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Volumn 12, Issue 1, 2013, Pages

Role of ceramide in diabetes mellitus: Evidence and mechanisms

Author keywords

Ceramide; Diabetes; Insulin resistance; Pancreatic apoptosis; Sphingolipid

Indexed keywords

APOPTOTIC PROTEASE ACTIVATING FACTOR 1; CERAMIDE; CYTOCHROME C; FREE RADICAL; FUMONISIN B1; GLUCOSE TRANSPORTER 4; GLYCOGEN SYNTHASE KINASE 3; INSULIN; INSULIN RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1; PROTEIN KINASE B; PROTEIN KINASE C ZETA; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; TUMOR NECROSIS FACTOR RECEPTOR;

EID: 84879821802     PISSN: None     EISSN: 1476511X     Source Type: Journal    
DOI: 10.1186/1476-511X-12-98     Document Type: Article
Times cited : (158)

References (185)
  • 1
    • 0031851293 scopus 로고    scopus 로고
    • Definition, diagnosis and classification of diabetes mellitus and its complications. Part 1: Diagnosis and classification of diabetes mellitus provisional report of a WHO consultation
    • 10.1002/(SICI)1096-9136(199807)15:7<539: AID-DIA668>3.0.CO;2-S 9686693
    • Definition, diagnosis and classification of diabetes mellitus and its complications. Part 1: diagnosis and classification of diabetes mellitus provisional report of a WHO consultation. Alberti KG, Zimmet PZ, Diabet Med 1998 15 539 553 10.1002/(SICI)1096-9136(199807)15:7<539::AID-DIA668>3.0.CO;2-S 9686693
    • (1998) Diabet Med , vol.15 , pp. 539-553
    • Alberti, K.G.1    Zimmet, P.Z.2
  • 3
    • 4444309565 scopus 로고    scopus 로고
    • The complex life of simple sphingolipids
    • 10.1038/sj.embor.7400208 15289826
    • The complex life of simple sphingolipids. Futerman AH, Hannun YA, EMBO Rep 2004 5 777 782 10.1038/sj.embor.7400208 15289826
    • (2004) EMBO Rep , vol.5 , pp. 777-782
    • Futerman, A.H.1    Hannun, Y.A.2
  • 4
    • 66349086742 scopus 로고    scopus 로고
    • Bioactive sphingolipids: Metabolism and function
    • 19017611
    • Bioactive sphingolipids: metabolism and function. Bartke N, Hannun YA, J Lipid Res 2009 50 91 S96 19017611
    • (2009) J Lipid Res , vol.50
    • Bartke, N.1    Hannun, Y.A.2
  • 5
    • 0035660246 scopus 로고    scopus 로고
    • Sphingolipids in mammalian cell signaling
    • 10.1007/PL00000836 11814056
    • Sphingolipids in mammalian cell signaling. Ohanian J, Ohanian V, Cell Mol Life Sci 2001 58 2053 2068 10.1007/PL00000836 11814056
    • (2001) Cell Mol Life Sci , vol.58 , pp. 2053-2068
    • Ohanian, J.1    Ohanian, V.2
  • 6
    • 84859150636 scopus 로고    scopus 로고
    • Glutathione regulates caspase-dependent ceramide production and curcumin-induced apoptosis in human leukemic cells
    • 10.1016/j.freeradbiomed.2012.02.026 22387197
    • Glutathione regulates caspase-dependent ceramide production and curcumin-induced apoptosis in human leukemic cells. Kizhakkayil J, Thayyullathil F, Chathoth S, Hago A, Patel M, Galadari S, Free Radic Biol Med 2012 52 1854 1864 10.1016/j.freeradbiomed.2012.02.026 22387197
    • (2012) Free Radic Biol Med , vol.52 , pp. 1854-1864
    • Kizhakkayil, J.1    Thayyullathil, F.2    Chathoth, S.3    Hago, A.4    Patel, M.5    Galadari, S.6
  • 7
    • 43049085142 scopus 로고    scopus 로고
    • Sphingolipid signaling in the cardiovascular system: Good, bad or both?
    • 10.1016/j.ejphar.2008.02.089 18420192
    • Sphingolipid signaling in the cardiovascular system: good, bad or both? Alewijnse AE, Peters SL, Eur J Pharmacol 2008 585 292 302 10.1016/j.ejphar.2008. 02.089 18420192
    • (2008) Eur J Pharmacol , vol.585 , pp. 292-302
    • Alewijnse, A.E.1    Peters, S.L.2
  • 8
    • 74149083982 scopus 로고    scopus 로고
    • Deregulation of sphingolipid metabolism in Alzheimer's disease
    • 10.1016/j.neurobiolaging.2008.05.010 18547682
    • Deregulation of sphingolipid metabolism in Alzheimer's disease. He X, Huang Y, Li B, Gong CX, Schuchman EH, Neurobiol Aging 2010 31 398 408 10.1016/j.neurobiolaging.2008.05.010 18547682
    • (2010) Neurobiol Aging , vol.31 , pp. 398-408
    • He, X.1    Huang, Y.2    Li, B.3    Gong, C.X.4    Schuchman, E.H.5
  • 9
    • 0028085078 scopus 로고
    • The insulin signaling system
    • 8276779
    • The insulin signaling system. White MF, Kahn CR, J Biol Chem 1994 269 1 4 8276779
    • (1994) J Biol Chem , vol.269 , pp. 1-4
    • White, M.F.1    Kahn, C.R.2
  • 10
    • 0036710280 scopus 로고    scopus 로고
    • IRS proteins and the common path to diabetes
    • 12169433
    • IRS proteins and the common path to diabetes. White MF, Am J Physiol Endocrinol Metab 2002 283 413 E422 12169433
    • (2002) Am J Physiol Endocrinol Metab , vol.283
    • White, M.F.1
  • 11
    • 0028269980 scopus 로고
    • Insulin signalling: The role of insulin receptor substrate 1
    • 10.1016/0962-8924(94)90065-5 14731733
    • Insulin signalling: the role of insulin receptor substrate 1. Keller SR, Lienhard GE, Trends Cell Biol 1994 4 115 119 10.1016/0962-8924(94)90065-5 14731733
    • (1994) Trends Cell Biol , vol.4 , pp. 115-119
    • Keller, S.R.1    Lienhard, G.E.2
  • 12
    • 67349130083 scopus 로고    scopus 로고
    • Glycosphingolipids and insulin resistance
    • 10.1016/j.plipres.2009.03.002 19303901
    • Glycosphingolipids and insulin resistance. Langeveld M, Aerts JM, Prog Lipid Res 2009 48 196 205 10.1016/j.plipres.2009.03.002 19303901
    • (2009) Prog Lipid Res , vol.48 , pp. 196-205
    • Langeveld, M.1    Aerts, J.M.2
  • 13
    • 29244462334 scopus 로고    scopus 로고
    • Insulin signaling and the regulation of glucose transport
    • 16307172
    • Insulin signaling and the regulation of glucose transport. Chang L, Chiang SH, Saltiel AR, Mol Med 2004 10 65 71 16307172
    • (2004) Mol Med , vol.10 , pp. 65-71
    • Chang, L.1    Chiang, S.H.2    Saltiel, A.R.3
  • 14
    • 31644443192 scopus 로고    scopus 로고
    • Ceramides in insulin resistance and lipotoxicity
    • 10.1016/j.plipres.2005.11.002 16445986
    • Ceramides in insulin resistance and lipotoxicity. Summers SA, Prog Lipid Res 2006 45 42 72 10.1016/j.plipres.2005.11.002 16445986
    • (2006) Prog Lipid Res , vol.45 , pp. 42-72
    • Summers, S.A.1
  • 15
    • 0033588253 scopus 로고    scopus 로고
    • Ceramide generation is sufficient to account for the inhibition of the insulin-stimulated PKB pathway in C2C12 skeletal muscle cells pretreated with palmitate
    • 10.1074/jbc.274.34.24202
    • Ceramide generation is sufficient to account for the inhibition of the insulin-stimulated PKB pathway in C2C12 skeletal muscle cells pretreated with palmitate. Schmitz-Peiffer C, Craig DL, Biden TJ, J Biol Che 1999 274 24202 24210 10.1074/jbc.274.34.24202
    • (1999) J Biol Che , vol.274 , pp. 24202-24210
    • Schmitz-Peiffer, C.1    Craig, D.L.2    Biden, T.J.3
  • 16
    • 0035133331 scopus 로고    scopus 로고
    • Ceramide impairs the insulin-dependent membrane recruitment of protein kinase B leading to a loss in downstream signalling in L6 skeletal muscle cells
    • 10.1007/s001250051596 11270673
    • Ceramide impairs the insulin-dependent membrane recruitment of protein kinase B leading to a loss in downstream signalling in L6 skeletal muscle cells. Hajduch E, Balendran A, Batty IH, Litherland GJ, Blair AS, Downes CP, Hundal HS, Diabetologia 2001 44 173 183 10.1007/s001250051596 11270673
    • (2001) Diabetologia , vol.44 , pp. 173-183
    • Hajduch, E.1    Balendran, A.2    Batty, I.H.3    Litherland, G.J.4    Blair, A.S.5    Downes, C.P.6    Hundal, H.S.7
  • 17
    • 0037135536 scopus 로고    scopus 로고
    • De novo sphingolipid biosynthesis: A necessary, but dangerous, pathway
    • 10.1074/jbc.R200009200 12011104
    • De novo sphingolipid biosynthesis: a necessary, but dangerous, pathway. Merrill AH Jr, J Biol Chem 2002 277 25843 25846 10.1074/jbc.R200009200 12011104
    • (2002) J Biol Chem , vol.277 , pp. 25843-25846
    • Merrill Jr., A.H.1
  • 18
    • 42249105215 scopus 로고    scopus 로고
    • The sphingolipid salvage pathway in ceramide metabolism and signaling
    • 10.1016/j.cellsig.2007.12.006 18191382
    • The sphingolipid salvage pathway in ceramide metabolism and signaling. Kitatani K, Idkowiak-Baldys J, Hannun YA, Cell Signal 2008 20 1010 1018 10.1016/j.cellsig.2007.12.006 18191382
    • (2008) Cell Signal , vol.20 , pp. 1010-1018
    • Kitatani, K.1    Idkowiak-Baldys, J.2    Hannun, Y.A.3
  • 19
    • 38549152194 scopus 로고    scopus 로고
    • Principles of bioactive lipid signalling: Lessons from sphingolipids
    • 10.1038/nrm2329 18216770
    • Principles of bioactive lipid signalling: lessons from sphingolipids. Hannun YA, Obeid LM, Nat Rev Mol Cell Biol 2008 9 139 150 10.1038/nrm2329 18216770
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 139-150
    • Hannun, Y.A.1    Obeid, L.M.2
  • 21
    • 33845343984 scopus 로고    scopus 로고
    • Sphingolipid metabolism diseases
    • 10.1016/j.bbamem.2006.05.027 16854371
    • Sphingolipid metabolism diseases. Kolter T, Sandhoff K, Biochim Biophys Acta 2006 1758 2057 2079 10.1016/j.bbamem.2006.05.027 16854371
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 2057-2079
    • Kolter, T.1    Sandhoff, K.2
  • 22
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • 10.1038/nrm1496 15520809
    • Molecular mechanisms of caspase regulation during apoptosis. Riedl SJ, Shi Y, Nat Rev Mol Cell Biol 2004 5 897 907 10.1038/nrm1496 15520809
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 23
    • 1342305497 scopus 로고    scopus 로고
    • Caspase-12 and ER-stress-mediated apoptosis: The story so far
    • 10.1196/annals.1299.032 15033718
    • Caspase-12 and ER-stress-mediated apoptosis: the story so far. Szegezdi E, Fitzgerald U, Samali A, Ann N Y Acad Sci 2003 1010 186 194 10.1196/annals.1299.032 15033718
    • (2003) Ann N y Acad Sci , vol.1010 , pp. 186-194
    • Szegezdi, E.1    Fitzgerald, U.2    Samali, A.3
  • 24
    • 0035856952 scopus 로고    scopus 로고
    • Beta-Cell death during progression to diabetes
    • 10.1038/414792a 11742411
    • Beta-Cell death during progression to diabetes. Mathis D, Vence L, Benoist C, Nature 2001 414 792 798 10.1038/414792a 11742411
    • (2001) Nature , vol.414 , pp. 792-798
    • Mathis, D.1    Vence, L.2    Benoist, C.3
  • 26
    • 63849267286 scopus 로고    scopus 로고
    • Recent progress in research on beta-cell apoptosis by cytokines
    • 19273093
    • Recent progress in research on beta-cell apoptosis by cytokines. Kim KA, Lee MS, Front Biosci 2009 14 657 664 19273093
    • (2009) Front Biosci , vol.14 , pp. 657-664
    • Kim, K.A.1    Lee, M.S.2
  • 27
    • 80051757598 scopus 로고    scopus 로고
    • Ceramide formation as a target in beta-cell survival and function
    • 10.1517/14728222.2011.588209 21635197
    • Ceramide formation as a target in beta-cell survival and function. Lang F, Ullrich S, Gulbins E, Expert Opin Ther Targets 2011 15 1061 1071 10.1517/14728222.2011.588209 21635197
    • (2011) Expert Opin Ther Targets , vol.15 , pp. 1061-1071
    • Lang, F.1    Ullrich, S.2    Gulbins, E.3
  • 29
    • 0029059122 scopus 로고
    • Ceramide inhibits pancreatic beta-cell insulin production and mitogenesis and mimics the actions of interleukin-1 beta
    • 10.1016/0014-5793(95)00470-T 7607324
    • Ceramide inhibits pancreatic beta-cell insulin production and mitogenesis and mimics the actions of interleukin-1 beta. Sjoholm A, FEBS Lett 1995 367 283 286 10.1016/0014-5793(95)00470-T 7607324
    • (1995) FEBS Lett , vol.367 , pp. 283-286
    • Sjoholm, A.1
  • 30
    • 0029932759 scopus 로고    scopus 로고
    • Interleukin-1 beta-induced ceramide and diacylglycerol generation may lead to activation of the c-Jun NH2-terminal kinase and the transcription factor ATF2 in the insulin-producing cell line RINm5F
    • 8626526
    • Interleukin-1 beta-induced ceramide and diacylglycerol generation may lead to activation of the c-Jun NH2-terminal kinase and the transcription factor ATF2 in the insulin-producing cell line RINm5F. Welsh N, J Biol Chem 1996 271 8307 8312 8626526
    • (1996) J Biol Chem , vol.271 , pp. 8307-8312
    • Welsh, N.1
  • 31
    • 0032989112 scopus 로고    scopus 로고
    • Activation of the sphingomyelinase/ceramide signal transduction pathway in insulin-secreting beta-cells: Role in cytokine-induced beta-cell death
    • 10.2337/diabetes.48.7.1372 10389841
    • Activation of the sphingomyelinase/ceramide signal transduction pathway in insulin-secreting beta-cells: role in cytokine-induced beta-cell death. Major CD, Gao ZY, Wolf BA, Diabetes 1999 48 1372 1380 10.2337/diabetes.48.7.1372 10389841
    • (1999) Diabetes , vol.48 , pp. 1372-1380
    • Major, C.D.1    Gao, Z.Y.2    Wolf, B.A.3
  • 32
    • 66949148332 scopus 로고    scopus 로고
    • Acute activation of acid ceramidase affects cytokine-induced cytotoxicity in rat islet beta-cells
    • 10.1016/j.febslet.2009.05.047 19497324
    • Acute activation of acid ceramidase affects cytokine-induced cytotoxicity in rat islet beta-cells. Zhu Q, Shan X, Miao H, Lu Y, Xu J, You N, Liu C, Liao DF, Jin J, FEBS Lett 2009 583 2136 2141 10.1016/j.febslet.2009.05.047 19497324
    • (2009) FEBS Lett , vol.583 , pp. 2136-2141
    • Zhu, Q.1    Shan, X.2    Miao, H.3    Lu, Y.4    Xu, J.5    You, N.6    Liu, C.7    Liao, D.F.8    Jin, J.9
  • 33
    • 17844364503 scopus 로고    scopus 로고
    • Sphingosine kinase activity and sphingosine-1 phosphate production in rat pancreatic islets and INS-1 cells: Response to cytokines
    • 10.2337/diabetes.54.5.1429 15855330
    • Sphingosine kinase activity and sphingosine-1 phosphate production in rat pancreatic islets and INS-1 cells: response to cytokines. Mastrandrea LD, Sessanna SM, Laychock SG, Diabetes 2005 54 1429 1436 10.2337/diabetes.54.5.1429 15855330
    • (2005) Diabetes , vol.54 , pp. 1429-1436
    • Mastrandrea, L.D.1    Sessanna, S.M.2    Laychock, S.G.3
  • 34
    • 0032478314 scopus 로고    scopus 로고
    • Fatty acid-induced beta cell apoptosis: A link between obesity and diabetes
    • 10.1073/pnas.95.5.2498 9482914
    • Fatty acid-induced beta cell apoptosis: a link between obesity and diabetes. Shimabukuro M, Zhou YT, Levi M, Unger RH, Proc Natl Acad Sci USA 1998 95 2498 2502 10.1073/pnas.95.5.2498 9482914
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2498-2502
    • Shimabukuro, M.1    Zhou, Y.T.2    Levi, M.3    Unger, R.H.4
  • 35
    • 0035156817 scopus 로고    scopus 로고
    • Distinct effects of saturated and monounsaturated fatty acids on beta-cell turnover and function
    • 10.2337/diabetes.50.1.69 11147797
    • Distinct effects of saturated and monounsaturated fatty acids on beta-cell turnover and function. Maedler K, Spinas GA, Dyntar D, Moritz W, Kaiser N, Donath MY, Diabetes 2001 50 69 76 10.2337/diabetes.50.1.69 11147797
    • (2001) Diabetes , vol.50 , pp. 69-76
    • Maedler, K.1    Spinas, G.A.2    Dyntar, D.3    Moritz, W.4    Kaiser, N.5    Donath, M.Y.6
  • 36
    • 0036315888 scopus 로고    scopus 로고
    • Prolonged exposure to free fatty acids has cytostatic and proapoptotic effects on human pancreatic islets: Evidence that beta cell death is caspase mediated, partially dependent on ceramide pathway, and Bcl-2 regulated
    • 10.2337/diabetes.51.5.1437 11978640
    • Prolonged exposure to free fatty acids has cytostatic and proapoptotic 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, Santangelo C, Patané G, Boggi U, Piro S, Anello M, Bergamini E, Mosca F, Di Mario U, Del Prato S, Marchetti P, Diabetes 2002 51 1437 1442 10.2337/diabetes.51.5.1437 11978640
    • (2002) Diabetes , vol.51 , pp. 1437-1442
    • Lupi, R.1    Dotta, F.2    Marselli, L.3    Del Guerra, S.4    Masini, M.5    Santangelo, C.6    Patané, G.7    Boggi, U.8    Piro, S.9    Anello, M.10    Bergamini, E.11    Mosca, F.12    Di Mario, U.13    Del Prato, S.14    Marchetti, P.15
  • 37
    • 0345354674 scopus 로고    scopus 로고
    • Monounsaturated fatty acids prevent the deleterious effects of palmitate and high glucose on human pancreatic beta-cell turnover and function
    • 10.2337/diabetes.52.3.726 12606514
    • Monounsaturated fatty acids prevent the deleterious effects of palmitate and high glucose on human pancreatic beta-cell turnover and function. Maedler K, Oberholzer J, Bucher P, Spinas GA, Donath MY, Diabetes 2003 52 726 733 10.2337/diabetes.52.3.726 12606514
    • (2003) Diabetes , vol.52 , pp. 726-733
    • Maedler, K.1    Oberholzer, J.2    Bucher, P.3    Spinas, G.A.4    Donath, M.Y.5
  • 39
    • 0032484132 scopus 로고    scopus 로고
    • Lipoapoptosis in beta-cells of obese prediabetic fa/fa rats. Role of serine palmitoyltransferase overexpression
    • 10.1074/jbc.273.49.32487 9829981
    • Lipoapoptosis in beta-cells of obese prediabetic fa/fa rats. Role of serine palmitoyltransferase overexpression. Shimabukuro M, Higa M, Zhou YT, Wang MY, Newgard CB, Unger RH, J Biol Chem 1998 273 32487 32490 10.1074/jbc.273.49. 32487 9829981
    • (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
  • 41
    • 84864396455 scopus 로고    scopus 로고
    • Roles of ceramide and sphingolipids in pancreatic β-cell function and dysfunction
    • 10.4161/isl.20102 22847494
    • Roles of ceramide and sphingolipids in pancreatic β-cell function and dysfunction. Boslem E, Meikle PJ, Biden TJ, Islets 2012 4 177 187 10.4161/isl.20102 22847494
    • (2012) Islets , vol.4 , pp. 177-187
    • Boslem, E.1    Meikle, P.J.2    Biden, T.J.3
  • 42
    • 4544261024 scopus 로고    scopus 로고
    • Subcellular compartmentalization of ceramide metabolism: MAM (mitochondria-associated membrane) and/or mitochondria?
    • 10.1042/BJ20031819 15144238
    • Subcellular compartmentalization of ceramide metabolism: MAM (mitochondria-associated membrane) and/or mitochondria? Bionda C, Portoukalian J, Schmitt D, Rodriguez-Lafrasse C, Ardail D, Biochem J 2004 382 527 533 10.1042/BJ20031819 15144238
    • (2004) Biochem J , vol.382 , pp. 527-533
    • Bionda, C.1    Portoukalian, J.2    Schmitt, D.3    Rodriguez-Lafrasse, C.4    Ardail, D.5
  • 43
    • 79952836464 scopus 로고    scopus 로고
    • A lipidomic screen of palmitate-treated MIN6 β-cells links sphingolipid metabolites with endoplasmic reticulum (ER) stress and impaired protein trafficking
    • 10.1042/BJ20101867 21265737
    • A lipidomic screen of palmitate-treated MIN6 β-cells links sphingolipid metabolites with endoplasmic reticulum (ER) stress and impaired protein trafficking. Boslem E, MacIntosh G, Preston AM, Bartley C, Busch AK, Fuller M, Laybutt DR, Meikle PJ, Biden TJ, Biochem J 2011 435 267 276 10.1042/BJ20101867 21265737
    • (2011) Biochem J , vol.435 , pp. 267-276
    • Boslem, E.1    Macintosh, G.2    Preston, A.M.3    Bartley, C.4    Busch, A.K.5    Fuller, M.6    Laybutt, D.R.7    Meikle, P.J.8    Biden, T.J.9
  • 44
    • 79960814460 scopus 로고    scopus 로고
    • Ceramide synthase 4 and de novo production of ceramides with specific N-acyl chain lengths are involved in glucolipotoxicity-induced apoptosis of INS-1 β-cells
    • 10.1042/BJ20101386 21592087
    • Ceramide synthase 4 and de novo production of ceramides with specific N-acyl chain lengths are involved in glucolipotoxicity-induced apoptosis of INS-1 β-cells. Veret J, Coant N, Berdyshev EV, Skobeleva A, Therville N, Bailbé D, Gorshkova I, Natarajan V, Portha B, Le Stunff H, Biochem J 2011 438 177 189 10.1042/BJ20101386 21592087
    • (2011) Biochem J , vol.438 , pp. 177-189
    • Veret, J.1    Coant, N.2    Berdyshev, E.V.3    Skobeleva, A.4    Therville, N.5    Bailbé, D.6    Gorshkova, I.7    Natarajan, V.8    Portha, B.9    Le Stunff, H.10
  • 45
    • 20444430478 scopus 로고    scopus 로고
    • Apoptotic pathways: Ten minutes to dead
    • 10.1016/j.cell.2005.05.019 15935754
    • Apoptotic pathways: ten minutes to dead. Green DR, Cell 2005 121 671 674 10.1016/j.cell.2005.05.019 15935754
    • (2005) Cell , vol.121 , pp. 671-674
    • Green, D.R.1
  • 46
    • 39749182234 scopus 로고    scopus 로고
    • Apoptosis: Controlled demolition at the cellular level
    • 18073771
    • Apoptosis: controlled demolition at the cellular level. Taylor RC, Cullen SP, Martin SJ, Nat Rev Mol Cell Biol 2008 9 231 241 18073771
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 231-241
    • Taylor, R.C.1    Cullen, S.P.2    Martin, S.J.3
  • 49
    • 17644379373 scopus 로고    scopus 로고
    • Caspase-3-dependent beta-cell apoptosis in the initiation of autoimmune diabetes mellitus
    • 10.1128/MCB.25.9.3620-3629.2005 15831467
    • Caspase-3-dependent beta-cell apoptosis in the initiation of autoimmune diabetes mellitus. Liadis N, Murakami K, Eweida M, Elford AR, Sheu L, Gaisano HY, Hakem R, Ohashi PS, Woo M, Mol Cell Biol 2005 25 3620 3629 10.1128/MCB.25.9.3620-3629.2005 15831467
    • (2005) Mol Cell Biol , vol.25 , pp. 3620-3629
    • Liadis, N.1    Murakami, K.2    Eweida, M.3    Elford, A.R.4    Sheu, L.5    Gaisano, H.Y.6    Hakem, R.7    Ohashi, P.S.8    Woo, M.9
  • 50
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: Outer membrane permeabilization and beyond
    • 10.1038/nrm2952 20683470
    • Mitochondria and cell death: outer membrane permeabilization and beyond. Tait SW, Green DR, Nat Rev Mol Cell Biol 2010 11 621 632 10.1038/nrm2952 20683470
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 52
    • 0035199418 scopus 로고    scopus 로고
    • Selective hydrolysis of a mitochondrial pool of sphingomyelin induces apoptosis
    • 10.1096/fj.01-0539com 11726543
    • Selective hydrolysis of a mitochondrial pool of sphingomyelin induces apoptosis. Birbes H, El Bawab S, Hannun YA, Obeid LM, FASEB J 2001 15 2669 2679 10.1096/fj.01-0539com 11726543
    • (2001) FASEB J , vol.15 , pp. 2669-2679
    • Birbes, H.1    El Bawab, S.2    Hannun, Y.A.3    Obeid, L.M.4
  • 53
    • 15944425766 scopus 로고    scopus 로고
    • A mitochondrial pool of sphingomyelin is involved in TNFalpha-induced Bax translocation to mitochondria
    • 10.1042/BJ20041627 15516208
    • A mitochondrial pool of sphingomyelin is involved in TNFalpha-induced Bax translocation to mitochondria. Birbes H, Luberto C, Hsu YT, El Bawab S, Hannun YA, Obeid LM, Biochem J 2005 386 445 451 10.1042/BJ20041627 15516208
    • (2005) Biochem J , vol.386 , pp. 445-451
    • Birbes, H.1    Luberto, C.2    Hsu, Y.T.3    El Bawab, S.4    Hannun, Y.A.5    Obeid, L.M.6
  • 54
    • 20144367155 scopus 로고    scopus 로고
    • Acid sphingomyelinase is indispensable for UV light-induced Bax conformational change at the mitochondrial membrane
    • 10.1074/jbc.M410869200 15743760
    • Acid sphingomyelinase is indispensable for UV light-induced Bax conformational change at the mitochondrial membrane. Kashkar H, Wiegmann V, Yazdanpanah B, Haubert D, Kronke M, J Biol Chem 2005 280 20804 20813 10.1074/jbc.M410869200 15743760
    • (2005) J Biol Chem , vol.280 , pp. 20804-20813
    • Kashkar, H.1    Wiegmann, V.2    Yazdanpanah, B.3    Haubert, D.4    Kronke, M.5
  • 55
    • 0036375662 scopus 로고    scopus 로고
    • Mitochondria and ceramide: Intertwined roles in regulation of apoptosis
    • 12123710
    • Mitochondria and ceramide: intertwined roles in regulation of apoptosis. Birbes H, El Bawab S, Obeid LM, Hannun YA, Adv Enzyme Regul 2002 42 113 129 12123710
    • (2002) Adv Enzyme Regul , vol.42 , pp. 113-129
    • Birbes, H.1    El Bawab, S.2    Obeid, L.M.3    Hannun, Y.A.4
  • 56
    • 0033957476 scopus 로고    scopus 로고
    • Transgenic overexpression of human Bcl-2 in islet beta cells inhibits apoptosis but does not prevent autoimmune destruction
    • 10.1093/intimm/12.1.9 10607745
    • Transgenic overexpression of human Bcl-2 in islet beta cells inhibits apoptosis but does not prevent autoimmune destruction. Allison J, Thomas H, Beck D, Brady JL, Lew AM, Elefanty A, Kosaka H, Kay TW, Huang DC, Strasser A, Int Immunol 2000 12 9 17 10.1093/intimm/12.1.9 10607745
    • (2000) Int Immunol , vol.12 , pp. 9-17
    • Allison, J.1    Thomas, H.2    Beck, D.3    Brady, J.L.4    Lew, A.M.5    Elefanty, A.6    Kosaka, H.7    Kay, T.W.8    Huang, D.C.9    Strasser, A.10
  • 57
    • 0037030465 scopus 로고    scopus 로고
    • Ceramide induces mitochondrial activation and apoptosis via a Bax-dependent pathway in human carcinoma cells
    • 10.1038/sj.onc.1205497 12037683
    • Ceramide induces mitochondrial activation and apoptosis via a Bax-dependent pathway in human carcinoma cells. Von Haefen C, Wieder T, Gillissen B, Starck L, Graupner V, Dorken B, Daniel PT, Oncogene 2002 21 4009 4019 10.1038/sj.onc.1205497 12037683
    • (2002) Oncogene , vol.21 , pp. 4009-4019
    • Von Haefen, C.1    Wieder, T.2    Gillissen, B.3    Starck, L.4    Graupner, V.5    Dorken, B.6    Daniel, P.T.7
  • 58
    • 0037230114 scopus 로고    scopus 로고
    • Mitochondrial dysfunction is involved in apoptosis induced by serum withdrawal and fatty acids in the beta-cell line INS-1
    • 10.1210/en.2001-211282 12488362
    • Mitochondrial dysfunction is involved in apoptosis induced by serum withdrawal and fatty acids in the beta-cell line INS-1. Maestre I, Jordan J, Calvo S, Reig JA, Cena V, Soria B, Prentki M, Roche E, Endocrinology 2003 144 335 345 10.1210/en.2001-211282 12488362
    • (2003) Endocrinology , vol.144 , pp. 335-345
    • Maestre, I.1    Jordan, J.2    Calvo, S.3    Reig, J.A.4    Cena, V.5    Soria, B.6    Prentki, M.7    Roche, E.8
  • 59
    • 33745037188 scopus 로고    scopus 로고
    • Ceramide forms channels in mitochondrial outer membranes at physiologically relevant concentrations
    • 10.1016/j.mito.2006.03.002 16713754
    • Ceramide forms channels in mitochondrial outer membranes at physiologically relevant concentrations. Siskind LJ, Kolesnick RN, Colombini M, Mitochondrion 2006 6 118 125 10.1016/j.mito.2006.03.002 16713754
    • (2006) Mitochondrion , vol.6 , pp. 118-125
    • Siskind, L.J.1    Kolesnick, R.N.2    Colombini, M.3
  • 60
    • 0033758144 scopus 로고    scopus 로고
    • Akt mediates insulin rescue from apoptosis in brown adipocytes: Effect of ceramide
    • 10.1054/ghir.2000.0165 11042022
    • Akt mediates insulin rescue from apoptosis in brown adipocytes: effect of ceramide. Navarro P, Valverde AM, Rohn JL, Benito M, Lorenzo M, Growth Horm IGF Res 2000 10 256 266 10.1054/ghir.2000.0165 11042022
    • (2000) Growth Horm IGF Res , vol.10 , pp. 256-266
    • Navarro, P.1    Valverde, A.M.2    Rohn, J.L.3    Benito, M.4    Lorenzo, M.5
  • 61
    • 79651474666 scopus 로고    scopus 로고
    • Reactive oxygen species and insulin resistance: The good, the bad and the ugly
    • 10.1016/j.tips.2010.11.006 21159388
    • Reactive oxygen species and insulin resistance: the good, the bad and the ugly. Tiganis T, Trends Pharmacol Sci 2011 32 82 89 10.1016/j.tips.2010.11.006 21159388
    • (2011) Trends Pharmacol Sci , vol.32 , pp. 82-89
    • Tiganis, T.1
  • 62
    • 12344286763 scopus 로고    scopus 로고
    • Endostatin uncouples NO and Ca2+ response to bradykinin through enhanced O2*- production in the intact coronary endothelium
    • 15471985
    • Endostatin uncouples NO and Ca2+ response to bradykinin through enhanced O2*- production in the intact coronary endothelium. Zhang AY, Teggatz EG, Zou AP, Campbell WB, Li PL, Am J Physiol Heart Circ Physiol 2005 288 686 H694 15471985
    • (2005) Am J Physiol Heart Circ Physiol , vol.288
    • Zhang, A.Y.1    Teggatz, E.G.2    Zou, A.P.3    Campbell, W.B.4    Li, P.L.5
  • 63
    • 1842330849 scopus 로고    scopus 로고
    • Direct effect of ceramide on the mitochondrial electron transport chain leads to generation of reactive oxygen species. Role of mitochondrial glutathione
    • 10.1074/jbc.272.17.11369 9111045
    • Direct effect of ceramide on the mitochondrial electron transport chain leads to generation of reactive oxygen species. Role of mitochondrial glutathione. García-Ruiz C, Colell A, Marí M, Morales A, Fernandez-Checa JC, J Biol Chem 1997 272 11369 11377 10.1074/jbc.272.17.11369 9111045
    • (1997) J Biol Chem , vol.272 , pp. 11369-11377
    • García-Ruiz, C.1    Colell, A.2    Marí, M.3    Morales, A.4    Fernandez-Checa, J.C.5
  • 64
    • 0032584532 scopus 로고    scopus 로고
    • Reactive oxygen species enhances the induction of inducible nitric oxide synthase by sphingomyelinase in RAW264.7 cells
    • 10.1016/S0005-2760(98)00066-6 9714807
    • Reactive oxygen species enhances the induction of inducible nitric oxide synthase by sphingomyelinase in RAW264.7 cells. Hatanaka Y, Fujii J, Fukutomi T, Watanabe T, Che W, Sanada Y, Igarashi Y, Taniguchi N, Biochim Biophys Acta 1998 1393 203 210 10.1016/S0005-2760(98)00066-6 9714807
    • (1998) Biochim Biophys Acta , vol.1393 , pp. 203-210
    • Hatanaka, Y.1    Fujii, J.2    Fukutomi, T.3    Watanabe, T.4    Che, W.5    Sanada, Y.6    Igarashi, Y.7    Taniguchi, N.8
  • 66
    • 0346577312 scopus 로고    scopus 로고
    • NO induced apoptosis of vascular smooth muscle cells accompanied by ceramide increase
    • 10.1002/jcp.10464 15040013
    • NO induced apoptosis of vascular smooth muscle cells accompanied by ceramide increase. Pilane CM, LaBelle EF, J Cell Physiol 2004 199 310 315 10.1002/jcp.10464 15040013
    • (2004) J Cell Physiol , vol.199 , pp. 310-315
    • Pilane, C.M.1    Labelle, E.F.2
  • 67
    • 2242423614 scopus 로고    scopus 로고
    • Nitric oxide induces degradation of the neutral ceramidase in rat renal mesangial cells and is counterregulated by protein kinase C
    • 10.1074/jbc.M204034200 12359735
    • Nitric oxide induces degradation of the neutral ceramidase in rat renal mesangial cells and is counterregulated by protein kinase C. Franzen R, Fabbro D, Aschrafi A, Pfeilschifter J, Huwiler A, J Biol Chem 2002 277 46184 46190 10.1074/jbc.M204034200 12359735
    • (2002) J Biol Chem , vol.277 , pp. 46184-46190
    • Franzen, R.1    Fabbro, D.2    Aschrafi, A.3    Pfeilschifter, J.4    Huwiler, A.5
  • 68
    • 0034612304 scopus 로고    scopus 로고
    • Ceramide interaction with the respiratory chain of heart mitochondria
    • 10.1021/bi9924415 10828984
    • Ceramide interaction with the respiratory chain of heart mitochondria. Di Paola M, Cocco T, Lorusso M, Biochemistry 2000 39 6660 6668 10.1021/bi9924415 10828984
    • (2000) Biochemistry , vol.39 , pp. 6660-6668
    • Di Paola, M.1    Cocco, T.2    Lorusso, M.3
  • 69
    • 0030856714 scopus 로고    scopus 로고
    • Direct inhibition of mitochondrial respiratory chain complex III by cell-permeable ceramide
    • 10.1074/jbc.272.39.24154 9305864
    • Direct inhibition of mitochondrial respiratory chain complex III by cell-permeable ceramide. Gudz TI, Tserng KY, Hoppel CL, J Biol Chem 1997 272 24154 24158 10.1074/jbc.272.39.24154 9305864
    • (1997) J Biol Chem , vol.272 , pp. 24154-24158
    • Gudz, T.I.1    Tserng, K.Y.2    Hoppel, C.L.3
  • 70
    • 22844440003 scopus 로고    scopus 로고
    • Involvement of NADPH oxidase isoforms and Src family kinases in CD95-dependent hepatocyte apoptosis
    • 10.1074/jbc.M414361200 15917250
    • Involvement of NADPH oxidase isoforms and Src family kinases in CD95-dependent hepatocyte apoptosis. Reinehr R, Becker S, Eberle A, Grether-Beck S, Haussinger D, J Biol Chem 2005 280 27179 27194 10.1074/jbc.M414361200 15917250
    • (2005) J Biol Chem , vol.280 , pp. 27179-27194
    • Reinehr, R.1    Becker, S.2    Eberle, A.3    Grether-Beck, S.4    Haussinger, D.5
  • 72
    • 0032482988 scopus 로고    scopus 로고
    • Protection against lipoapoptosis of beta cells through leptin-dependent maintenance of Bcl-2 expression
    • 10.1073/pnas.95.16.9558 9689119
    • Protection against lipoapoptosis of beta cells through leptin-dependent maintenance of Bcl-2 expression. Shimabukuro M, Wang MY, Zhou YT, Newgard CB, Unger RH, Proc Natl Acad Sci U S A 1998 95 9558 9561 10.1073/pnas.95.16.9558 9689119
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 9558-9561
    • Shimabukuro, M.1    Wang, M.Y.2    Zhou, Y.T.3    Newgard, C.B.4    Unger, R.H.5
  • 73
    • 0037203345 scopus 로고    scopus 로고
    • Lipoapoptosis: Its mechanism and its diseases
    • 10.1016/S1388-1981(02)00342-6 12531555
    • Lipoapoptosis: its mechanism and its diseases. Unger RH, Orci L, Biochim Biophys Acta 2002 1585 202 212 10.1016/S1388-1981(02)00342-6 12531555
    • (2002) Biochim Biophys Acta , vol.1585 , pp. 202-212
    • Unger, R.H.1    Orci, L.2
  • 74
    • 0942287672 scopus 로고    scopus 로고
    • The role of neutral sphingomyelinase produced ceramide in lipopolysaccharide-mediated expression of inducible nitric oxide synthase
    • 14720208
    • The role of neutral sphingomyelinase produced ceramide in lipopolysaccharide-mediated expression of inducible nitric oxide synthase. Won JS, Im YB, Khan M, Singh AK, Singh I, J Neurochem 2004 88 583 593 14720208
    • (2004) J Neurochem , vol.88 , pp. 583-593
    • Won, J.S.1    Im, Y.B.2    Khan, M.3    Singh, A.K.4    Singh, I.5
  • 76
    • 43549105167 scopus 로고    scopus 로고
    • The unfolded protein response: A pathway that links insulin demand with beta-cell failure and diabetes
    • 18436705
    • The unfolded protein response: a pathway that links insulin demand with beta-cell failure and diabetes. Scheuner D, Kaufman RJ, Endocr Rev 2008 29 317 333 18436705
    • (2008) Endocr Rev , vol.29 , pp. 317-333
    • Scheuner, D.1    Kaufman, R.J.2
  • 77
    • 39149104320 scopus 로고    scopus 로고
    • The role for endoplasmic reticulum stress in diabetes mellitus
    • 18048764
    • The role for endoplasmic reticulum stress in diabetes mellitus. Eizirik DL, Cardozo AK, Cnop M, Endocr Rev 2008 29 42 61 18048764
    • (2008) Endocr Rev , vol.29 , pp. 42-61
    • Eizirik, D.L.1    Cardozo, A.K.2    Cnop, M.3
  • 78
    • 70449494871 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in beta-cells and development of diabetes
    • 10.1016/j.coph.2009.07.003 19665428
    • Endoplasmic reticulum stress in beta-cells and development of diabetes. Fonseca SG, Burcin M, Gromada J, Urano F, Curr Opin Pharmacol 2009 9 763 770 10.1016/j.coph.2009.07.003 19665428
    • (2009) Curr Opin Pharmacol , vol.9 , pp. 763-770
    • Fonseca, S.G.1    Burcin, M.2    Gromada, J.3    Urano, F.4
  • 79
    • 84855605795 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress, obesity and diabetes
    • 10.1016/j.molmed.2011.07.010 21889406
    • Endoplasmic reticulum stress, obesity and diabetes. Cnop M, Foufelle F, Velloso LA, Trends Mol Med 2012 18 59 68 10.1016/j.molmed.2011.07.010 21889406
    • (2012) Trends Mol Med , vol.18 , pp. 59-68
    • Cnop, M.1    Foufelle, F.2    Velloso, L.A.3
  • 80
    • 0036022403 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-mediated apoptosis in pancreatic beta-cells
    • 10.1023/A:1016175429877 12101393
    • Endoplasmic reticulum stress-mediated apoptosis in pancreatic beta-cells. Oyadomari S, Araki E, Mori M, Apoptosis 2002 7 335 345 10.1023/A:1016175429877 12101393
    • (2002) Apoptosis , vol.7 , pp. 335-345
    • Oyadomari, S.1    Araki, E.2    Mori, M.3
  • 81
    • 1942475176 scopus 로고    scopus 로고
    • The role of endoplasmic reticulum stress in nonimmune diabetes: NOD.k iHEL, a novel model of beta cell death
    • 10.1196/annals.1288.022 14679055
    • The role of endoplasmic reticulum stress in nonimmune diabetes: NOD.k iHEL, a novel model of beta cell death. Socha L, Silva D, Lesage S, Goodnow C, Petrovsky N, Ann N Y Acad Sci 2003 1005 178 183 10.1196/annals.1288.022 14679055
    • (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
  • 82
  • 83
    • 40449106191 scopus 로고    scopus 로고
    • Differential activation of ER stress and apoptosis in response to chronically elevated free fatty acids in pancreatic beta-cells
    • 10.1152/ajpendo.00478.2007 18198352
    • Differential activation of ER stress and apoptosis in response to chronically elevated free fatty acids in pancreatic beta-cells. Lai E, Bikopoulos G, Wheeler MB, Rozakis-Adcock M, Volchuk A, Am J Physiol Endocrinol Metab 2008 294 540 E550 10.1152/ajpendo.00478.2007 18198352
    • (2008) Am J Physiol Endocrinol Metab , vol.294
    • Lai, E.1    Bikopoulos, G.2    Wheeler, M.B.3    Rozakis-Adcock, M.4    Volchuk, A.5
  • 84
    • 77953285560 scopus 로고    scopus 로고
    • Group VIA Ca2 + -independent phospholipase A2 (iPLA2beta) and its role in beta-cell programmed cell death
    • 10.1016/j.biochi.2010.01.005 20083151
    • Group VIA Ca2 + -independent phospholipase A2 (iPLA2beta) and its role in beta-cell programmed cell death. Lei X, Barbour SE, Ramanadham S, Biochimie 2010 92 627 637 10.1016/j.biochi.2010.01.005 20083151
    • (2010) Biochimie , vol.92 , pp. 627-637
    • Lei, X.1    Barbour, S.E.2    Ramanadham, S.3
  • 85
    • 66749163678 scopus 로고    scopus 로고
    • Disulfide formation in the ER and mitochondria: Two solutions to a common process
    • 10.1126/science.1170653 19498160
    • Disulfide formation in the ER and mitochondria: two solutions to a common process. Riemer J, Bulleid N, Herrmann JM, Science 2009 324 1284 1287 10.1126/science.1170653 19498160
    • (2009) Science , vol.324 , pp. 1284-1287
    • Riemer, J.1    Bulleid, N.2    Herrmann, J.M.3
  • 86
    • 0037352170 scopus 로고    scopus 로고
    • Involvement of PI3K/Akt pathway in cell cycle progression, apoptosis, and neoplastic transformation: A target for cancer chemotherapy
    • 10.1038/sj.leu.2402824 12646949
    • Involvement of PI3K/Akt pathway in cell cycle progression, apoptosis, and neoplastic transformation: a target for cancer chemotherapy. Chang F, Lee JT, Navolanic PM, Steelman LS, Shelton JG, Blalock WL, Franklin RA, McCubrey JA, Leukemia 2003 17 590 603 10.1038/sj.leu.2402824 12646949
    • (2003) Leukemia , vol.17 , pp. 590-603
    • Chang, F.1    Lee, J.T.2    Navolanic, P.M.3    Steelman, L.S.4    Shelton, J.G.5    Blalock, W.L.6    Franklin, R.A.7    McCubrey, J.A.8
  • 87
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • 10.1016/S0092-8674(00)81067-3 8601312
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Muslin AJ, Tanner JW, Allen PM, Shaw AS, Cell 1996 84 889 897 10.1016/S0092-8674(00)81067-3 8601312
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 88
    • 0031809427 scopus 로고    scopus 로고
    • Protein kinase C isoforms alpha, delta and theta require insulin receptor substrate-1 to inhibit the tyrosine kinase activity of the insulin receptor in human kidney embryonic cells (HEK 293 cells)
    • 10.1007/s001250050995 9686926
    • Protein kinase C isoforms alpha, delta and theta require insulin receptor substrate-1 to inhibit the tyrosine kinase activity of the insulin receptor in human kidney embryonic cells (HEK 293 cells). Kellerer M, Mushack J, Seffer E, Mischak H, Ullrich A, Haring HU, Diabetologia 1998 41 833 838 10.1007/s001250050995 9686926
    • (1998) Diabetologia , vol.41 , pp. 833-838
    • Kellerer, M.1    Mushack, J.2    Seffer, E.3    Mischak, H.4    Ullrich, A.5    Haring, H.U.6
  • 89
    • 34250303939 scopus 로고    scopus 로고
    • Key role for ceramides in mediating insulin resistance in human muscle cells
    • 10.1074/jbc.M611157200 17337731
    • Key role for ceramides in mediating insulin resistance in human muscle cells. Pickersgill L, Litherland GJ, Greenberg AS, Walker M, Yeaman SJ, J Biol Chem 2007 282 12583 12589 10.1074/jbc.M611157200 17337731
    • (2007) J Biol Chem , vol.282 , pp. 12583-12589
    • Pickersgill, L.1    Litherland, G.J.2    Greenberg, A.S.3    Walker, M.4    Yeaman, S.J.5
  • 90
    • 33847628837 scopus 로고    scopus 로고
    • Fatty acid-induced defects in insulin signalling, in myotubes derived from children, are related to ceramide production from palmitate rather than the accumulation of intramyocellular lipid
    • 10.1002/jcp.20922 17219404
    • Fatty acid-induced defects in insulin signalling, in myotubes derived from children, are related to ceramide production from palmitate rather than the accumulation of intramyocellular lipid. Sabin MA, Stewart CE, Crowne EC, Turner SJ, Hunt LP, Welsh GI, Grohmann MJ, Holly JM, Shield JP, J Cell Physiol 2007 211 244 252 10.1002/jcp.20922 17219404
    • (2007) J Cell Physiol , vol.211 , pp. 244-252
    • Sabin, M.A.1    Stewart, C.E.2    Crowne, E.C.3    Turner, S.J.4    Hunt, L.P.5    Welsh, G.I.6    Grohmann, M.J.7    Holly, J.M.8    Shield, J.P.9
  • 92
    • 0038532298 scopus 로고    scopus 로고
    • A role for ceramide, but not diacylglycerol, in the antagonism of insulin signal transduction by saturated fatty acids
    • 10.1074/jbc.M212307200 12525490
    • A role for ceramide, but not diacylglycerol, in the antagonism of insulin signal transduction by saturated fatty acids. Chavez JA, Knotts TA, Wang LP, Li G, Dobrowsky RT, Florant GL, Summers SA, J Biol Chem 2003 278 10297 10303 10.1074/jbc.M212307200 12525490
    • (2003) J Biol Chem , vol.278 , pp. 10297-10303
    • Chavez, J.A.1    Knotts, T.A.2    Wang, L.P.3    Li, G.4    Dobrowsky, R.T.5    Florant, G.L.6    Summers, S.A.7
  • 93
    • 21244442275 scopus 로고    scopus 로고
    • Acid ceramidase overexpression prevents the inhibitory effects of saturated fatty acids on insulin signaling
    • 10.1074/jbc.M412769200 15774472
    • Acid ceramidase overexpression prevents the inhibitory effects of saturated fatty acids on insulin signaling. Chavez JA, Holland WL, Bar J, Sandhoff K, Summers SA, J Biol Chem 2005 280 20148 20153 10.1074/jbc.M412769200 15774472
    • (2005) J Biol Chem , vol.280 , pp. 20148-20153
    • Chavez, J.A.1    Holland, W.L.2    Bar, J.3    Sandhoff, K.4    Summers, S.A.5
  • 94
    • 4544242908 scopus 로고    scopus 로고
    • Intracellular ceramide synthesis and protein kinase Czeta activation play an essential role in palmitate-induced insulin resistance in rat L6 skeletal muscle cells
    • 10.1042/BJ20040139 15193147
    • Intracellular ceramide synthesis and protein kinase Czeta activation play an essential role in palmitate-induced insulin resistance in rat L6 skeletal muscle cells. Powell DJ, Turban S, Gray A, Hajduch E, Hundal HS, Biochem J 2004 382 619 629 10.1042/BJ20040139 15193147
    • (2004) Biochem J , vol.382 , pp. 619-629
    • Powell, D.J.1    Turban, S.2    Gray, A.3    Hajduch, E.4    Hundal, H.S.5
  • 95
    • 14644445144 scopus 로고    scopus 로고
    • A role for sphingolipids in producing the common features of type 2 diabetes, metabolic syndrome X, and Cushing's syndrome
    • 10.2337/diabetes.54.3.591 15734832
    • A role for sphingolipids in producing the common features of type 2 diabetes, metabolic syndrome X, and Cushing's syndrome. Summers SA, Nelson DH, Diabetes 2005 54 591 602 10.2337/diabetes.54.3.591 15734832
    • (2005) Diabetes , vol.54 , pp. 591-602
    • Summers, S.A.1    Nelson, D.H.2
  • 96
    • 0031841949 scopus 로고    scopus 로고
    • Regulation of insulin-stimulated glucose transporter GLUT4 translocation and Akt kinase activity by ceramide
    • Regulation of insulin-stimulated glucose transporter GLUT4 translocation and Akt kinase activity by ceramide. Summers SA, Garza LA, Zhou H, Birnbaum MJ, Mol Cell Bio 1998 18 5457 5464
    • (1998) Mol Cell Bio , vol.18 , pp. 5457-5464
    • Summers, S.A.1    Garza, L.A.2    Zhou, H.3    Birnbaum, M.J.4
  • 97
    • 0031964986 scopus 로고    scopus 로고
    • Effects of cell-permeable ceramides and tumor necrosis factor-alpha on insulin signaling and glucose uptake in 3T3-L1 adipocytes
    • 10.2337/diabetes.47.1.24 9421370
    • Effects of cell-permeable ceramides and tumor necrosis factor-alpha on insulin signaling and glucose uptake in 3T3-L1 adipocytes. Wang CN, O'Brien L, Brindley DN, Diabetes 1998 47 24 31 10.2337/diabetes.47.1.24 9421370
    • (1998) Diabetes , vol.47 , pp. 24-31
    • Wang, C.N.1    O'Brien, L.2    Brindley, D.N.3
  • 98
    • 0030886025 scopus 로고    scopus 로고
    • Fatty acid-induced insulin resistance in adipocytes
    • 10.1210/en.138.10.4338 9322948
    • Fatty acid-induced insulin resistance in adipocytes. Van Epps-Fung M, Williford J, Wells A, Hardy RW, Endocrinology 1997 138 4338 4345 10.1210/en.138.10.4338 9322948
    • (1997) Endocrinology , vol.138 , pp. 4338-4345
    • Van Epps-Fung, M.1    Williford, J.2    Wells, A.3    Hardy, R.W.4
  • 100
    • 59849098608 scopus 로고    scopus 로고
    • Modulating serine palmitoyl transferase (SPT) expression and activity unveils a crucial role in lipid-induced insulin resistance in rat skeletal muscle cells
    • 10.1042/BJ20081149 18922131
    • Modulating serine palmitoyl transferase (SPT) expression and activity unveils a crucial role in lipid-induced insulin resistance in rat skeletal muscle cells. Watson ML, Coghlan M, Hundal HS, Biochem J 2009 417 791 801 10.1042/BJ20081149 18922131
    • (2009) Biochem J , vol.417 , pp. 791-801
    • Watson, M.L.1    Coghlan, M.2    Hundal, H.S.3
  • 101
    • 79955758735 scopus 로고    scopus 로고
    • Differential regulation of dihydroceramide desaturase by palmitate versus monounsaturated fatty acids: Implications for insulin resistance
    • 10.1074/jbc.M110.186916 21454530
    • Differential regulation of dihydroceramide desaturase by palmitate versus monounsaturated fatty acids: implications for insulin resistance. Hu W, Ross J, Geng T, Brice SE, Cowart LA, J Biol Chem 2011 286 16596 16605 10.1074/jbc.M110.186916 21454530
    • (2011) J Biol Chem , vol.286 , pp. 16596-16605
    • Hu, W.1    Ross, J.2    Geng, T.3    Brice, S.E.4    Cowart, L.A.5
  • 102
    • 0037261135 scopus 로고    scopus 로고
    • Cell-permeable ceramides increase basal glucose incorporation into triacylglycerols but decrease the stimulation by insulin in 3T3-L1 adipocytes
    • 10.1038/sj.ijo.0802183 12532151
    • Cell-permeable ceramides increase basal glucose incorporation into triacylglycerols but decrease the stimulation by insulin in 3T3-L1 adipocytes. Mei J, Wang CN, O'Brien L, Brindley DN, Int J Obes Relat Metab Disord 2003 27 31 39 10.1038/sj.ijo.0802183 12532151
    • (2003) Int J Obes Relat Metab Disord , vol.27 , pp. 31-39
    • Mei, J.1    Wang, C.N.2    O'Brien, L.3    Brindley, D.N.4
  • 103
    • 77956040410 scopus 로고    scopus 로고
    • Saturated- and n-6 polyunsaturated-fat diets each induce ceramide accumulation in mouse skeletal muscle: Reversal and improvement of glucose tolerance by lipid metabolism inhibitors
    • 10.1210/en.2010-0250 20660065
    • Saturated- and n-6 polyunsaturated-fat diets each induce ceramide accumulation in mouse skeletal muscle: reversal and improvement of glucose tolerance by lipid metabolism inhibitors. Frangioudakis G, Garrard J, Raddatz K, Nadler JL, Mitchell TW, Schmitz-Peiffer C, Endocrinology 2010 151 4187 4196 10.1210/en.2010-0250 20660065
    • (2010) Endocrinology , vol.151 , pp. 4187-4196
    • Frangioudakis, G.1    Garrard, J.2    Raddatz, K.3    Nadler, J.L.4    Mitchell, T.W.5    Schmitz-Peiffer, C.6
  • 104
    • 67650096801 scopus 로고    scopus 로고
    • Central role of ceramide biosynthesis in body weight regulation, energy metabolism, and the metabolic syndrome
    • 10.1152/ajpendo.91014.2008 19435851
    • Central role of ceramide biosynthesis in body weight regulation, energy metabolism, and the metabolic syndrome. Yang G, Badeanlou L, Bielawski J, Roberts AJ, Hannun YA, Samad F, Am J Physiol Endocrinol Metab 2009 297 211 E224 10.1152/ajpendo.91014.2008 19435851
    • (2009) Am J Physiol Endocrinol Metab , vol.297
    • Yang, G.1    Badeanlou, L.2    Bielawski, J.3    Roberts, A.J.4    Hannun, Y.A.5    Samad, F.6
  • 106
    • 0036300538 scopus 로고    scopus 로고
    • Lipid-induced insulin resistance in human muscle is associated with changes in diacylglycerol, protein kinase C, and IkappaB-alpha
    • 10.2337/diabetes.51.7.2005 12086926
    • Lipid-induced insulin resistance in human muscle is associated with changes in diacylglycerol, protein kinase C, and IkappaB-alpha. Itani SI, Ruderman NB, Schmieder F, Boden G, Diabetes 2002 51 2005 2011 10.2337/diabetes.51.7.2005 12086926
    • (2002) Diabetes , vol.51 , pp. 2005-2011
    • Itani, S.I.1    Ruderman, N.B.2    Schmieder, F.3    Boden, G.4
  • 110
    • 77957327998 scopus 로고    scopus 로고
    • Role of PUFAs, the precursors of endocannabinoids, in human obesity and type 2 diabetes
    • Role of PUFAs, the precursors of endocannabinoids, in human obesity and type 2 diabetes. Dain A, Repossi G, Das UN, Eynard AR, Front Biosci (Elite Ed) 2010 2 1432 1447
    • (2010) Front Biosci (Elite Ed) , vol.2 , pp. 1432-1447
    • Dain, A.1    Repossi, G.2    Das, U.N.3    Eynard, A.R.4
  • 111
    • 48149101434 scopus 로고    scopus 로고
    • The endocannabinoid system in obesity and type 2 diabetes
    • 10.1007/s00125-008-1048-2 18563385
    • The endocannabinoid system in obesity and type 2 diabetes. Di Marzo V, Diabetologia 2008 51 1356 1367 10.1007/s00125-008-1048-2 18563385
    • (2008) Diabetologia , vol.51 , pp. 1356-1367
    • Di Marzo, V.1
  • 113
    • 79960837542 scopus 로고    scopus 로고
    • Eicosanoids, β-cell function, and diabetes
    • 10.1016/j.prostaglandins.2011.06.001 21757024
    • Eicosanoids, β-cell function, and diabetes. Luo P, Wang MH, Prostaglandins Other Lipid Mediat 2011 95 1 4 10.1016/j.prostaglandins.2011.06. 001 21757024
    • (2011) Prostaglandins Other Lipid Mediat , vol.95 , pp. 1-4
    • Luo, P.1    Wang, M.H.2
  • 114
    • 84867867477 scopus 로고    scopus 로고
    • The nuclear factor kappa B signaling pathway: Integrating metabolism with inflammation
    • 10.1016/j.tcb.2012.08.001 22995730
    • The nuclear factor kappa B signaling pathway: integrating metabolism with inflammation. Tornatore L, Thotakura AK, Bennett J, Moretti M, Franzoso G, Trends Cell Biol 2012 22 557 566 10.1016/j.tcb.2012.08.001 22995730
    • (2012) Trends Cell Biol , vol.22 , pp. 557-566
    • Tornatore, L.1    Thotakura, A.K.2    Bennett, J.3    Moretti, M.4    Franzoso, G.5
  • 115
    • 77955806634 scopus 로고    scopus 로고
    • JNK1 and IKKβ: Molecular links between obesity and metabolic dysfunction
    • 10.1096/fj.09-151340 20371626
    • JNK1 and IKKβ: molecular links between obesity and metabolic dysfunction. Solinas G, Karin M, FASEB J 2010 24 2596 2611 10.1096/fj.09-151340 20371626
    • (2010) FASEB J , vol.24 , pp. 2596-2611
    • Solinas, G.1    Karin, M.2
  • 116
    • 0028050242 scopus 로고
    • Ceramide mediates the apoptotic response of WEHI 231 cells to anti-immunoglobulin, corticosteroids and irradiation
    • 10.1006/bbrc.1994.1988 8048941
    • Ceramide mediates the apoptotic response of WEHI 231 cells to anti-immunoglobulin, corticosteroids and irradiation. Quintans J, Kilkus J, McShan CL, Gottschalk AR, Dawson G, Biochem Biophys Res Commun 1994 202 710 714 10.1006/bbrc.1994.1988 8048941
    • (1994) Biochem Biophys Res Commun , vol.202 , pp. 710-714
    • Quintans, J.1    Kilkus, J.2    McShan, C.L.3    Gottschalk, A.R.4    Dawson, G.5
  • 117
    • 0035212942 scopus 로고    scopus 로고
    • Regulation of de novo sphingolipid biosynthesis and the toxic consequences of its disruption
    • 10.1042/BST0290831 11709083
    • Regulation of de novo sphingolipid biosynthesis and the toxic consequences of its disruption. Linn SC, Kim HS, Keane EM, Andras LM, Wang E, Merrill AH Jr, Biochem Soc Trans 2001 29 831 835 10.1042/BST0290831 11709083
    • (2001) Biochem Soc Trans , vol.29 , pp. 831-835
    • Linn, S.C.1    Kim, H.S.2    Keane, E.M.3    Andras, L.M.4    Wang, E.5    Merrill Jr., A.H.6
  • 118
    • 0036959692 scopus 로고    scopus 로고
    • Involvement of sphingosine in dexamethasone-induced thymocyte apoptosis
    • 10.1111/j.1749-6632.2002.tb04631.x 12485859
    • Involvement of sphingosine in dexamethasone-induced thymocyte apoptosis. Lepine S, Lakatos B, Maziere P, Courageot MP, Sulpice JC, Giraud F, Ann N Y Acad Sci 2002 973 190 193 10.1111/j.1749-6632.2002.tb04631.x 12485859
    • (2002) Ann N y Acad Sci , vol.973 , pp. 190-193
    • Lepine, S.1    Lakatos, B.2    Maziere, P.3    Courageot, M.P.4    Sulpice, J.C.5    Giraud, F.6
  • 119
    • 33846452968 scopus 로고    scopus 로고
    • Pioglitazone induces de novo ceramide synthesis in the rat heart
    • 10.1016/j.prostaglandins.2006.10.004
    • Pioglitazone induces de novo ceramide synthesis in the rat heart. Baranowski M, Blachnio A, Zabielski P, Gorski J, Prostaglandins Lipid Mediat 2007 83 99 111 10.1016/j.prostaglandins.2006.10.004
    • (2007) Prostaglandins Lipid Mediat , vol.83 , pp. 99-111
    • Baranowski, M.1    Blachnio, A.2    Zabielski, P.3    Gorski, J.4
  • 120
    • 0037417725 scopus 로고    scopus 로고
    • A critical role for PPARalpha-mediated lipotoxicity in the pathogenesis of diabetic cardiomyopathy: Modulation by dietary fat content
    • 10.1073/pnas.0336724100 12552126
    • A critical role for PPARalpha-mediated lipotoxicity in the pathogenesis of diabetic cardiomyopathy: modulation by dietary fat content. Finck BN, Han X, Courtois M, Aimond F, Nerbonne JM, Kovacs A, Gross RW, Kelly DP, Proc Natl Acad Sci USA 2003 100 1226 1231 10.1073/pnas.0336724100 12552126
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1226-1231
    • Finck, B.N.1    Han, X.2    Courtois, M.3    Aimond, F.4    Nerbonne, J.M.5    Kovacs, A.6    Gross, R.W.7    Kelly, D.P.8
  • 121
    • 0036255529 scopus 로고    scopus 로고
    • The mode of action of thiazolidinediones
    • 10.1002/dmrr.249 11921433
    • The mode of action of thiazolidinediones. Hauner H, Diabetes Metab Res Rev 2002 18 10 S15 10.1002/dmrr.249 11921433
    • (2002) Diabetes Metab Res Rev , vol.18
    • Hauner, H.1
  • 122
    • 34047276087 scopus 로고    scopus 로고
    • Effects of pioglitazone and high-fat diet on ceramide metabolism in rat skeletal muscles
    • 17242494
    • Effects of pioglitazone and high-fat diet on ceramide metabolism in rat skeletal muscles. Zendzian-Piotrowska M, Baranowski M, Zabielski P, Gorski J, J Physiol Pharmacol 2006 57 101 114 17242494
    • (2006) J Physiol Pharmacol , vol.57 , pp. 101-114
    • Zendzian-Piotrowska, M.1    Baranowski, M.2    Zabielski, P.3    Gorski, J.4
  • 123
    • 15744365009 scopus 로고    scopus 로고
    • Increased Akt protein expression is associated with decreased ceramide content in skeletal muscle of troglitazone-treated mice
    • 10.1016/j.bcp.2005.01.015 15794940
    • Increased Akt protein expression is associated with decreased ceramide content in skeletal muscle of troglitazone-treated mice. Planavila A, Alegret M, Sanchez RM, Rodriguez-Calvo R, Laguna JC, Vazquez-Carrera M, Biochem Pharmacol 2005 69 1195 1204 10.1016/j.bcp.2005.01.015 15794940
    • (2005) Biochem Pharmacol , vol.69 , pp. 1195-1204
    • Planavila, A.1    Alegret, M.2    Sanchez, R.M.3    Rodriguez-Calvo, R.4    Laguna, J.C.5    Vazquez-Carrera, M.6
  • 124
    • 9444230624 scopus 로고    scopus 로고
    • Rosiglitazone enhances glucose tolerance by mechanisms other than reduction of fatty acid accumulation within skeletal muscle
    • 10.1210/en.2004-0659 15375026
    • Rosiglitazone enhances glucose tolerance by mechanisms other than reduction of fatty acid accumulation within skeletal muscle. Lessard SJ, Lo Giudice SL, Lau W, Reid JJ, Turner N, Febbraio MA, Hawley JA, Watt MJ, Endocrinology 2004 145 5665 5670 10.1210/en.2004-0659 15375026
    • (2004) Endocrinology , vol.145 , pp. 5665-5670
    • Lessard, S.J.1    Lo Giudice, S.L.2    Lau, W.3    Reid, J.J.4    Turner, N.5    Febbraio, M.A.6    Hawley, J.A.7    Watt, M.J.8
  • 125
    • 34347208708 scopus 로고    scopus 로고
    • Serum retinol-binding protein: A link between obesity, insulin resistance, and type 2 diabetes
    • 10.1111/j.1753-4887.2007.tb00302.x 17566551
    • Serum retinol-binding protein: a link between obesity, insulin resistance, and type 2 diabetes. Wolf G, Nutr Rev 2007 65 251 256 10.1111/j.1753-4887.2007.tb00302.x 17566551
    • (2007) Nutr Rev , vol.65 , pp. 251-256
    • Wolf, G.1
  • 127
    • 3142624494 scopus 로고    scopus 로고
    • Effect of endurance training on the sphingomyelin-signalling pathway activity in the skeletal muscles of the rat
    • 15213354
    • Effect of endurance training on the sphingomyelin-signalling pathway activity in the skeletal muscles of the rat. Dobrzyn A, Zendzian-Piotrowska M, Gorski J, J Physiol Pharmacol 2004 55 305 313 15213354
    • (2004) J Physiol Pharmacol , vol.55 , pp. 305-313
    • Dobrzyn, A.1    Zendzian-Piotrowska, M.2    Gorski, J.3
  • 128
    • 34547131281 scopus 로고    scopus 로고
    • Metformin and exercise reduce muscle FAT/CD36 and lipid accumulation and blunt the progression of high-fat diet-induced hyperglycemia
    • 10.1152/ajpendo.00677.2006 17374701
    • Metformin and exercise reduce muscle FAT/CD36 and lipid accumulation and blunt the progression of high-fat diet-induced hyperglycemia. Smith AC, Mullen KL, Junkin KA, Nickerson J, Chabowski A, Bonen A, Dyck DJ, Am J Physiol Endocrinol Metab 2007 293 172 E181 10.1152/ajpendo.00677.2006 17374701
    • (2007) Am J Physiol Endocrinol Metab , vol.293
    • Smith, A.C.1    Mullen, K.L.2    Junkin, K.A.3    Nickerson, J.4    Chabowski, A.5    Bonen, A.6    Dyck, D.J.7
  • 129
    • 45549084515 scopus 로고    scopus 로고
    • Exercise-induced alterations in intramyocellular lipids and insulin resistance: The athlete's paradox revisited
    • 10.1152/ajpendo.00769.2007 18319352
    • Exercise-induced alterations in intramyocellular lipids and insulin resistance: the athlete's paradox revisited. Dube JJ, Amati F, Stefanovic-Racic M, Toledo FG, Sauers SE, Goodpaster BH, Am J Physiol Endocrinol Metab 2008 294 882 E888 10.1152/ajpendo.00769.2007 18319352
    • (2008) Am J Physiol Endocrinol Metab , vol.294
    • Dube, J.J.1    Amati, F.2    Stefanovic-Racic, M.3    Toledo, F.G.4    Sauers, S.E.5    Goodpaster, B.H.6
  • 130
    • 33745841299 scopus 로고    scopus 로고
    • Endurance training in obese humans improves glucose tolerance and mitochondrial fatty acid oxidation and alters muscle lipid content
    • 10.1152/ajpendo.00587.2005 16464906
    • Endurance training in obese humans improves glucose tolerance and mitochondrial fatty acid oxidation and alters muscle lipid content. Bruce CR, Thrush AB, Mertz VA, Bezaire V, Chabowski A, Heigenhauser GJ, Dyck DJ, Am J Physiol Endocrinol Metab 2006 291 99 E107 10.1152/ajpendo.00587.2005 16464906
    • (2006) Am J Physiol Endocrinol Metab , vol.291
    • Bruce, C.R.1    Thrush, A.B.2    Mertz, V.A.3    Bezaire, V.4    Chabowski, A.5    Heigenhauser, G.J.6    Dyck, D.J.7
  • 131
  • 132
    • 1642503772 scopus 로고    scopus 로고
    • Exercise and training effects on ceramide metabolism in human skeletal muscle
    • 10.1113/expphysiol.2003.002605 15109217
    • Exercise and training effects on ceramide metabolism in human skeletal muscle. Helge JW, Dobrzyn A, Saltin B, Gorski J, Exp Physiol 2004 89 119 127 10.1113/expphysiol.2003.002605 15109217
    • (2004) Exp Physiol , vol.89 , pp. 119-127
    • Helge, J.W.1    Dobrzyn, A.2    Saltin, B.3    Gorski, J.4
  • 133
    • 0348222671 scopus 로고    scopus 로고
    • Inflammation: The link between insulin resistance, obesity and diabetes
    • 10.1016/j.it.2003.10.013 14698276
    • Inflammation: the link between insulin resistance, obesity and diabetes. Dandona P, Aljada A, Bandyopadhyay A, Trends Immunol 2004 25 4 7 10.1016/j.it.2003.10.013 14698276
    • (2004) Trends Immunol , vol.25 , pp. 4-7
    • Dandona, P.1    Aljada, A.2    Bandyopadhyay, A.3
  • 134
    • 3042618753 scopus 로고    scopus 로고
    • Serum tumor necrosis factor-alpha levels and components of the metabolic syndrome in obese adolescents
    • 10.1016/j.metabol.2004.02.007 15254878
    • Serum tumor necrosis factor-alpha levels and components of the metabolic syndrome in obese adolescents. Moon YS, Kim DH, Song DK, Metabolism 2004 53 863 867 10.1016/j.metabol.2004.02.007 15254878
    • (2004) Metabolism , vol.53 , pp. 863-867
    • Moon, Y.S.1    Kim, D.H.2    Song, D.K.3
  • 135
    • 41249098290 scopus 로고    scopus 로고
    • Aging up-regulates expression of inflammatory mediators in mouse adipose tissue
    • 17878382
    • Aging up-regulates expression of inflammatory mediators in mouse adipose tissue. Wu D, Ren Z, Pae M, Guo W, Cui X, Merrill AH, Meydani SN, J Immunol 2007 179 4829 4839 17878382
    • (2007) J Immunol , vol.179 , pp. 4829-4839
    • Wu, D.1    Ren, Z.2    Pae, M.3    Guo, W.4    Cui, X.5    Merrill, A.H.6    Meydani, S.N.7
  • 136
    • 0029874429 scopus 로고    scopus 로고
    • Sphingomyelinase and ceramide suppress insulin-induced tyrosine phosphorylation of the insulin receptor substrate-1
    • 10.1074/jbc.271.17.9895 8626623
    • Sphingomyelinase and ceramide suppress insulin-induced tyrosine phosphorylation of the insulin receptor substrate-1. Kanety H, Hemi R, Papa MZ, Karasik A, J Biol Chem 1996 271 9895 9897 10.1074/jbc.271.17.9895 8626623
    • (1996) J Biol Chem , vol.271 , pp. 9895-9897
    • Kanety, H.1    Hemi, R.2    Papa, M.Z.3    Karasik, A.4
  • 137
    • 0030669392 scopus 로고    scopus 로고
    • A molecular basis for insulin resistance. Elevated serine/threonine phosphorylation of IRS-1 and IRS-2 inhibitstheir binding to the juxtamembrane region of the insulin receptor and impairs their ability to undergo insulin-induced tyrosine phosphorylation
    • 10.1074/jbc.272.47.29911 9368067
    • A molecular basis for insulin resistance. Elevated serine/threonine phosphorylation of IRS-1 and IRS-2 inhibitstheir binding to the juxtamembrane region of the insulin receptor and impairs their ability to undergo insulin-induced tyrosine phosphorylation. Paz K, Hemi R, LeRoith D, Karasik A, Elhanany E, Kanety H, Zick Y, J Biol Chem 1997 272 29911 29918 10.1074/jbc.272.47.29911 9368067
    • (1997) J Biol Chem , vol.272 , pp. 29911-29918
    • Paz, K.1    Hemi, R.2    Leroith, D.3    Karasik, A.4    Elhanany, E.5    Kanety, H.6    Zick, Y.7
  • 138
    • 0036924048 scopus 로고    scopus 로고
    • Activation of the Drosophila MLK by ceramide reveals TNF-alpha and ceramide as agonists of mammalian MLK3
    • 10.1016/S1097-2765(02)00734-7 12504027
    • Activation of the Drosophila MLK by ceramide reveals TNF-alpha and ceramide as agonists of mammalian MLK3. Sathyanarayana P, Barthwal MK, Kundu CN, Lane ME, Bergmann A, Tzivion G, Rana A, Mol Cell 2002 10 1527 1533 10.1016/S1097-2765(02)00734-7 12504027
    • (2002) Mol Cell , vol.10 , pp. 1527-1533
    • Sathyanarayana, P.1    Barthwal, M.K.2    Kundu, C.N.3    Lane, M.E.4    Bergmann, A.5    Tzivion, G.6    Rana, A.7
  • 139
    • 0034954603 scopus 로고    scopus 로고
    • The MLK family mediates c-Jun N-terminal kinase activation in neuronal apoptosis
    • 10.1128/MCB.21.14.4713-4724.2001 11416147
    • The MLK family mediates c-Jun N-terminal kinase activation in neuronal apoptosis. Xu Z, Maroney AC, Dobrzanski P, Kukekov NV, Greene LA, Mol Cell Biol 2001 21 4713 4724 10.1128/MCB.21.14.4713-4724.2001 11416147
    • (2001) Mol Cell Biol , vol.21 , pp. 4713-4724
    • Xu, Z.1    Maroney, A.C.2    Dobrzanski, P.3    Kukekov, N.V.4    Greene, L.A.5
  • 140
    • 3142741044 scopus 로고    scopus 로고
    • Mixed lineage kinase 3 (MLK3)-activated p38 MAP kinase mediates transforming growth factor-beta-induced apoptosis in hepatoma cells
    • 10.1074/jbc.M313947200 15069087
    • Mixed lineage kinase 3 (MLK3)-activated p38 MAP kinase mediates transforming growth factor-beta-induced apoptosis in hepatoma cells. Kim KY, Kim BC, Xu Z, Kim SJ, J Biol Chem 2004 279 29478 29484 10.1074/jbc.M313947200 15069087
    • (2004) J Biol Chem , vol.279 , pp. 29478-29484
    • Kim, K.Y.1    Kim, B.C.2    Xu, Z.3    Kim, S.J.4
  • 141
    • 0034708832 scopus 로고    scopus 로고
    • The c-Jun NH(2)-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser(307)
    • 10.1074/jbc.275.12.9047 10722755
    • The c-Jun NH(2)-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser(307). Aguirre V, Uchida T, Yenush L, Davis R, White MF, J Biol Chem 2000 275 9047 9054 10.1074/jbc.275.12.9047 10722755
    • (2000) J Biol Chem , vol.275 , pp. 9047-9054
    • Aguirre, V.1    Uchida, T.2    Yenush, L.3    Davis, R.4    White, M.F.5
  • 143
    • 14544271905 scopus 로고    scopus 로고
    • Marchand-Brustel, J.F. Tanti, Positive and negative regulation of insulin signaling through IRS-1 phosphorylation
    • 10.1016/j.biochi.2004.10.019 15733744
    • Marchand-Brustel, J.F. Tanti, Positive and negative regulation of insulin signaling through IRS-1 phosphorylation. Gual P, Le Y, Biochimie 2005 87 99 109 10.1016/j.biochi.2004.10.019 15733744
    • (2005) Biochimie , vol.87 , pp. 99-109
    • Gual, P.1    Le, Y.2
  • 145
    • 0342980927 scopus 로고    scopus 로고
    • Inhibition of PKB/Akt1 by C2-ceramide involves activation of
    • 10.1006/mcne.1999.0813 10673324
    • Inhibition of PKB/Akt1 by C2-ceramide involves activation of ceramide-activated protein phosphatase in PC12 cells. Salinas M, Lopez-Valdaliso R, Martin D, Alvarez A, Cuadrado A, Mol Cell Neurosci 2000 15 156 169 10.1006/mcne.1999.0813 10673324
    • (2000) Mol Cell Neurosci , vol.15 , pp. 156-169
    • Salinas, M.1    Lopez-Valdaliso, R.2    Martin, D.3    Alvarez, A.4    Cuadrado, A.5
  • 146
    • 0034607914 scopus 로고    scopus 로고
    • Ceramide inhibits protein kinase B/Akt by promoting dephosphorylation of serine 473
    • 10.1074/jbc.275.18.13330 10788440
    • Ceramide inhibits protein kinase B/Akt by promoting dephosphorylation of serine 473. Schubert KM, Scheid MP, Duronio V, J Biol Chem 2000 275 13330 13335 10.1074/jbc.275.18.13330 10788440
    • (2000) J Biol Chem , vol.275 , pp. 13330-13335
    • Schubert, K.M.1    Scheid, M.P.2    Duronio, V.3
  • 147
    • 0035281991 scopus 로고    scopus 로고
    • Ceramide dissociates 3′-phosphoinositide production from pleckstrin homology domain translocation
    • 10.1042/0264-6021:3540359 11171115
    • Ceramide dissociates 3′-phosphoinositide production from pleckstrin homology domain translocation. Stratford S, DeWald DB, Summers SA, Biochem J 2001 354 359 368 10.1042/0264-6021:3540359 11171115
    • (2001) Biochem J , vol.354 , pp. 359-368
    • Stratford, S.1    Dewald, D.B.2    Summers, S.A.3
  • 148
    • 0032128301 scopus 로고    scopus 로고
    • Inhibition of the anti-apoptotic PI(3)K/Akt/Bad pathway by stress
    • 10.1101/gad.12.13.1941 9649498
    • Inhibition of the anti-apoptotic PI(3)K/Akt/Bad pathway by stress. Zundel W, Giaccia A, Genes Dev 1998 12 1941 1946 10.1101/gad.12.13.1941 9649498
    • (1998) Genes Dev , vol.12 , pp. 1941-1946
    • Zundel, W.1    Giaccia, A.2
  • 149
    • 0035513703 scopus 로고    scopus 로고
    • Ceramide mediates insulin resistance by tumor necrosis factor-alpha in brown adipocytes by maintaining Akt in an inactive dephosphorylated state
    • 10.2337/diabetes.50.11.2563 11679435
    • Ceramide mediates insulin resistance by tumor necrosis factor-alpha in brown adipocytes by maintaining Akt in an inactive dephosphorylated state. Teruel T, Hernandez R, Lorenzo M, Diabetes 2001 50 2563 2571 10.2337/diabetes.50.11.2563 11679435
    • (2001) Diabetes , vol.50 , pp. 2563-2571
    • Teruel, T.1    Hernandez, R.2    Lorenzo, M.3
  • 150
    • 0034816711 scopus 로고    scopus 로고
    • Ceramide induces the dephosphorylation and inhibition of constitutively activated Akt in PTEN negative U87MG cells
    • 10.1006/bbrc.2000.4248 11162641
    • Ceramide induces the dephosphorylation and inhibition of constitutively activated Akt in PTEN negative U87MG cells. Zinda MJ, Vlahos CJ, Lai MT, Biochem Biophys Res Commun 2001 280 1107 1115 10.1006/bbrc.2000.4248 11162641
    • (2001) Biochem Biophys Res Commun , vol.280 , pp. 1107-1115
    • Zinda, M.J.1    Vlahos, C.J.2    Lai, M.T.3
  • 151
    • 0036479251 scopus 로고    scopus 로고
    • Ceramide-induced inhibition of Akt is mediated through protein kinase Czeta: Implications for growth arrest
    • 10.1074/jbc.M110541200 11723139
    • Ceramide-induced inhibition of Akt is mediated through protein kinase Czeta: implications for growth arrest. Bourbon NA, Sandirasegarane L, Kester M, J Biol Chem 2002 277 3286 3292 10.1074/jbc.M110541200 11723139
    • (2002) J Biol Chem , vol.277 , pp. 3286-3292
    • Bourbon, N.A.1    Sandirasegarane, L.2    Kester, M.3
  • 152
    • 0142091454 scopus 로고    scopus 로고
    • Ceramide disables 3-phosphoinositide binding to the pleckstrin homology domain of protein kinase B (PKB)/Akt by a PKCzeta-dependent mechanism
    • 10.1128/MCB.23.21.7794-7808.2003 14560023
    • Ceramide disables 3-phosphoinositide binding to the pleckstrin homology domain of protein kinase B (PKB)/Akt by a PKCzeta-dependent mechanism. Powell DJ, Hajduch E, Kular G, Hundal HS, Mol Cell Biol 2003 23 7794 7808 10.1128/MCB.23.21.7794-7808.2003 14560023
    • (2003) Mol Cell Biol , vol.23 , pp. 7794-7808
    • Powell, D.J.1    Hajduch, E.2    Kular, G.3    Hundal, H.S.4
  • 153
    • 40449097575 scopus 로고    scopus 로고
    • Targeting of PKCzeta and PKB to caveolin-enriched microdomains represents a crucial step underpinning the disruption in PKB-directed signalling by ceramide
    • 10.1042/BJ20070936 17983354
    • Targeting of PKCzeta and PKB to caveolin-enriched microdomains represents a crucial step underpinning the disruption in PKB-directed signalling by ceramide. Hajduch E, Turban S, Le Liepvre X, Le Lay S, Lipina C, Dimopoulos N, Dugail I, Hundal HS, Biochem J 2008 410 369 379 10.1042/BJ20070936 17983354
    • (2008) Biochem J , vol.410 , pp. 369-379
    • Hajduch, E.1    Turban, S.2    Le Liepvre, X.3    Le Lay, S.4    Lipina, C.5    Dimopoulos, N.6    Dugail, I.7    Hundal, H.S.8
  • 154
    • 84862798795 scopus 로고    scopus 로고
    • Lipid raft: A floating island of death or survival
    • 10.1016/j.taap.2012.01.007 22289360
    • Lipid raft: a floating island of death or survival. George KS, Wu S, Toxicol Appl Pharmacol 2012 259 311 319 10.1016/j.taap.2012.01.007 22289360
    • (2012) Toxicol Appl Pharmacol , vol.259 , pp. 311-319
    • George, K.S.1    Wu, S.2
  • 155
    • 58149204290 scopus 로고    scopus 로고
    • Ceramide-enriched membrane domains-structure and function
    • 10.1016/j.bbamem.2008.07.030 18786504
    • Ceramide-enriched membrane domains-structure and function. Zhang Y, Li X, Becker KA, Gulbins E, Biochim Biophys Acta 2009 1788 178 183 10.1016/j.bbamem.2008.07.030 18786504
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 178-183
    • Zhang, Y.1    Li, X.2    Becker, K.A.3    Gulbins, E.4
  • 156
    • 34250742501 scopus 로고    scopus 로고
    • Biological aspects of ceramide-enriched membrane domains
    • 10.1016/j.plipres.2007.03.002 17490747
    • Biological aspects of ceramide-enriched membrane domains. Grassme H, Riethmuller J, Gulbins E, Prog Lipid Res 2007 46 161 170 10.1016/j.plipres.2007. 03.002 17490747
    • (2007) Prog Lipid Res , vol.46 , pp. 161-170
    • Grassme, H.1    Riethmuller, J.2    Gulbins, E.3
  • 158
    • 0036195136 scopus 로고    scopus 로고
    • An essential role for membrane rafts in the initiation of Fas/CD95-triggered cell death in mouse thymocytes
    • 10.1093/embo-reports/kvf022 11818332
    • An essential role for membrane rafts in the initiation of Fas/CD95-triggered cell death in mouse thymocytes. Hueber AO, Bernard AM, Herincs Z, Couzinet A, He HT, EMBO Rep 2002 3 190 196 10.1093/embo-reports/ kvf022 11818332
    • (2002) EMBO Rep , vol.3 , pp. 190-196
    • Hueber, A.O.1    Bernard, A.M.2    Herincs, Z.3    Couzinet, A.4    He, H.T.5
  • 159
    • 84859786953 scopus 로고    scopus 로고
    • Caveolins and caveolae, roles in insulin signalling and diabetes
    • 10.1007/978-1-4614-1222-9-8 22411317
    • Caveolins and caveolae, roles in insulin signalling and diabetes. Stralfors P, Adv Exp Med Biol 2012 729 111 126 10.1007/978-1-4614-1222-9-8 22411317
    • (2012) Adv Exp Med Biol , vol.729 , pp. 111-126
    • Stralfors, P.1
  • 160
    • 24744459879 scopus 로고    scopus 로고
    • Ceramide regulation of the tumor suppressor phosphatase PTEN in rafts isolated from neurotumor cell lines
    • 10.1002/jnr.20550 15968641
    • Ceramide regulation of the tumor suppressor phosphatase PTEN in rafts isolated from neurotumor cell lines. Goswami R, Singh D, Phillips G, Kilkus J, Dawson G, J Neurosci Res 2005 81 541 550 10.1002/jnr.20550 15968641
    • (2005) J Neurosci Res , vol.81 , pp. 541-550
    • Goswami, R.1    Singh, D.2    Phillips, G.3    Kilkus, J.4    Dawson, G.5
  • 161
    • 79959746261 scopus 로고    scopus 로고
    • Sphingolipids: Agents provocateurs in the pathogenesis of insulin resistance
    • 10.1007/s00125-011-2127-3 21468641
    • Sphingolipids: agents provocateurs in the pathogenesis of insulin resistance. Lipina C, Hundal HS, Diabetologia 2011 54 1596 1607 10.1007/s00125-011-2127-3 21468641
    • (2011) Diabetologia , vol.54 , pp. 1596-1607
    • Lipina, C.1    Hundal, H.S.2
  • 162
    • 0035145780 scopus 로고    scopus 로고
    • Lipotoxicity of the pancreatic beta-cell is associated with glucose-dependent esterification of fatty acids into neutral lipids
    • 10.2337/diabetes.50.2.315 11272142
    • 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, Diabetes 2001 50 315 321 10.2337/diabetes.50.2.315 11272142
    • (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
  • 163
    • 0042531617 scopus 로고    scopus 로고
    • Palmitate inhibition of insulin gene expression is mediated at the transcriptional level via ceramide synthesis
    • 10.1074/jbc.M302548200 12771145
    • 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, Poitout V, J Biol Chem 2003 278 30015 30021 10.1074/jbc.M302548200 12771145
    • (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
  • 164
    • 77951295434 scopus 로고    scopus 로고
    • Blockage of ceramide metabolism exacerbates palmitate inhibition of pro-insulin gene expression in pancreatic beta-cells
    • 10.1007/s11010-009-0362-4 20063116
    • Blockage of ceramide metabolism exacerbates palmitate inhibition of pro-insulin gene expression in pancreatic beta-cells. Guo J, Qian Y, Xi X, Hu X, Zhu J, Han X, Mol Cell Biochem 2010 338 283 290 10.1007/s11010-009-0362-4 20063116
    • (2010) Mol Cell Biochem , vol.338 , pp. 283-290
    • Guo, J.1    Qian, Y.2    Xi, X.3    Hu, X.4    Zhu, J.5    Han, X.6
  • 165
    • 0028174029 scopus 로고
    • C-jun inhibits transcriptional activation by the insulin enhancer, and the insulin control element is the target of control
    • 8264634
    • c-jun inhibits transcriptional activation by the insulin enhancer, and the insulin control element is the target of control. Henderson E, Stein R, Mol Cell Biol 1994 14 655 662 8264634
    • (1994) Mol Cell Biol , vol.14 , pp. 655-662
    • Henderson, E.1    Stein, R.2
  • 166
    • 0037119417 scopus 로고    scopus 로고
    • Involvement of c-Jun N-terminal kinase in oxidative stress-mediated suppression of insulin gene expression
    • 10.1074/jbc.M202066200 12011047
    • Involvement of c-Jun N-terminal kinase in oxidative stress-mediated suppression of insulin gene expression. Kaneto H, Xu G, Fujii N, Kim S, Bonner-Weir S, Weir GC, J Biol Chem 2002 277 30010 30018 10.1074/jbc.M202066200 12011047
    • (2002) J Biol Chem , vol.277 , pp. 30010-30018
    • Kaneto, H.1    Xu, G.2    Fujii, N.3    Kim, S.4    Bonner-Weir, S.5    Weir, G.C.6
  • 167
    • 0034634596 scopus 로고    scopus 로고
    • Ceramide directly activates protein kinase C zeta to regulate a stress-activated protein kinase signaling complex
    • 10.1074/jbc.M007346200 10962008
    • Ceramide directly activates protein kinase C zeta to regulate a stress-activated protein kinase signaling complex. Bourbon NA, Yun J, Kester M, J Biol Chem 2000 275 35617 35623 10.1074/jbc.M007346200 10962008
    • (2000) J Biol Chem , vol.275 , pp. 35617-35623
    • Bourbon, N.A.1    Yun, J.2    Kester, M.3
  • 168
    • 0032926648 scopus 로고    scopus 로고
    • Possible involvement of atypical protein kinase C (PKC) in glucose-sensitive expression of the human insulingene: DNA binding activity and transcriptional activity of pancreatic and duodenal homeobox gene-1 (PDX-1) areenhanced via calphostin C-sensitive but phorbol 12-myristate 13-acetate (PMA) and Go 6976-insensitive pathway
    • 10.1507/endocrj.46.43 10426567
    • Possible involvement of atypical protein kinase C (PKC) in glucose-sensitive expression of the human insulingene: DNA binding activity and transcriptional activity of pancreatic and duodenal homeobox gene-1 (PDX-1) areenhanced via calphostin C-sensitive but phorbol 12-myristate 13-acetate (PMA) and Go 6976-insensitive pathway. Furukawa N, Shirotani T, Araki E, Kaneko K, Todaka M, Matsumoto K, Tsuruzoe K, Motoshima H, Yoshizato K, Kishikawa H, Shichiri M, Endocr J 1999 46 43 58 10.1507/endocrj.46.43 10426567
    • (1999) Endocr J , vol.46 , pp. 43-58
    • Furukawa, N.1    Shirotani, T.2    Araki, E.3    Kaneko, K.4    Todaka, M.5    Matsumoto, K.6    Tsuruzoe, K.7    Motoshima, H.8    Yoshizato, K.9    Kishikawa, H.10    Shichiri, M.11
  • 169
    • 0029853098 scopus 로고    scopus 로고
    • Lipid mediators of insulin resistance: Ceramide signalling down-regulates GLUT4 gene transcription in 3T3-L1 adipocytes
    • 8870666
    • Lipid mediators of insulin resistance: ceramide signalling down-regulates GLUT4 gene transcription in 3T3-L1 adipocytes. Long SD, Pekala PH, Biochem J 1996 319 179 184 8870666
    • (1996) Biochem J , vol.319 , pp. 179-184
    • Long, S.D.1    Pekala, P.H.2
  • 170
    • 34347352169 scopus 로고    scopus 로고
    • Diabetic cardiomyopathy revisited
    • 10.1161/CIRCULATIONAHA.106.679597 17592090
    • Diabetic cardiomyopathy revisited. Boudina S, Abel ED, Circulation 2007 115 3213 3223 10.1161/CIRCULATIONAHA.106.679597 17592090
    • (2007) Circulation , vol.115 , pp. 3213-3223
    • Boudina, S.1    Abel, E.D.2
  • 172
    • 72249100585 scopus 로고    scopus 로고
    • Type 1 diabetic cardiomyopathy in the Akita (Ins2WT/C96Y) mouse model is characterized by lipotoxicity and diastolic dysfunction with preserved systolic function
    • 10.1152/ajpheart.00452.2009 19801494
    • Type 1 diabetic cardiomyopathy in the Akita (Ins2WT/C96Y) mouse model is characterized by lipotoxicity and diastolic dysfunction with preserved systolic function. Basu R, Oudit GY, Wang X, Zhang L, Ussher JR, Lopaschuk GD, Kassiri Z, Am J Physiol Heart Circ Physiol 2009 297 2096 H2108 10.1152/ajpheart.00452.2009 19801494
    • (2009) Am J Physiol Heart Circ Physiol , vol.297
    • Basu, R.1    Oudit, G.Y.2    Wang, X.3    Zhang, L.4    Ussher, J.R.5    Lopaschuk, G.D.6    Kassiri, Z.7
  • 173
    • 0141563667 scopus 로고    scopus 로고
    • Secretory Zn2 + -dependent sphingomyelinase activity in the serum of patients with type 2 diabetes is elevated
    • 12953170
    • Secretory Zn2 + -dependent sphingomyelinase activity in the serum of patients with type 2 diabetes is elevated. Gorska M, Baranczuk E, Dobrzyn A, Horm Metab Res 2003 35 506 507 12953170
    • (2003) Horm Metab Res , vol.35 , pp. 506-507
    • Gorska, M.1    Baranczuk, E.2    Dobrzyn, A.3
  • 174
    • 0029762320 scopus 로고    scopus 로고
    • Rabbit aorta and human atherosclerotic lesions hydrolyze the sphingomyelin of retained low density lipoprotein. Proposed role for arterial-wall sphingomyelinase in subendothelial retention and aggregation of atherogenic lipoproteins
    • 10.1172/JCI118934 8823312
    • Rabbit aorta and human atherosclerotic lesions hydrolyze the sphingomyelin of retained low density lipoprotein. Proposed role for arterial-wall sphingomyelinase in subendothelial retention and aggregation of atherogenic lipoproteins. Schissel SL, Tweedie-Hardman J, Rapp JH, Graham G, Williams KJ, Tabas I, J Clin Invest 1996 98 1455 1464 10.1172/JCI118934 8823312
    • (1996) J Clin Invest , vol.98 , pp. 1455-1464
    • Schissel, S.L.1    Tweedie-Hardman, J.2    Rapp, J.H.3    Graham, G.4    Williams, K.J.5    Tabas, I.6
  • 175
    • 53449098208 scopus 로고    scopus 로고
    • Acid sphingomyelinase promotes lipoprotein retention within early atheromata and accelerates lesion progression
    • 10.1161/ATVBAHA.108.173344 18669882
    • Acid sphingomyelinase promotes lipoprotein retention within early atheromata and accelerates lesion progression. Devlin CM, Leventhal AR, Kuriakose G, Schuchman EH, Williams KJ, Tabas I, Arterioscler Thromb Vasc Biol 2008 28 1723 1730 10.1161/ATVBAHA.108.173344 18669882
    • (2008) Arterioscler Thromb Vasc Biol , vol.28 , pp. 1723-1730
    • Devlin, C.M.1    Leventhal, A.R.2    Kuriakose, G.3    Schuchman, E.H.4    Williams, K.J.5    Tabas, I.6
  • 177
    • 79955581245 scopus 로고    scopus 로고
    • Evaluation of sphingolipid metabolism in renal cortex of rats with streptozotocin-induced diabetes and the effectsof rapamycin
    • 10.1093/ndt/gfq633 20961887
    • Evaluation of sphingolipid metabolism in renal cortex of rats with streptozotocin-induced diabetes and the effectsof rapamycin. Liu G, Han F, Yang Y, Xie Y, Jiang H, Mao Y, Wang H, Wang M, Chen R, Yang J, Chen J, Nephrol Dial Transplant 2011 26 1493 1502 10.1093/ndt/gfq633 20961887
    • (2011) Nephrol Dial Transplant , vol.26 , pp. 1493-1502
    • Liu, G.1    Han, F.2    Yang, Y.3    Xie, Y.4    Jiang, H.5    Mao, Y.6    Wang, H.7    Wang, M.8    Chen, R.9    Yang, J.10    Chen, J.11
  • 178
    • 33644641640 scopus 로고    scopus 로고
    • Involvement of de novo ceramide synthesis in radiocontrast-induced renal tubular cell injury
    • 10.1038/sj.ki.5000057 16408118
    • Involvement of de novo ceramide synthesis in radiocontrast-induced renal tubular cell injury. Itoh Y, Yano T, Sendo T, Sueyasu M, Hirano K, Kanaide H, Oishi R, Kidney Int 2006 69 288 297 10.1038/sj.ki.5000057 16408118
    • (2006) Kidney Int , vol.69 , pp. 288-297
    • Itoh, Y.1    Yano, T.2    Sendo, T.3    Sueyasu, M.4    Hirano, K.5    Kanaide, H.6    Oishi, R.7
  • 179
    • 12144252951 scopus 로고    scopus 로고
    • Ceramide synthase is essential for endonuclease-mediated death of renal tubular epithelial cells induced by hypoxia-reoxygenation
    • 15479855
    • Ceramide synthase is essential for endonuclease-mediated death of renal tubular epithelial cells induced by hypoxia-reoxygenation. Basnakian AG, Ueda N, Hong X, Galitovsky VE, Yin X, Shah SV, Am J Physiol Renal Physiol 2005 288 308 F314 15479855
    • (2005) Am J Physiol Renal Physiol , vol.288
    • Basnakian, A.G.1    Ueda, N.2    Hong, X.3    Galitovsky, V.E.4    Yin, X.5    Shah, S.V.6
  • 182
    • 20044386906 scopus 로고    scopus 로고
    • Palmitate-induced apoptosis in cultured bovine retinal pericytes: Roles of NAD(P)H oxidase, oxidant stress, and ceramide
    • 10.2337/diabetes.54.6.1838 15919807
    • Palmitate-induced apoptosis in cultured bovine retinal pericytes: roles of NAD(P)H oxidase, oxidant stress, and ceramide. Cacicedo JM, Benjachareowong S, Chou E, Ruderman NB, Ido Y, Diabetes 2005 54 1838 1845 10.2337/diabetes.54.6. 1838 15919807
    • (2005) Diabetes , vol.54 , pp. 1838-1845
    • Cacicedo, J.M.1    Benjachareowong, S.2    Chou, E.3    Ruderman, N.B.4    Ido, Y.5
  • 183
    • 0037098871 scopus 로고    scopus 로고
    • Advanced glycation endproducts induce apoptosis of bovine retinal pericytes in culture: Involvement ofdiacylglycerol/ceramide production and oxidative stress induction
    • 10.1016/S0891-5849(02)00879-1 12106819
    • Advanced glycation endproducts induce apoptosis of bovine retinal pericytes in culture: involvement ofdiacylglycerol/ceramide production and oxidative stress induction. Denis U, Lecomte M, Paget C, Ruggiero D, Wiernsperger N, Lagarde M, Free Radic Biol Med 2002 33 236 247 10.1016/S0891-5849(02)00879-1 12106819
    • (2002) Free Radic Biol Med , vol.33 , pp. 236-247
    • Denis, U.1    Lecomte, M.2    Paget, C.3    Ruggiero, D.4    Wiernsperger, N.5    Lagarde, M.6
  • 184
    • 12144266206 scopus 로고    scopus 로고
    • A series a series gangliosides mediate the effects of advanced glycation end products on pericyte and mesangial cell proliferation: A common mediator for retinal and renal microangiopathy?
    • 10.2337/diabetes.54.1.220 15616032
    • A series a series gangliosides mediate the effects of advanced glycation end products on pericyte and mesangial cell proliferation: a common mediator for retinal and renal microangiopathy? Masson E, Troncy L, Ruggiero D, Wiernsperger N, Lagarde M, El Bawab S, Diabetes 2005 54 220 227 10.2337/diabetes.54.1.220 15616032
    • (2005) Diabetes , vol.54 , pp. 220-227
    • Masson, E.1    Troncy, L.2    Ruggiero, D.3    Wiernsperger, N.4    Lagarde, M.5    El Bawab, S.6
  • 185
    • 33845547166 scopus 로고    scopus 로고
    • Diabetes alters sphingolipid metabolism in the retina: A potential mechanism of cell death in diabetic retinopathy
    • 10.2337/db06-0539 17130506
    • Diabetes alters sphingolipid metabolism in the retina: a potential mechanism of cell death in diabetic retinopathy. Fox TE, Han X, Kelly S, Merrill AH 2nd, Martin RE, Anderson RE, Gardner TW, Kester M, Diabetes 2006 55 3573 3580 10.2337/db06-0539 17130506
    • (2006) Diabetes , vol.55 , pp. 3573-3580
    • Fox, T.E.1    Han, X.2    Kelly, S.3    Merrill, A.H.4    Martin, R.E.5    Anderson, R.E.6    Gardner, T.W.7    Kester, M.8


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