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Volumn 46, Issue 35, 2007, Pages 10170-10185

The group VIA calcium-independent phospholipase A2 participates in ER stress-induced INS-1 insulinoma cell apoptosis by promoting ceramide generation via hydrolysis of sphingomyelins by neutral sphingomyelinase

Author keywords

[No Author keywords available]

Indexed keywords

AMIDES; BIOASSAY; CALCIUM; CELL DEATH; CELL GROWTH; HYDROLYSIS; IMMUNOLOGY; RNA;

EID: 34548522699     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700017z     Document Type: Article
Times cited : (73)

References (101)
  • 1
    • 0029954214 scopus 로고    scopus 로고
    • Insulin-dependent diabetes mellitus
    • Tisch, R., and McDevitt, H. (1996) Insulin-dependent diabetes mellitus, Cell 85, 291-297.
    • (1996) Cell , vol.85 , pp. 291-297
    • Tisch, R.1    McDevitt, H.2
  • 2
    • 0035856952 scopus 로고    scopus 로고
    • β-Cell death during progression to diabetes
    • Mathis, D., Vence, L., and Benoist, C. (2001) β-Cell death during progression to diabetes, Nature 414, 792-798.
    • (2001) Nature , vol.414 , pp. 792-798
    • Mathis, D.1    Vence, L.2    Benoist, C.3
  • 3
    • 0024026298 scopus 로고
    • Lilly lecture 1987. The triumvirate: β-cell, muscle, liver. A collusion responsible for NIDDM
    • DeFronzo, R. A. (1988) Lilly lecture 1987. The triumvirate: β-cell, muscle, liver. A collusion responsible for NIDDM, Diabetes 37, 667-687.
    • (1988) Diabetes , vol.37 , pp. 667-687
    • DeFronzo, R.A.1
  • 4
    • 0030938616 scopus 로고    scopus 로고
    • Insulin resistance: A multifaceted syndrome responsible for NIDDM, obesity, hypertension, dyslipidaemia and atherosclerosis
    • DeFronzo, R. A. (1997) Insulin resistance: A multifaceted syndrome responsible for NIDDM, obesity, hypertension, dyslipidaemia and atherosclerosis, Neth. J. Med. 50, 191-197.
    • (1997) Neth. J. Med , vol.50 , pp. 191-197
    • DeFronzo, R.A.1
  • 5
    • 0028872358 scopus 로고
    • Diabetes. Causes of insulin resistance
    • Kahn, C. R. (1995) Diabetes. Causes of insulin resistance, Nature 373, 384-385.
    • (1995) Nature , vol.373 , pp. 384-385
    • Kahn, C.R.1
  • 6
    • 0009781763 scopus 로고    scopus 로고
    • Insulin secretion in type 2 diabetes mellitus
    • Draznin, B, and Rizza, R, Eds, pp, Humana Press, Totowa, NJ
    • Kudva, Y. C., and Butler, P. C. (1997) Insulin secretion in type 2 diabetes mellitus, in Clinicl Research in Diabetes and Obesity (Draznin, B., and Rizza, R., Eds.) pp 119-136, Humana Press, Totowa, NJ.
    • (1997) Clinicl Research in Diabetes and Obesity , pp. 119-136
    • Kudva, Y.C.1    Butler, P.C.2
  • 8
    • 0021777067 scopus 로고
    • Islet pathology and the pathogenesis of type 1 and type 2 diabetes mellitus revisited
    • Kloppel, G., Lohr, M., Habich, K., Oberholzer, M., and Heitz, P. U. (1985) Islet pathology and the pathogenesis of type 1 and type 2 diabetes mellitus revisited, Surv. Synth. Pathol. Res. 4, 110-125.
    • (1985) Surv. Synth. Pathol. Res , vol.4 , pp. 110-125
    • Kloppel, G.1    Lohr, M.2    Habich, K.3    Oberholzer, M.4    Heitz, P.U.5
  • 9
    • 0019996086 scopus 로고
    • Quantitation of endocrine cell content in the pancreas of nondiabetic and diabetic humans
    • Stefan, Y., Orci, L., Malaisse-Lagae, F., Perrelet, A., Patel, Y., and Unger, R. H. (1982) Quantitation of endocrine cell content in the pancreas of nondiabetic and diabetic humans, Diabetes 31, 694-700.
    • (1982) Diabetes , vol.31 , pp. 694-700
    • Stefan, Y.1    Orci, L.2    Malaisse-Lagae, F.3    Perrelet, A.4    Patel, Y.5    Unger, R.H.6
  • 10
    • 0037219411 scopus 로고    scopus 로고
    • β-Cell deficit and increased β-cell apoptosis in humans with type 2 diabetes
    • Butler, A. E., Janson, J., Bonner-Weir, S., Ritzel, R., Rizza, R. A., and Butler, P. C. (2003) β-Cell deficit and increased β-cell apoptosis in humans with type 2 diabetes, Diabetes 52, 102-110.
    • (2003) Diabetes , vol.52 , pp. 102-110
    • Butler, A.E.1    Janson, J.2    Bonner-Weir, S.3    Ritzel, R.4    Rizza, R.A.5    Butler, P.C.6
  • 12
    • 0032999544 scopus 로고    scopus 로고
    • Neogenesis vs. apoptosis as main components of pancreatic β-cell mass changes in glucose-infused normal and mildly diabetic adult rats
    • Bernard, C., Berthault, M.-F., Saulnier, C., and Ktorza, A. (1999) Neogenesis vs. apoptosis as main components of pancreatic β-cell mass changes in glucose-infused normal and mildly diabetic adult rats, FASEB J. 13, 1195-1205.
    • (1999) FASEB J , vol.13 , pp. 1195-1205
    • Bernard, C.1    Berthault, M.-F.2    Saulnier, C.3    Ktorza, A.4
  • 14
    • 0042822112 scopus 로고    scopus 로고
    • Increased β-cell apoptosis prevents adaptive increase in β-cell mass in mouse model of type 2 diabetes: Evidence for role of islet amyloid formation rather than direct action of am
    • Butler, A. E., Janson, J., Soeller, W. C., and Butler, P. C. (2003) Increased β-cell apoptosis prevents adaptive increase in β-cell mass in mouse model of type 2 diabetes: Evidence for role of islet amyloid formation rather than direct action of am, Diabetes 52, 2304-2314.
    • (2003) Diabetes , vol.52 , pp. 2304-2314
    • Butler, A.E.1    Janson, J.2    Soeller, W.C.3    Butler, P.C.4
  • 15
    • 0036175128 scopus 로고    scopus 로고
    • Targeted disruption of the CHOP gene delays endoplasmic reticulum stress-mediated diabetes
    • Oyadomari, S., Koizumi, A., Takeda, K., Gotoh, T., Akira, S., Araki, E., and Mori, M. (2002) Targeted disruption of the CHOP gene delays endoplasmic reticulum stress-mediated diabetes, J. Clin. Invest. 109, 525-532.
    • (2002) J. Clin. Invest , vol.109 , pp. 525-532
    • Oyadomari, S.1    Koizumi, A.2    Takeda, K.3    Gotoh, T.4    Akira, S.5    Araki, E.6    Mori, M.7
  • 16
    • 0031913829 scopus 로고    scopus 로고
    • Role of apoptosis in failure of β-cell mass compensation for insulin resistance and β-cell defects in the male Zucker diabetic fatty rat
    • Pick, A., Clark, J., Kubstrup, C., Levisetti, M., Pugh, W., Bonner-Weir, S., and Polonsky, K. S. (1998) Role of apoptosis in failure of β-cell mass compensation for insulin resistance and β-cell defects in the male Zucker diabetic fatty rat, Diabetes 47, 358-364.
    • (1998) Diabetes , vol.47 , pp. 358-364
    • Pick, A.1    Clark, J.2    Kubstrup, C.3    Levisetti, M.4    Pugh, W.5    Bonner-Weir, S.6    Polonsky, K.S.7
  • 17
    • 0034203929 scopus 로고    scopus 로고
    • Type 2 diabetes and β cell apoptosis
    • Cerasi, E., Kaiser, N., and Leibowitz, G. (2000) Type 2 diabetes and β cell apoptosis, Diabetes Metab. 26, 13-16.
    • (2000) Diabetes Metab , vol.26 , pp. 13-16
    • Cerasi, E.1    Kaiser, N.2    Leibowitz, G.3
  • 19
    • 0035128723 scopus 로고    scopus 로고
    • β-Cell apoptosis: Stimuli and signaling
    • Mandrup-Poulsen, T. (2001) β-Cell apoptosis: Stimuli and signaling, Diabetes 50, S58-S63.
    • (2001) Diabetes , vol.50
    • Mandrup-Poulsen, T.1
  • 20
    • 0036910731 scopus 로고    scopus 로고
    • Apoptosis in the β cells: Cause or consequence of insulin secretion defect in diabetes?
    • Sesti, G. (2002) Apoptosis in the β cells: Cause or consequence of insulin secretion defect in diabetes? Ann. Med. 34, 444-450.
    • (2002) Ann. Med , vol.34 , pp. 444-450
    • Sesti, G.1
  • 21
    • 0036022403 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-mediated apoptosis in pancreatic β-cells
    • Oyadomari, S., Araki, E., and Mori, M. (2002) Endoplasmic reticulum stress-mediated apoptosis in pancreatic β-cells, Apoptosis 7, 335-345.
    • (2002) Apoptosis , vol.7 , pp. 335-345
    • Oyadomari, S.1    Araki, E.2    Mori, M.3
  • 22
    • 0036260052 scopus 로고    scopus 로고
    • Na/Ca exchanger overexpression induces endoplasmic reticulum-related apoptosis and caspase-12 activation in insulin-releasing BRIN-BD11 cells
    • Diaz-Horta, O., Kamagate, A., Herchuelz, A., and Van Eylen, F. (2002) Na/Ca exchanger overexpression induces endoplasmic reticulum-related apoptosis and caspase-12 activation in insulin-releasing BRIN-BD11 cells, Diabetes 51, 1815-1824.
    • (2002) Diabetes , vol.51 , pp. 1815-1824
    • Diaz-Horta, O.1    Kamagate, A.2    Herchuelz, A.3    Van Eylen, F.4
  • 23
    • 0034610792 scopus 로고    scopus 로고
    • Caspases find a new place to hide
    • Mehmet, H. (2000) Caspases find a new place to hide, Nature 403, 29-30.
    • (2000) Nature , vol.403 , pp. 29-30
    • Mehmet, H.1
  • 24
    • 0034476896 scopus 로고    scopus 로고
    • An endoplasmic reticulum-specific stress-activated caspase (caspase-12) is implicated in the apoptosis of A549 epithelial cells by respiratory syncytial virus
    • Bitko, V., and Barik, S. (2001) An endoplasmic reticulum-specific stress-activated caspase (caspase-12) is implicated in the apoptosis of A549 epithelial cells by respiratory syncytial virus, J. Cell Biochem. 80, 441-454.
    • (2001) J. Cell Biochem , vol.80 , pp. 441-454
    • Bitko, V.1    Barik, S.2
  • 25
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
    • Nakagawa, T., Zhu, H., Morishima, N., Li, E., Xu, J., Yankner, B., and Yuan, J. (2000) Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β, Nature 403, 98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.6    Yuan, J.7
  • 27
    • 0345465663 scopus 로고    scopus 로고
    • Integration of endoplasmic reticulum signaling in health and disease
    • Aridor, M., and Balch, W. E. (1999) Integration of endoplasmic reticulum signaling in health and disease, Nat. Med. 5, 745-751.
    • (1999) Nat. Med , vol.5 , pp. 745-751
    • Aridor, M.1    Balch, W.E.2
  • 28
    • 0036856008 scopus 로고    scopus 로고
    • Translational control in the endoplasmic reticulum stress response
    • Ron, D. (2002) Translational control in the endoplasmic reticulum stress response, J. Clin. Invest. 110, 1383-1388.
    • (2002) J. Clin. Invest , vol.110 , pp. 1383-1388
    • Ron, D.1
  • 29
    • 0036895383 scopus 로고    scopus 로고
    • Endoplasmic Reticulum Stress and the Development of Diabetes: A Review
    • Harding, H. P., and Ron, D. (2002) Endoplasmic Reticulum Stress and the Development of Diabetes: A Review, Diabetes 51, S455-S461.
    • (2002) Diabetes , vol.51
    • Harding, H.P.1    Ron, D.2
  • 30
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen, G. M. (1997) Caspases: The executioners of apoptosis, Biochem. J. 326, 1-16.
    • (1997) Biochem. J , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 31
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • Kaufman, R. J. (1999) Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls, Genes Dev. 13, 1211-1233.
    • (1999) Genes Dev , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 33
    • 0034425698 scopus 로고    scopus 로고
    • EIF2AK3, encoding translation initiation factor 2-α kinase 3, is mutated in patients with Wolcott-Rallison syndrome
    • Delepine, M., Nicolino, M., Barrett, T., Golamaully, M., Lathrop, G. M., and Julier, C. (2000) EIF2AK3, encoding translation initiation factor 2-α kinase 3, is mutated in patients with Wolcott-Rallison syndrome, Nat. Genet. 25, 406.
    • (2000) Nat. Genet , vol.25 , pp. 406
    • Delepine, M.1    Nicolino, M.2    Barrett, T.3    Golamaully, M.4    Lathrop, G.M.5    Julier, C.6
  • 34
    • 0035283066 scopus 로고    scopus 로고
    • WFS1 (Wolfram syndrome 1) gene product: Predominant subcellular localization to endoplasmic reticulum in cultured cells and neuronal expression in rat brain
    • Takeda, K., Inoue, H., Tanizawa, Y., Matsuzaki, Y., Oba, J., Watanabe, Y., Shinoda, K., and Oka, Y. (2001) WFS1 (Wolfram syndrome 1) gene product: Predominant subcellular localization to endoplasmic reticulum in cultured cells and neuronal expression in rat brain, Hum. Mol. Genet. 10, 477-484.
    • (2001) Hum. Mol. Genet , vol.10 , pp. 477-484
    • Takeda, K.1    Inoue, H.2    Tanizawa, Y.3    Matsuzaki, Y.4    Oba, J.5    Watanabe, Y.6    Shinoda, K.7    Oka, Y.8
  • 35
    • 0242609973 scopus 로고    scopus 로고
    • Impact of endoplasmic reticulum stress pathway on pancreatic β-cells and diabetes mellitus
    • Araki, E., Oyadomari, S., and Mori, M. (2003) Impact of endoplasmic reticulum stress pathway on pancreatic β-cells and diabetes mellitus, Exp. Biol. Med. 228, 1213-1217.
    • (2003) Exp. Biol. Med , vol.228 , pp. 1213-1217
    • Araki, E.1    Oyadomari, S.2    Mori, M.3
  • 36
    • 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, R. T., Remotti, H., Stevens, J. L., and Ron, D. (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    Remotti, H.6    Stevens, J.L.7    Ron, D.8
  • 37
    • 0037288692 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and diabetes mellitus
    • Araki, E., Oyadomari, S., and Mori, M. (2003) Endoplasmic reticulum stress and diabetes mellitus, Intern. Med. 42, 7-14.
    • (2003) Intern. Med , vol.42 , pp. 7-14
    • Araki, E.1    Oyadomari, S.2    Mori, M.3
  • 46
    • 0030999048 scopus 로고    scopus 로고
    • 2 enzyme that contains a repeated structural motif homologous to the integral membrane protein binding domain of ankyrin
    • 2 enzyme that contains a repeated structural motif homologous to the integral membrane protein binding domain of ankyrin, J. Biol. Chem. 272, 11118-11127.
    • (1997) J. Biol. Chem , vol.272 , pp. 11118-11127
    • Ma, Z.1    Ramanadham, S.2    Kempe, K.3    Chi, X.S.4    Ladenson, J.5    Turk, J.6
  • 48
    • 0035907356 scopus 로고    scopus 로고
    • 2 in remodeling and increased susceptibility of proliferating T cells to CoA-independent transacylase inhibitor-induced apoptosis
    • 2 in remodeling and increased susceptibility of proliferating T cells to CoA-independent transacylase inhibitor-induced apoptosis, J. Biol. Chem. 276, 17568-17575.
    • (2001) J. Biol. Chem , vol.276 , pp. 17568-17575
    • Boilard, E.1    Surette, M.E.2
  • 49
    • 0033957940 scopus 로고    scopus 로고
    • 2 in the Regulation of Inducible Nitric Oxide Synthase in Cardiac Myocytes
    • 2 in the Regulation of Inducible Nitric Oxide Synthase in Cardiac Myocytes, Hypertension 35, 249-254.
    • (2000) Hypertension , vol.35 , pp. 249-254
    • Isenovic, E.1    LaPointe, M.C.2
  • 52
    • 0034814686 scopus 로고    scopus 로고
    • 2 mediates CREB phosphorylation and c-fos expression during ischemia
    • 2 mediates CREB phosphorylation and c-fos expression during ischemia, Am. J. Physiol. 281, H168-H176.
    • (2001) Am. J. Physiol , vol.281
    • Williams, S.D.1    Ford, D.A.2
  • 54
    • 0033553432 scopus 로고    scopus 로고
    • 2 in fatty acid incorporation, phospholipid remodeling, lysophosphatidylcholine generation, and secretagogue-induced arachidonic acid release in pancreatic islets and insulinoma cells
    • 2 in fatty acid incorporation, phospholipid remodeling, lysophosphatidylcholine generation, and secretagogue-induced arachidonic acid release in pancreatic islets and insulinoma cells, J. Biol. Chem. 274, 13915-13927.
    • (1999) J. Biol. Chem , vol.274 , pp. 13915-13927
    • Ramanadham, S.1    Hsu, F.-F.2    Bohrer, A.3    Ma, Z.4    Turk, J.5
  • 61
    • 0027510919 scopus 로고
    • 2 activity selective for hydrolysis of arachidonate which is stimulated by adenosine triphosphate and is specifically localized to islet β-cells
    • 2 activity selective for hydrolysis of arachidonate which is stimulated by adenosine triphosphate and is specifically localized to islet β-cells, Biochemistry 32, 327-336.
    • (1993) Biochemistry , vol.32 , pp. 327-336
    • Gross, R.W.1    Ramanadham, S.2    Kruszka, K.K.3    Han, X.4    Turk, J.5
  • 62
    • 0027505285 scopus 로고
    • Inhibition of arachidonate release by secretagogue-stimulated pancreatic islets suppresses both insulin secretion and the rise in β-cell cytosolic calcium ion concentration
    • Ramanadham, S., Gross, R. W., Han, X., and Turk, J. (1993) Inhibition of arachidonate release by secretagogue-stimulated pancreatic islets suppresses both insulin secretion and the rise in β-cell cytosolic calcium ion concentration, Biochemistry 32, 337-346.
    • (1993) Biochemistry , vol.32 , pp. 337-346
    • Ramanadham, S.1    Gross, R.W.2    Han, X.3    Turk, J.4
  • 65
    • 0029055676 scopus 로고
    • Ceramide: A stress signal and mediator of growth suppression and apoptosis
    • Obeid, L. M., and Hannun, Y. A. (1995) Ceramide: A stress signal and mediator of growth suppression and apoptosis, J. Cell. Biochem. 58, 191-198.
    • (1995) J. Cell. Biochem , vol.58 , pp. 191-198
    • Obeid, L.M.1    Hannun, Y.A.2
  • 67
    • 0004131383 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, Plainview, NY
    • Coffin, J. M., and Hart, G. W. (1996) Retrovirus, Cold Spring Harbor Laboratory Press, Plainview, NY.
    • (1996) Retrovirus
    • Coffin, J.M.1    Hart, G.W.2
  • 69
    • 0016377705 scopus 로고
    • Isolation of rough and smooth microsomes: General
    • Dallner, G. (1974) Isolation of rough and smooth microsomes: General, Methods Enzymol. 31 (Part A), 191-201.
    • (1974) Methods Enzymol , vol.31 , Issue.PART A , pp. 191-201
    • Dallner, G.1
  • 72
    • 0036585050 scopus 로고    scopus 로고
    • Characterization of ceramides by low energy collisional-activated dissociation tandem mass spectrometry with negative-ion electrospray ionization
    • Hsu, F. F., and Turk, J. (2002) Characterization of ceramides by low energy collisional-activated dissociation tandem mass spectrometry with negative-ion electrospray ionization, J. Am. Soc. Mass Spectrom. 13, 558-570.
    • (2002) J. Am. Soc. Mass Spectrom , vol.13 , pp. 558-570
    • Hsu, F.F.1    Turk, J.2
  • 73
    • 0036615735 scopus 로고    scopus 로고
    • Structural studies on ceramides as lithiated adducts by low energy collisional-activated dissociation tandem mass spectrometry with electrospray ionization
    • Hsu, F. F., Turk, J., Stewart, M. E., and Downing, D. T. (2002) Structural studies on ceramides as lithiated adducts by low energy collisional-activated dissociation tandem mass spectrometry with electrospray ionization, J. Am. Soc. Mass Spectrom. 13, 680-695.
    • (2002) J. Am. Soc. Mass Spectrom , vol.13 , pp. 680-695
    • Hsu, F.F.1    Turk, J.2    Stewart, M.E.3    Downing, D.T.4
  • 74
    • 0034478707 scopus 로고    scopus 로고
    • Structural determination of sphingomyelin by tandem mass spectrometry with electrospray ionization
    • Hsu, F. F., and Turk, J. (2000) Structural determination of sphingomyelin by tandem mass spectrometry with electrospray ionization, J. Am. Soc. Mass Spectrom. 11, 437-449.
    • (2000) J. Am. Soc. Mass Spectrom , vol.11 , pp. 437-449
    • Hsu, F.F.1    Turk, J.2
  • 77
    • 0032509239 scopus 로고    scopus 로고
    • Importance of poly(ADP-ribose) polymerase and its cleavage in apoptosis. Lesson from an uncleavable mutant
    • Oliver, F. J., de la Rubia, G., Rolli, V., Ruiz-Ruiz, M. C., de Murcia, G., and Murcia, J. M.-d. (1998) Importance of poly(ADP-ribose) polymerase and its cleavage in apoptosis. Lesson from an uncleavable mutant, J. Biol. Chem. 273, 33533-33539.
    • (1998) J. Biol. Chem , vol.273 , pp. 33533-33539
    • Oliver, F.J.1    de la Rubia, G.2    Rolli, V.3    Ruiz-Ruiz, M.C.4    de Murcia, G.5    Murcia, J.M.-D.6
  • 78
    • 0038529730 scopus 로고    scopus 로고
    • Biochemical properties of mammalian neutral sphingomyelinase2 and its role in sphingolipid metabolism
    • Marchesini, N., Luberto, C., and Hannun, Y. A. (2003) Biochemical properties of mammalian neutral sphingomyelinase2 and its role in sphingolipid metabolism, J. Biol. Chem. 278, 13775-13783.
    • (2003) J. Biol. Chem , vol.278 , pp. 13775-13783
    • Marchesini, N.1    Luberto, C.2    Hannun, Y.A.3
  • 79
    • 0032484132 scopus 로고    scopus 로고
    • Lipoapoptosis in β-cells of obese prediabetic fa/fa rats. Role of serine palmitoyltransferase overexpression
    • Shimabukuro, M., Higa, M., Zhou, Y.-T., Wang, M.-Y., Newgard, C. B., and Unger, R. H. (1998) Lipoapoptosis in β-cells of obese prediabetic fa/fa rats. Role of serine palmitoyltransferase overexpression, J. Biol. Chem. 273, 32487-32490.
    • (1998) J. Biol. Chem , vol.273 , pp. 32487-32490
    • Shimabukuro, M.1    Higa, M.2    Zhou, Y.-T.3    Wang, M.-Y.4    Newgard, C.B.5    Unger, R.H.6
  • 80
    • 28244435870 scopus 로고    scopus 로고
    • WFS1 is a novel component of the unfolded protein response and maintains homeostasis of the endoplasmic reticulum in pancreatic β-cells
    • Fonseca, S. G., Fukuma, M., Lipson, K. L., Nguyen, L. X., Allen, J. R., Oka, Y., and Urano, F. (2005) WFS1 is a novel component of the unfolded protein response and maintains homeostasis of the endoplasmic reticulum in pancreatic β-cells, J. Biol. Chem. 280, 39609-39615.
    • (2005) J. Biol. Chem , vol.280 , pp. 39609-39615
    • Fonseca, S.G.1    Fukuma, M.2    Lipson, K.L.3    Nguyen, L.X.4    Allen, J.R.5    Oka, Y.6    Urano, F.7
  • 83
    • 1942475176 scopus 로고    scopus 로고
    • The role of endoplasmic reticulum stress in nonimmune diabetes: NOD.k iHEL, a novel model of β-cell death
    • Socha, L., Silva, D., Lesage, S., Goodnow, C., and Petrovsky, N. (2003) The role of endoplasmic reticulum stress in nonimmune diabetes: NOD.k iHEL, a novel model of β-cell death, Ann. N.Y. Acad. Sci. 1005, 178-183.
    • (2003) Ann. N.Y. Acad. Sci , vol.1005 , pp. 178-183
    • Socha, L.1    Silva, D.2    Lesage, S.3    Goodnow, C.4    Petrovsky, N.5
  • 84
    • 0027994349 scopus 로고
    • The sphingomyelin cycle and the second messenger function of ceramide
    • Hannun, Y. A. (1994) The sphingomyelin cycle and the second messenger function of ceramide, J. Biol. Chem. 269, 3125-3128.
    • (1994) J. Biol. Chem , vol.269 , pp. 3125-3128
    • Hannun, Y.A.1
  • 85
    • 2242423614 scopus 로고    scopus 로고
    • Nitric oxide induces degradation of the neutral ceramidase in rat renal mesangial cells and is counterregulated by protein kinase
    • Franzen, R., Fabbro, D., Aschrafi, A., Pfeilschifter, J., and Huwiler, A. (2002) Nitric oxide induces degradation of the neutral ceramidase in rat renal mesangial cells and is counterregulated by protein kinase, J. Biol. Chem. 277, 46184-46190.
    • (2002) J. Biol. Chem , vol.277 , pp. 46184-46190
    • Franzen, R.1    Fabbro, D.2    Aschrafi, A.3    Pfeilschifter, J.4    Huwiler, A.5
  • 86
    • 0042531617 scopus 로고    scopus 로고
    • Palmitate inhibition of insulin gene expression is mediated at the transcriptional level via ceramide synthesis
    • Kelpe, C. L., Moore, P. C., Parazzoli, S. D., Wicksteed, B., Rhodes, C. J., and Poitout, V. (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    Poitout, V.6
  • 87
    • 0036315888 scopus 로고    scopus 로고
    • Lupi, R., Dotta, F., Marselli, L., Del, Guerra, S., Masini, M., Santangelo, C., Patane, G., Boggi, U., Piro, S., Anello, M., Bergamini, E., Mosca, F., Di Mario, U., Del Prato, S., and Marchetti, P. (2002) Prolonged exposure to free fatty acids has cytostatic and pro-apoptotic effects on human pancreatic islets: Evidence that β-cell death is caspase mediated, partially dependent on ceramide pathway, and Bcl-2 regulated, Diabetes 51, 1437-1442.
    • Lupi, R., Dotta, F., Marselli, L., Del, Guerra, S., Masini, M., Santangelo, C., Patane, G., Boggi, U., Piro, S., Anello, M., Bergamini, E., Mosca, F., Di Mario, U., Del Prato, S., and Marchetti, P. (2002) Prolonged exposure to free fatty acids has cytostatic and pro-apoptotic effects on human pancreatic islets: Evidence that β-cell death is caspase mediated, partially dependent on ceramide pathway, and Bcl-2 regulated, Diabetes 51, 1437-1442.
  • 88
    • 13244259440 scopus 로고    scopus 로고
    • Selective inhibition of juxtanuclear translocation of protein kinase c βII by a negative feedback mechanism involving ceramide formed from the salvage pathway
    • Becker, K. P., Kitatani, K., Idkowiak-Baldys, J., Bielawski, J., and Hannun, Y. A. (2005) Selective inhibition of juxtanuclear translocation of protein kinase c βII by a negative feedback mechanism involving ceramide formed from the salvage pathway, J. Biol. Chem. 280, 2606-2612.
    • (2005) J. Biol. Chem , vol.280 , pp. 2606-2612
    • Becker, K.P.1    Kitatani, K.2    Idkowiak-Baldys, J.3    Bielawski, J.4    Hannun, Y.A.5
  • 91
    • 0027752299 scopus 로고
    • Mass spectrometric characterization of arachidonate-containing plasmalogens in human pancreatic islets and in rat islet β-cells and subcellular membranes
    • Ramanadham, S., Bohrer, A., Gross, R. W., and Turk, J. (1993) Mass spectrometric characterization of arachidonate-containing plasmalogens in human pancreatic islets and in rat islet β-cells and subcellular membranes, Biochemistry 32, 13499-13509.
    • (1993) Biochemistry , vol.32 , pp. 13499-13509
    • Ramanadham, S.1    Bohrer, A.2    Gross, R.W.3    Turk, J.4
  • 93
    • 0030903804 scopus 로고    scopus 로고
    • Activation of neutral sphingomyelinase in human neutrophils by polyunsaturated fatty acids
    • Robinson, B. S., Hii, C. S., Poulos, A., and Ferrante, A. (1997) Activation of neutral sphingomyelinase in human neutrophils by polyunsaturated fatty acids, Immunology 91, 274-280.
    • (1997) Immunology , vol.91 , pp. 274-280
    • Robinson, B.S.1    Hii, C.S.2    Poulos, A.3    Ferrante, A.4
  • 95
    • 0031781921 scopus 로고    scopus 로고
    • Ceramide accumulation during oxidant renal tubular injury: Mechanisms and potential consequences
    • Zager, R. A., Conrad, D. S., and Burkhart, K. (1998) Ceramide accumulation during oxidant renal tubular injury: Mechanisms and potential consequences, J. Am. Soc. Nephrol. 9, 1670-1680.
    • (1998) J. Am. Soc. Nephrol , vol.9 , pp. 1670-1680
    • Zager, R.A.1    Conrad, D.S.2    Burkhart, K.3
  • 96
    • 2342570273 scopus 로고    scopus 로고
    • Acid and neutral sphingomyelinases: Roles and mechanisms of regulation
    • Marchesini, N., and Hannun, Y. A. (2004) Acid and neutral sphingomyelinases: Roles and mechanisms of regulation, Biochem. Cell Biol. 82, 27-44.
    • (2004) Biochem. Cell Biol , vol.82 , pp. 27-44
    • Marchesini, N.1    Hannun, Y.A.2
  • 97
    • 0036645698 scopus 로고    scopus 로고
    • Biochemical identification of a neutral sphingomyelinase 1 (NSM1)-like enzyme as the major NSM activity in the DT40 B-cell line: Absence of a role in the apoptotic response to endoplasmic reticulum stress
    • Fensome, A. C., Josephs, M., Katan, M., and Rodrigues-Lima, F. (2002) Biochemical identification of a neutral sphingomyelinase 1 (NSM1)-like enzyme as the major NSM activity in the DT40 B-cell line: Absence of a role in the apoptotic response to endoplasmic reticulum stress, Biochem. J. 365, 69-77.
    • (2002) Biochem. J , vol.365 , pp. 69-77
    • Fensome, A.C.1    Josephs, M.2    Katan, M.3    Rodrigues-Lima, F.4
  • 100
    • 0028361236 scopus 로고
    • 2 from clonal insulin-secreting HIT cells and rat pancreatic islets: A possible molecular component of the β-cell fuel sensor
    • 2 from clonal insulin-secreting HIT cells and rat pancreatic islets: A possible molecular component of the β-cell fuel sensor, Biochemistry 33, 7442-7452.
    • (1994) Biochemistry , vol.33 , pp. 7442-7452
    • Ramanadham, S.1    Wolf, M.J.2    Jett, P.A.3    Gross, R.W.4    Turk, J.5
  • 101
    • 0034631827 scopus 로고    scopus 로고
    • Sphingomyelin hydrolysis to ceramide during the execution phase of apoptosis results from phospholipid scrambling and alters cell-surface morphology
    • Tepper, A. D., Ruurs, P., Wiedmer, T., Sims, P. J., Borst, J., and van Blitterswijk, W. J. (2000) Sphingomyelin hydrolysis to ceramide during the execution phase of apoptosis results from phospholipid scrambling and alters cell-surface morphology, J. Cell Biol. 150, 155-164.
    • (2000) J. Cell Biol , vol.150 , pp. 155-164
    • Tepper, A.D.1    Ruurs, P.2    Wiedmer, T.3    Sims, P.J.4    Borst, J.5    van Blitterswijk, W.J.6


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