Del Guerra S, Masini M, et al. (2002) Prolonged exposure to free fatty acids has cytostatic and pro-apoptotic effects on human pancreatic islets: evidence that beta-cell death is caspase mediated, partially dependent on ceramide pathway, and Bcl-2 regulated. Diabetes 51: 1437-1442.
    • (2002) Diabetes , vol.51 , pp. 1437-1442
    • Lupi, R.1    Dotta, F.2    Marselli, L.3    Del Guerra, S.4    Masini, M.5
  • 34
    • 0042922453 scopus 로고    scopus 로고
    • Saturated fatty acids synergize with elevated glucose to cause pancreatic beta-cell death
    • El-Assaad W, Buteau J, Peyot ML, Nolan C, Roduit R, et al. (2003) Saturated fatty acids synergize with elevated glucose to cause pancreatic beta-cell death. Endocrinology 144: 4154-4163.
    • (2003) Endocrinology , vol.144 , pp. 4154-4163
    • El-Assaad, W.1    Buteau, J.2    Peyot, M.L.3    Nolan, C.4    Roduit, R.5
  • 35
    • 70449494871 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in beta-cells and development of diabetes
    • Fonseca SG, Burcin M, Gromada J, Urano F, (2009) Endoplasmic reticulum stress in beta-cells and development of diabetes. Curr Opin Pharmacol 9: 763-770.
    • (2009) Curr Opin Pharmacol , vol.9 , pp. 763-770
    • Fonseca, S.G.1    Burcin, M.2    Gromada, J.3    Urano, F.4
  • 36
    • 0035423875 scopus 로고    scopus 로고
    • The glucose-regulated proteins: stress induction and clinical applications
    • Lee AS, (2001) The glucose-regulated proteins: stress induction and clinical applications. Trends Biochem Sci 26: 504-510.
    • (2001) Trends Biochem Sci , vol.26 , pp. 504-510
    • Lee, A.S.1
  • 37
    • 0032054744 scopus 로고    scopus 로고
    • CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum
    • Zinszner H, Kuroda M, Wang X, Batchvarova N, Lightfoot RT, et al. (1998) CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes Dev 12: 982-995.
    • (1998) Genes Dev , vol.12 , pp. 982-995
    • Zinszner, H.1    Kuroda, M.2    Wang, X.3    Batchvarova, N.4    Lightfoot, R.T.5
  • 38
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • Lee AH, Iwakoshi NN, Glimcher LH, (2003) XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol Cell Biol 23: 7448-7459.
    • (2003) Mol Cell Biol , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 39
    • 77956340663 scopus 로고    scopus 로고
    • Arsenic induces apoptosis of human umbilical vein endothelial cells through mitochondrial pathways
    • Shi Y, Wei Y, Qu S, Wang Y, Li Y, et al. (2010) Arsenic induces apoptosis of human umbilical vein endothelial cells through mitochondrial pathways. Cardiovasc Toxicol 10: 153-160.
    • (2010) Cardiovasc Toxicol , vol.10 , pp. 153-160
    • Shi, Y.1    Wei, Y.2    Qu, S.3    Wang, Y.4    Li, Y.5
  • 40
    • 41149174763 scopus 로고    scopus 로고
    • Mechanistic role of calpains in postischemic neurodegeneration
    • Bevers MB, Neumar RW, (2008) Mechanistic role of calpains in postischemic neurodegeneration. J Cereb Blood Flow Metab 28: 655-673.
    • (2008) J Cereb Blood Flow Metab , vol.28 , pp. 655-673
    • Bevers, M.B.1    Neumar, R.W.2
  • 43
    • 0034992155 scopus 로고    scopus 로고
    • The structure of calpain
    • Sorimachi H, Suzuki K, (2001) The structure of calpain. J Biochem 129: 653-664.
    • (2001) J Biochem , vol.129 , pp. 653-664
    • Sorimachi, H.1    Suzuki, K.2
  • 44
    • 84861316167 scopus 로고    scopus 로고
    • Human U87 astrocytoma cell invasion induced by interaction of βig-h3 with integrin α5β1 involves calpain-2
    • Ma J, Cui W, He SM, Duan YH, Heng LJ, et al. (2012) Human U87 astrocytoma cell invasion induced by interaction of βig-h3 with integrin α5β1 involves calpain-2. Plos One 7: e37297.
    • (2012) Plos One , vol.7
    • Ma, J.1    Cui, W.2    He, S.M.3    Duan, Y.H.4    Heng, L.J.5
  • 45
    • 33845947971 scopus 로고    scopus 로고
    • Suppression of cancer cell migration and invasion by protein phosphatase 2A through dephosphorylation of μ- and m-Calpains
    • Xu LJ, Deng XM, (2006) Suppression of cancer cell migration and invasion by protein phosphatase 2A through dephosphorylation of μ- and m-Calpains. J Biol Chem 281: 35567-35575.
    • (2006) J Biol Chem , vol.281 , pp. 35567-35575
    • Xu, L.J.1    Deng, X.M.2
  • 46
    • 1842843854 scopus 로고    scopus 로고
    • Hsp70-DnaJ chaperone pair prevent snitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria
    • Gotoh T, Terada K, Oyadomari S, Mori M, (2004) Hsp70-DnaJ chaperone pair prevent snitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria. Cell Death Differ 11: 390-402.
    • (2004) Cell Death Differ , vol.11 , pp. 390-402
    • Gotoh, T.1    Terada, K.2    Oyadomari, S.3    Mori, M.4
  • 47
    • 0034671837 scopus 로고    scopus 로고
    • CHOP gene expression in response to endoplasmic-reticular stress requires NFY interaction with different domains of a conserved DNA-binding element
    • Ubeda M, Habener JF, (2000) CHOP gene expression in response to endoplasmic-reticular stress requires NFY interaction with different domains of a conserved DNA-binding element. Nucleic Acids Res 28: 4987-4997.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4987-4997
    • Ubeda, M.1    Habener, J.F.2
  • 48
    • 10644260259 scopus 로고    scopus 로고
    • Induction of CCAAT/enhancer-binding protein (C/EBP)-homologous protein/growth arrest and DNA damage-inducible protein 153 expression during inhibition of phosphatidylcholine synthesis is mediated via activation of a C/EBP-activating transcription factor-responsive element
    • Michiel HM, Henriet M, Martin H, Bernd HJ, Arie BV, et al. (2004) Induction of CCAAT/enhancer-binding protein (C/EBP)-homologous protein/growth arrest and DNA damage-inducible protein 153 expression during inhibition of phosphatidylcholine synthesis is mediated via activation of a C/EBP-activating transcription factor-responsive element. J Biol Chem 279: 52007-52015.
    • (2004) J Biol Chem , vol.279 , pp. 52007-52015
    • Michiel, H.M.1    Henriet, M.2    Martin, H.3    Bernd, H.J.4    Arie, B.V.5
  • 49
    • 1842843860 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program
    • Rao RV, Ellerby H, Bredesen DE, (2004) Coupling endoplasmic reticulum stress to the cell death program. Cell Death Differ 11: 372-380.
    • (2004) Cell Death Differ , vol.11 , pp. 372-380
    • Rao, R.V.1    Ellerby, H.2    Bredesen, D.E.3
  • 50
    • 0029114542 scopus 로고
    • Effects of the hypoglycaemic drugs repaglinide and glibenclamide on ATP-sensitive potassium-channels and cytosolic calcium levels in beta TC3 cells and rat pancreatic beta cells
    • Gromada J, Dissing S, Kofod H, Frøkjaer-Jensen J, (1995) Effects of the hypoglycaemic drugs repaglinide and glibenclamide on ATP-sensitive potassium-channels and cytosolic calcium levels in beta TC3 cells and rat pancreatic beta cells. Diabetologia 38: 1025-1032.
    • (1995) Diabetologia , vol.38 , pp. 1025-1032
    • Gromada, J.1    Dissing, S.2    Kofod, H.3    Frøkjaer-Jensen, J.4
  • 51
    • 33749329784 scopus 로고    scopus 로고
    • Free fatty acids inhibit insulin signaling-stimulated endothelial nitric oxide synthase activation through upregulating PTEN or inhibiting Akt kinase
    • Wang XL, Zhang L, Youker K, Zhang MX, Wang J, et al. (2006) Free fatty acids inhibit insulin signaling-stimulated endothelial nitric oxide synthase activation through upregulating PTEN or inhibiting Akt kinase. Diabetes 55: 2301-2310.
    • (2006) Diabetes , vol.55 , pp. 2301-2310
    • Wang, X.L.1    Zhang, L.2    Youker, K.3    Zhang, M.X.4    Wang, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.