Sphingolipid signaling and redox regulation

Free Radical Biology and Medicine

Volumn 40, Issue 11, 2006, Pages 1875-1888

  Won, Je Seong ^a,b   Singh, Inderjit ^a  

^a MEDICAL UNIVERSITY OF SOUTH CAROLINA   (United States)

^b MEDICAL UNIVERSITY OF SOUTH CAROLINA   (United States)

Author keywords

Catalase; Ceramidase; Glycosylceramide; Mitochondria; NADPH oxidase; Nitric oxide synthase; Reactive nitrogen species; Reactive oxygen species; Sphingolipid; Sphingomyelinase; Superoxide dismutase

Indexed keywords

ACYLSPHINGOSINE DEACYLASE; CATALASE; CERAMIDE 1 PHOSPHATE; CERAMIDE DERIVATIVE; GLUTATHIONE; GLYCOSYLCERAMIDE; NITRIC OXIDE SYNTHASE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SPHINGOLIPID; SPHINGOMYELIN PHOSPHODIESTERASE; SPHINGOSINE 1 PHOSPHATE; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG;

APOPTOSIS; CELL PROLIFERATION; DIFFERENTIATION; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME REGULATION; GENE EXPRESSION; HOMEOSTASIS; HYDROLYSIS; INFLAMMATION; MITOCHONDRION; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PRIORITY JOURNAL; REVIEW;

ANIMALS; HUMANS; OXIDATION-REDUCTION; OXIDATIVE STRESS; SIGNAL TRANSDUCTION; SPHINGOLIPIDS;

EID: 33646589316     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2006.01.035     Document Type: Review

References (189)

1. Boveris A., and Chance B. The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen. Biochem. J. 134 (1973) 707-716
2. Grisham M.B., Jourd'Heuil D., and Wink D.A. Nitric oxide: I. Physiological chemistry of nitric oxide and its metabolites:implications in inflammation. Am. J. Physiol. 276 (1999) G315-G321
3. Endemann D.H., and Schiffrin E.L. Nitric oxide, oxidative excess, and vascular complications of diabetes mellitus. Curr. Hypertens. Rep. 6 (2004) 85-89
4. Arnold W.P., Mittal C.K., Katsuki S., and Murad F. Nitric oxide activates guanylate cyclase and increases guanosine 3′:5′-cyclic monophosphate levels in various tissue preparations. Proc. Natl. Acad. Sci. USA 74 (1977) 3203-3207
5. Pfeilschifter J., Eberhardt W., and Beck K.F. Regulation of gene expression by nitric oxide. Pflugers Arch. 442 (2001) 479-486
6. Pfeilschifter J., Eberhardt W., and Huwiler A. Nitric oxide and mechanisms of redox signalling: matrix and matrix-metabolizing enzymes as prime nitric oxide targets. Eur. J. Pharmacol. 429 (2001) 279-286
7. Pettus B.J., Chalfant C.E., and Hannun Y.A. Ceramide in apoptosis: an overview and current perspectives. Biochim. Biophys. Acta 1585 (2002) 114-125
8. Watterson K.R., Ratz P.H., and Spiegel S. The role of sphingosine-1-phosphate in smooth muscle contraction. Cell Signal. 17 (2005) 289-298
9. Proia R.L. Glycosphingolipid functions: insights from engineered mouse models. Philos. Trans. R. Soc. Lond. B: Biol. Sci. 358 (2003) 879-883
10. Won J.S., Im Y.B., Khan M., Singh A.K., and Singh I. The role of neutral sphingomyelinase produced ceramide in lipopolysaccharide-mediated expression of inducible nitric oxide synthase. J. Neurochem. 88 (2004) 583-593
11. Pahan K., Sheikh F.G., Khan M., Namboodiri A.M., and Singh I. Sphingomyelinase and ceramide stimulate the expression of inducible nitric-oxide synthase in rat primary astrocytes. J. Biol. Chem. 273 (1998) 2591-2600
12. Singh I., Pahan K., Khan M., and Singh A.K. Cytokine-mediated induction of ceramide production is redox-sensitive. Implications to proinflammatory cytokine-mediated apoptosis in demyelinating diseases. J. Biol. Chem. 273 (1998) 20354-20362
13. Dobrowsky R.T. Sphingolipid signalling domains floating on rafts or buried in caves?. Cell Signal. 12 (2000) 81-90
14. Gulbins E., and Kolesnick R. Raft ceramide in molecular medicine. Oncogene 22 (2003) 7070-7077
15. Rotolo J.A., Zhang J., Donepudi M., Lee H., Fuks Z., and Kolesnick R. Caspase-dependent and -independent activation of acid sphingomyelinase signaling. J. Biol. Chem. 280 (2005) 26425-26434
16. Kilkus J., Goswami R., Testai F.D., and Dawson G. Ceramide in rafts (detergent-insoluble fraction) mediates cell death in neurotumor cell lines. J. Neurosci. Res. 72 (2003) 65-75
17. Mitsutake S., Tani M., Okino N., Mori K., Ichinose S., Omori A., Iida H., Nakamura T., and Ito M. Purification, characterization, molecular cloning, and subcellular distribution of neutral ceramidase of rat kidney. J. Biol. Chem. 276 (2001) 26249-26259
18. Urtz N., Olivera A., Bofill-Cardona E., Csonga R., Billich A., Mechtcheriakova D., Bornancin F., Woisetschlager M., Rivera J., and Baumruker T. Early activation of sphingosine kinase in mast cells and recruitment to FcepsilonRI are mediated by its interaction with Lyn kinase. Mol. Cell. Biol. 24 (2004) 8765-8777
19. Hinkovska-Galcheva V., Boxer L.A., Kindzelskii A., Hiraoka M., Abe A., Goparju S., Spiegel S., Petty H.R., and Shayman J.A. Ceramide 1-phosphate, a mediator of phagocytosis. J. Biol. Chem. 280 (2005) 26612-26621
20. Ostrom R.S., and Insel P.A. The evolving role of lipid rafts and caveolae in G protein-coupled receptor signaling: implications for molecular pharmacology. Br. J. Pharmacol. 143 (2004) 235-245
21. Laude A.J., and Prior I.A. Plasma membrane microdomains: organization, function and trafficking. Mol. Membr. Biol. 21 (2004) 193-205
22. Huwiler A., Pfeilschifter J., and van den Bosch H. Nitric oxide donors induce stress signaling via ceramide formation in rat renal mesangial cells. J. Biol. Chem. 274 (1999) 7190-7195
23. Qiu H., Edmunds T., Baker-Malcolm J., Karey K.P., Estes S., Schwarz C., Hughes H., and Van Patten S.M. Activation of human acid sphingomyelinase through modification or deletion of C-terminal cysteine. J. Biol. Chem. 278 (2003) 32744-32752
24. De Nadai C., Sestili P., Cantoni O., Lievremont J.P., Sciorati C., Barsacchi R., Moncada S., Meldolesi J., and Clementi E. Nitric oxide inhibits tumor necrosis factor-alpha-induced apoptosis by reducing the generation of ceramide. Proc. Natl. Acad. Sci. USA 97 (2000) 5480-5485
25. Mansat-de Mas V., Bezombes C., Quillet-Mary A., Bettaieb A., D'Orgeix A.D., Laurent G., and Jaffrezou J.P. Implication of radical oxygen species in ceramide generation, c-Jun N-terminal kinase activation and apoptosis induced by daunorubicin. Mol. Pharmacol. 56 (1999) 867-874
26. Zhang D.X., Zou A.P., and Li P.L. Ceramide-induced activation of NADPH oxidase and endothelial dysfunction in small coronary arteries. Am. J. Physiol. Heart Circ. Physiol. 284 (2003) H605-H612
27. Garcia-Ruiz C., Colell A., Mari M., Morales A., and Fernandez-Checa J.C. Direct effect of ceramide on the mitochondrial electron transport chain leads to generation of reactive oxygen species. Role of mitochondrial glutathione. J. Biol. Chem. 272 (1997) 11369-11377
28. Viani P., Giussani P., Ferraretto A., Signorile A., Riboni L., and Tettamanti G. Nitric oxide production in living neurons is modulated by sphingosine: a fluorescence microscopy study. FEBS Lett. 506 (2001) 185-190
29. Johns D.G., Osborn H., and Webb R.C. Ceramide: a novel cell signaling mechanism for vasodilation. Biochem. Biophys. Res. Commun. 237 (1997) 95-97
30. Iwai K., Kondo T., Watanabe M., Yabu T., Kitano T., Taguchi Y., Umehara H., Takahashi A., Uchiyama T., and Okazaki T. Ceramide increases oxidative damage due to inhibition of catalase by caspase-3-dependent proteolysis in HL-60 cell apoptosis. J. Biol. Chem. 278 (2003) 9813-9822
31. Macmillan-Crow L.A., and Cruthirds D.L. Invited review: manganese superoxide dismutase in disease. Free Radic. Res. 34 (2001) 325-336
32. Goni F.M., and Alonso A. Sphingomyelinases: enzymology and membrane activity. FEBS Lett. 531 (2002) 38-46
33. Levade T., Andrieu-Abadie N., Segui B., Auge N., Chatelut M., Jaffrezou J.P., and Salvayre R. Sphingomyelin-degrading pathways in human cells role in cell signalling. Chem. Phys. Lipids 102 (1999) 167-178
34. Zumbansen M., and Stoffel W. Neutral sphingomyelinase 1 deficiency in the mouse causes no lipid storage disease. Mol. Cell. Biol. 22 (2002) 3633-3638
35. Hofmann K., Tomiuk S., Wolff G., and Stoffel W. Cloning and characterization of the mammalian brain-specific, Mg2+-dependent neutral sphingomyelinase. Proc. Natl. Acad. Sci. USA 97 (2000) 5895-5900
36. Tomiuk S., Hofmann K., Nix M., Zumbansen M., and Stoffel W. Cloned mammalian neutral sphingomyelinase: functions in sphingolipid signaling?. Proc. Natl. Acad. Sci. USA 95 (1998) 3638-3643
37. Horinouchi K., Erlich S., Perl D.P., Ferlinz K., Bisgaier C.L., Sandhoff K., Desnick R.J., Stewart C.L., and Schuchman E.H. Acid sphingomyelinase deficient mice: a model of types A and B Niemann-Pick disease. Nat. Genet. 10 (1995) 288-293
38. Schuchman E.H., Levran O., Pereira L.V., and Desnick R.J. Structural organization and complete nucleotide sequence of the gene encoding human acid sphingomyelinase (SMPD1). Genomics 12 (1992) 197-205
39. Hurwitz R., Ferlinz K., Vielhaber G., Moczall H., and Sandhoff K. Processing of human acid sphingomyelinase in normal and I-cell fibroblasts. J. Biol. Chem. 269 (1994) 5440-5445
40. Schissel S.L., Schuchman E.H., Williams K.J., and Tabas I. Zn2+-stimulated sphingomyelinase is secreted by many cell types and is a product of the acid sphingomyelinase gene. J. Biol. Chem. 271 (1996) 18431-18436
41. Itoh N., and Nagata S. A novel protein domain required for apoptosis. Mutational analysis of human Fas antigen. J. Biol. Chem. 268 (1993) 10932-10937
42. Gulbins E., and Grassme H. Ceramide and cell death receptor clustering. Biochim. Biophys. Acta 1585 (2002) 139-145
43. Ahmad T.Y., Beaudet A.L., Sparrow J.T., and Morrisett J.D. Human lysosomal sphingomyelinase: substrate efficacy of apolipoprotein/sphingomyelin complexes. Biochemistry 25 (1986) 4415-4420
44. Bilderback T.R., Gazula V.R., and Dobrowsky R.T. Phosphoinositide 3-kinase regulates crosstalk between Trk A tyrosine kinase and p75(NTR)-dependent sphingolipid signaling pathways. J. Neurochem. 76 (2001) 1540-1551
45. Quintern L.E., and Sandhoff K. Human acid sphingomyelinase from human urine. Methods Enzymol. 197 (1991) 536-540
46. Kolesnick R.N. 1,2-Diacylglycerols but not phorbol esters stimulate sphingomyelin hydrolysis in GH3 pituitary cells. J. Biol. Chem. 262 (1987) 16759-16762
47. Gomez-Munoz A., Kong J., Salh B., and Steinbrecher U.P. Sphingosine-1-phosphate inhibits acid sphingomyelinase and blocks apoptosis in macrophages. FEBS Lett. 539 (2003) 56-60
48. Rao B.G., and Spence M.W. Sphingomyelinase activity at pH 7.4 in human brain and a comparison to activity at pH 5.0. J. Lipid Res. 17 (1976) 506-515
49. Liu B., and Hannun Y.A. Inhibition of the neutral magnesium-dependent sphingomyelinase by glutathione. J. Biol. Chem. 272 (1997) 16281-16287
50. Alliegro M.C. Effects of dithiothreitol on protein activity unrelated to thiol-disulfide exchange: for consideration in the analysis of protein function with Cleland's reagent. Anal. Biochem. 282 (2000) 102-106
51. Bulotta S., Barsacchi R., Rotiroti D., Borgese N., and Clementi E. Activation of the endothelial nitric-oxide synthase by tumor necrosis factor-alpha. A novel feedback mechanism regulating cell death. J. Biol. Chem. 276 (2001) 6529-6536
52. Falcone S., Perrotta C., De Palma C., Pisconti A., Sciorati C., Capobianco A., Rovere-Querini P., Manfredi A.A., and Clementi E. Activation of acid sphingomyelinase and its inhibition by the nitric oxide/cyclic guanosine 3′,5′-monophosphate pathway: key events in Escherichia coli-elicited apoptosis of dendritic cells. J. Immunol. 173 (2004) 4452-4463
53. Barsacchi R., Perrotta C., Sestili P., Cantoni O., Moncada S., and Clementi E. Cyclic GMP-dependent inhibition of acid sphingomyelinase by nitric oxide: an early step in protection against apoptosis. Cell Death Differ. 9 (2002) 1248-1255
54. Pilane C.M., and LaBelle E.F. NO induced apoptosis of vascular smooth muscle cells accompanied by ceramide increase. J. Cell. Physiol. 199 (2004) 310-315
55. Matsumoto A., Comatas K.E., Liu L., and Stamler J.S. Screening for nitric oxide-dependent protein-protein interactions. Science 301 (2003) 657-661
56. Hess D.T., Matsumoto A., Kim S.O., Marshall H.E., and Stamler J.S. Protein S-nitrosylation: purview and parameters. Nat. Rev. Mol. Cell. Biol. 6 (2005) 150-166
57. Schneider P.B., and Kennedy E.P. Sphingomyelinase in normal human spleens and in spleens from subjects with Niemann-Pick disease. J. Lipid Res. 8 (1967) 202-209
58. Sawai H., Domae N., Nagan N., and Hannun Y.A. Function of the cloned putative neutral sphingomyelinase as lyso-platelet activating factor-phospholipase C. J. Biol. Chem. 274 (1999) 38131-38139
59. Marchesini N., and Hannun Y.A. Acid and neutral sphingomyelinases: roles and mechanisms of regulation. Biochem. Cell Biol. 82 (2004) 27-44
60. Marchesini N., Luberto C., and Hannun Y.A. Biochemical properties of mammalian neutral sphingomyelinase 2 and its role in sphingolipid metabolism. J. Biol. Chem. 278 (2003) 13775-13783
61. Bernardo K., Krut O., Wiegmann K., Kreder D., Micheli M., Schafer R., Sickman A., Schmidt W.E., Schroder J.M., Meyer H.E., Sandhoff K., and Kronke M. Purification and characterization of a magnesium-dependent neutral sphingomyelinase from bovine brain. J. Biol. Chem. 275 (2000) 7641-7647
62. Kondo T., Kitano T., Iwai K., Watanabe M., Taguchi Y., Yabu T., Umehara H., Domae N., Uchiyama T., and Okazaki T. Control of ceramide-induced apoptosis by IGF-1: involvement of PI-3 kinase, caspase-3 and catalase. Cell Death Differ. 9 (2002) 682-692
63. Sumitomo M., Ohba M., Asakuma J., Asano T., Kuroki T., Asano T., and Hayakawa M. Protein kinase Cdelta amplifies ceramide formation via mitochondrial signaling in prostate cancer cells. J. Clin. Invest. 109 (2002) 827-836
64. Adam D., Wiegmann K., Adam-Klages S., Ruff A., and Kronke M. A novel cytoplasmic domain of the p55 tumor necrosis factor receptor initiates the neutral sphingomyelinase pathway. J. Biol. Chem. 271 (1996) 14617-14622
65. Kreder D., Krut O., Adam-Klages S., Wiegmann K., Scherer G., Plitz T., Jensen J.M., Proksch E., Steinmann J., Pfeffer K., and Kronke M. Impaired neutral sphingomyelinase activation and cutaneous barrier repair in FAN-deficient mice. EMBO J. 18 (1999) 2472-2479
66. Segui B., Andrieu-Abadie N., Adam-Klages S., Meilhac O., Kreder D., Garcia V., Bruno A.P., Jaffrezou J.P., Salvayre R., Kronke M., and Levade T. CD40 signals apoptosis through FAN-regulated activation of the sphingomyelin-ceramide pathway. J. Biol. Chem. 274 (1999) 37251-37258
67. Jung S.Y., Suh J.H., Park H.J., Jung K.M., Kim M.Y., Na D.S., and Kim D.K. Identification of multiple forms of membrane-associated neutral sphingomyelinase in bovine brain. J. Neurochem. 75 (2000) 1004-1014
68. Yoshimura S., Banno Y., Nakashima S., Hayashi K., Yamakawa H., Sawada M., Sakai N., and Nozawa Y. Inhibition of neutral sphingomyelinase activation and ceramide formation by glutathione in hypoxic PC12 cell death. J. Neurochem. 73 (1999) 675-683
69. Ayasolla K., Khan M., Singh A.K., and Singh I. Inflammatory mediator and beta-amyloid (25-35)-induced ceramide generation and iNOS expression are inhibited by vitamin E. Free Radic. Biol. Med. 37 (2004) 325-338
70. Lee J.T., Xu J., Lee J.M., Ku G., Han X., Yang D.I., Chen S., and Hsu C.Y. Amyloid-beta peptide induces oligodendrocyte death by activating the neutral sphingomyelinase-ceramide pathway. J. Cell Biol. 164 (2004) 123-131
71. Okamoto Y., Obeid L.M., and Hannun Y.A. Bcl-xL interrupts oxidative activation of neutral sphingomyelinase. FEBS Lett. 530 (2002) 104-108
72. El-Assaad W., El-Sabban M., Awaraji C., Abboushi N., and Dbaibo G.S. Distinct sites of action of Bcl-2 and Bcl-xL in the ceramide pathway of apoptosis. Biochem. J. 336 Pt 3 (1998) 735-741
73. Grazide S., Maestre N., Veldman R.J., Bezombes C., Maddens S., Levade T., Laurent G., and Jaffrezou J.P. Ara-C- and daunorubicin-induced recruitment of Lyn in sphingomyelinase-enriched membrane rafts. FASEB J. 16 (2002) 1685-1687
74. Bezombes C., de Thonel A., Apostolou A., Louat T., Jaffrezou J.P., Laurent G., and Quillet-Mary A. Overexpression of protein kinase Czeta confers protection against antileukemic drugs by inhibiting the redox-dependent sphingomyelinase activation. Mol. Pharmacol. 62 (2002) 1446-1455
75. Takeda Y., Tashima M., Takahashi A., Uchiyama T., and Okazaki T. Ceramide generation in nitric oxide-induced apoptosis. Activation of magnesium-dependent neutral sphingomyelinase via caspase-3. J. Biol. Chem. 274 (1999) 10654-10660
76. Franzen R., Fabbro D., Aschrafi A., Pfeilschifter J., and Huwiler A. Nitric oxide induces degradation of the neutral ceramidase in rat renal mesangial cells and is counterregulated by protein kinase C. J. Biol. Chem. 277 (2002) 46184-46190
77. Franzen R., Pfeilschifter J., and Huwiler A. Nitric oxide induces neutral ceramidase degradation by the ubiquitin/proteasome complex in renal mesangial cell cultures. FEBS Lett. 532 (2002) 441-444
78. Di Paola M., Cocco T., and Lorusso M. Ceramide interaction with the respiratory chain of heart mitochondria. Biochemistry 39 (2000) 6660-6668
79. Bokoch G.M., and Diebold B.A. Current molecular models for NADPH oxidase regulation by Rac GTPase. Blood 100 (2002) 2692-2696
80. Nauseef W.M. Assembly of the phagocyte NADPH oxidase. Histochem. Cell Biol. 122 (2004) 277-291
81. Lambeth J.D. Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases. Curr. Opin. Hematol. 9 (2002) 11-17
82. Lambeth J.D., Cheng G., Arnold R.S., and Edens W.A. Novel homologs of gp91phox. Trends Biochem. Sci. 25 (2000) 459-461
83. Liel Y., Rudich A., Nagauker-Shriker O., Yermiyahu T., and Levy R. Monocyte dysfunction in patients with Gaucher disease: evidence for interference of glucocerebroside with superoxide generation. Blood 83 (1994) 2646-2653
84. Moskwa P., Palicz A., Paclet M.H., Dagher M.C., Erdos M., Marodi L., and Ligeti E. Glucocerebroside inhibits NADPH oxidase activation in cell-free system. Biochim. Biophys. Acta 1688 (2004) 197-203
85. Arai T., Bhunia A.K., Chatterjee S., and Bulkley G.B. Lactosylceramide stimulates human neutrophils to upregulate Mac-1, adhere to endothelium, and generate reactive oxygen metabolites in vitro. Circ. Res. 82 (1998) 540-547
86. Bhunia A.K., Han H., Snowden A., and Chatterjee S. Redox-regulated signaling by lactosylceramide in the proliferation of human aortic smooth muscle cells. J. Biol. Chem. 272 (1997) 15642-15649
87. Bhunia A.K., Arai T., Bulkley G., and Chatterjee S. Lactosylceramide mediates tumor necrosis factor-alpha-induced intercellular adhesion molecule-1 (ICAM-1) expression and the adhesion of neutrophil in human umbilical vein endothelial cells. J. Biol. Chem. 273 (1998) 34349-34357
88. Garcia-Ruiz C., Colell A., Paris R., and Fernandez-Checa J.C. Direct interaction of GD3 ganglioside with mitochondria generates reactive oxygen species followed by mitochondrial permeability transition, cytochrome c release, and caspase activation. FASEB J. 14 (2000) 847-858
89. Pannu R., Won J.S., Khan M., Singh A.K., and Singh I. A novel role of lactosylceramide in the regulation of lipopolysaccharide/interferon-gamma-mediated inducible nitric oxide synthase gene expression: implications for neuroinflammatory diseases. J. Neurosci. 24 (2004) 5942-5954
90. Iwabuchi K., and Nagaoka I. Lactosylceramide-enriched glycosphingolipid signaling domain mediates superoxide generation from human neutrophils. Blood 100 (2002) 1454-1464
91. Zhang A.Y., Teggatz E.G., Zou A.P., Campbell W.B., and Li P.L. Endostatin uncouples NO and Ca2+ response to bradykinin through enhanced O2*- production in the intact coronary endothelium. Am. J. Physiol. Heart Circ. Physiol. 288 (2005) H686-H694
92. Yi F., Zhang A.Y., Janscha J.L., Li P.L., and Zou A.P. Homocysteine activates NADH/NADPH oxidase through ceramide-stimulated Rac GTPase activity in rat mesangial cells. Kidney Int. 66 (2004) 1977-1987
93. Reinehr R., Becker S., Eberle A., Grether-Beck S., and Haussinger D. Involvement of NADPH oxidase isoforms and SRC family kinases in CD95-dependent hepatocyte apoptosis. J. Biol. Chem. 280 (2005) 27179-27194
94. Das D.K., George A., Liu X.K., and Rao P.S. Detection of hydroxyl radical in the mitochondria of ischemic-reperfused myocardium by trapping with salicylate. Biochem. Biophys. Res. Commun. 165 (1989) 1004-1009
95. Wang X. The expanding role of mitochondria in apoptosis. Genes Dev. 15 (2001) 2922-2933
96. Du C., Fang M., Li Y., Li L., and Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102 (2000) 33-42
97. Joza N., Susin S.A., Daugas E., Stanford W.L., Cho S.K., Li C.Y., Sasaki T., Elia A.J., Cheng H.Y., Ravagnan L., Ferri K.F., Zamzami N., Wakeham A., Hakem R., Yoshida H., Kong Y.Y., Mak T.W., Zuniga-Pflucker J.C., Kroemer G., and Penninger J.M. Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death. Nature 410 (2001) 549-554
98. Li L.Y., Luo X., and Wang X. Endonuclease G is an apoptotic DNase when released from mitochondria. Nature 412 (2001) 95-99
99. Cai J., and Jones D.P. Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss. J. Biol. Chem. 273 (1998) 11401-11404
100. Ghafourifar P., Klein S.D., Schucht O., Schenk U., Pruschy M., Rocha S., and Richter C. Ceramide induces cytochrome c release from isolated mitochondria. Importance of mitochondrial redox state. J. Biol. Chem. 274 (1999) 6080-6084
101. Voehringer D.W., McConkey D.J., McDonnell T.J., Brisbay S., and Meyn R.E. Bcl-2 expression causes redistribution of glutathione to the nucleus. Proc. Natl. Acad. Sci. USA 95 (1998) 2956-2960
102. Kane D.J., Sarafian T.A., Anton R., Hahn H., Gralla E.B., Valentine J.S., Ord T., and Bredesen D.E. Bcl-2 inhibition of neural death: decreased generation of reactive oxygen species. Science 262 (1993) 1274-1277
103. Voehringer D.W. BCL-2 and glutathione: alterations in cellular redox state that regulate apoptosis sensitivity. Free Radic. Biol. Med. 27 (1999) 945-950
104. Yang J., Liu X., Bhalla K., Kim C.N., Ibrado A.M., Cai J., Peng T.I., Jones D.P., and Wang X. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science 275 (1997) 1129-1132
105. Marzo I., Brenner C., Zamzami N., Jurgensmeier J.M., Susin S.A., Vieira H.L., Prevost M.C., Xie Z., Matsuyama S., Reed J.C., and Kroemer G. Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis. Science 281 (1998) 2027-2031
106. Petit P.X., Lecoeur H., Zorn E., Dauguet C., Mignotte B., and Gougeon M.L. Alterations in mitochondrial structure and function are early events of dexamethasone-induced thymocyte apoptosis. J. Cell Biol. 130 (1995) 157-167
107. Di Nardo A., Benassi L., Magnoni C., Cossarizza A., Seidenari S., and Giannetti A. Ceramide 2 (N-acetyl sphingosine) is associated with reduction in Bcl-2 protein levels by Western blotting and with apoptosis in cultured human keratinocytes. Br. J. Dermatol. 143 (2000) 491-497
108. Chen M., Quintans J., Fuks Z., Thompson C., Kufe D.W., and Weichselbaum R.R. Suppression of Bcl-2 messenger RNA production may mediate apoptosis after ionizing radiation, tumor necrosis factor alpha, and ceramide. Cancer Res. 55 (1995) 991-994
109. Gudz T.I., Tserng K.Y., and Hoppel C.L. Direct inhibition of mitochondrial respiratory chain complex III by cell-permeable ceramide. J. Biol. Chem. 272 (1997) 24154-24158
110. Schulze-Osthoff K., Bakker A.C., Vanhaesebroeck B., Beyaert R., Jacob W.A., and Fiers W. Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions. Evidence for the involvement of mitochondrial radical generation. J. Biol. Chem. 267 (1992) 5317-5323
111. Siskind L.J., and Colombini M. The lipids C2- and C16-ceramide form large stable channels. Implications for apoptosis. J. Biol. Chem. 275 (2000) 38640-38644
112. Ardail D., Popa I., Alcantara K., Pons A., Zanetta J.P., Louisot P., Thomas L., and Portoukalian J. Occurrence of ceramides and neutral glycolipids with unusual long-chain base composition in purified rat liver mitochondria. FEBS Lett. 488 (2001) 160-164
113. El Bawab S., Roddy P., Qian T., Bielawska A., Lemasters J.J., and Hannun Y.A. Molecular cloning and characterization of a human mitochondrial ceramidase. J. Biol. Chem. 275 (2000) 21508-21513
114. Shimeno H., Soeda S., Sakamoto M., Kouchi T., Kowakame T., and Kihara T. Partial purification and characterization of sphingosine N-acyltransferase (ceramide synthase) from bovine liver mitochondrion-rich fraction. Lipids 33 (1998) 601-605
115. Cuvillier O. Sphingosine in apoptosis signaling. Biochim. Biophys. Acta 1585 (2002) 153-162
116. Sakakura C., Sweeney E.A., Shirahama T., Hakomori S., and Igarashi Y. Suppression of bcl-2 gene expression by sphingosine in the apoptosis of human leukemic HL-60 cells during phorbol ester-induced terminal differentiation. FEBS Lett. 379 (1996) 177-180
117. Shirahama T., Sakakura C., Sweeney E.A., Ozawa M., Takemoto M., Nishiyama K., Ohi Y., and Igarashi Y. Sphingosine induces apoptosis in androgen-independent human prostatic carcinoma DU-145 cells by suppression of bcl-X(L) gene expression. FEBS Lett. 407 (1997) 97-100
118. Cuvillier O., Edsall L., and Spiegel S. Involvement of sphingosine in mitochondria-dependent Fas-induced apoptosis of type II Jurkat T cells. J. Biol. Chem. 275 (2000) 15691-15700
119. Cuvillier O., Nava V.E., Murthy S.K., Edsall L.C., Levade T., Milstien S., and Spiegel S. Sphingosine generation, cytochrome c release, and activation of caspase-7 in doxorubicin-induced apoptosis of MCF7 breast adenocarcinoma cells. Cell Death Differ. 8 (2001) 162-171
120. Kagedal K., Zhao M., Svensson I., and Brunk U.T. Sphingosine-induced apoptosis is dependent on lysosomal proteases. Biochem. J. 359 (2001) 335-343
121. Sauer B., Gonska H., Manggau M., Kim D.S., Schraut C., Schafer-Korting M., and Kleuser B. Sphingosine 1-phosphate is involved in cytoprotective actions of calcitriol in human fibroblasts and enhances the intracellular Bcl-2/Bax rheostat. Pharmazie 60 (2005) 298-304
122. Cuvillier O., and Levade T. Sphingosine 1-phosphate antagonizes apoptosis of human leukemia cells by inhibiting release of cytochrome c and Smac/DIABLO from mitochondria. Blood 98 (2001) 2828-2836
123. Edsall L.C., Cuvillier O., Twitty S., Spiegel S., and Milstien S. Sphingosine kinase expression regulates apoptosis and caspase activation in PC12 cells. J. Neurochem. 76 (2001) 1573-1584
124. Olivera A., Kohama T., Edsall L., Nava V., Cuvillier O., Poulton S., and Spiegel S. Sphingosine kinase expression increases intracellular sphingosine-1-phosphate and promotes cell growth and survival. J. Cell Biol. 147 (1999) 545-558
125. Hong Y.B., Kim E.Y., and Jung S.C. Down-regulation of Bcl-2 in the fetal brain of the Gaucher disease mouse model: a possible role in the neuronal loss. J. Hum. Genet. 49 (2004) 349-354
126. Lenartowicz E., Bernardi P., and Azzone G.F. Phenylarsine oxide induces the cyclosporin A-sensitive membrane permeability transition in rat liver mitochondria. J. Bioenerg. Biomembr. 23 (1991) 679-688
127. Petronilli V., Costantini P., Scorrano L., Colonna R., Passamonti S., and Bernardi P. The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents. J. Biol. Chem. 269 (1994) 16638-16642
128. Rippo M.R., Malisan F., Ravagnan L., Tomassini B., Condo I., Costantini P., Susin S.A., Rufini A., Todaro M., Kroemer G., and Testi R. GD3 ganglioside directly targets mitochondria in a bcl-2-controlled fashion. FASEB J. 14 (2000) 2047-2054
129. Ignarro L.J. Nitric oxide: a unique endogenous signaling molecule in vascular biology. Biosci. Rep. 19 (1999) 51-71
130. Murad F. Nitric oxide signaling: would you believe that a simple free radical could be a second messenger, autacoid, paracrine substance, neurotransmitter, and hormone?. Recent Prog. Horm. Res. 53 (1998) 43-59 discussion 59-60
131. Moncada S. Nitric oxide in the vasculature: physiology and pathophysiology. Ann. N. Y. Acad. Sci. 811 (1997) 60-67 discussion 67-69
132. Schmidt H.H., Lohmann S.M., and Walter U. The nitric oxide and cGMP signal transduction system: regulation and mechanism of action. Biochim. Biophys. Acta 1178 (1993) 153-175
133. Lecomte P.V., De Mulder P.A., Adriaensen H.F., and De Hert S.G. Role of the nitric oxide-cGMP pathway in the cardiovascular effects of anesthetic agents: a review. Acta Anaesthesiol. Belg. 50 (1999) 105-112
134. Mayer B., Koesling D., and Bohme E. Characterization of nitric oxide synthase, soluble guanylyl cyclase, and Ca2+/calmodulin-stimulated cGMP phosphodiesterase as components of neuronal signal transduction. Adv. Second Messenger Phosphoprotein Res. 28 (1993) 111-119
135. Beckman J.S., Beckman T.W., Chen J., Marshall P.A., and Freeman B.A. Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc. Natl. Acad. Sci. USA 87 (1990) 1620-1624
136. Koprowski H., Zheng Y.M., Heber-Katz E., Fraser N., Rorke L., Fu Z.F., Hanlon C., and Dietzschold B. In vivo expression of inducible nitric oxide synthase in experimentally induced neurologic diseases. Proc. Natl. Acad. Sci. USA 90 (1993) 3024-3027
137. Mitrovic B., Ignarro L.J., Montestruque S., Smoll A., and Merrill J.E. Nitric oxide as a potential pathological mechanism in demyelination: its differential effects on primary glial cells in vitro. Neuroscience 61 (1994) 575-585
138. Gross S.S., and Wolin M.S. Nitric oxide: pathophysiological mechanisms. Annu. Rev. Physiol. 57 (1995) 737-769
139. Kelly R.A., Balligand J.L., and Smith T.W. Nitric oxide and cardiac function. Circ. Res. 79 (1996) 363-380
140. Jones M.J., and Murray A.W. Evidence that ceramide selectively inhibits protein kinase C-alpha translocation and modulates bradykinin activation of phospholipase D. J. Biol. Chem. 270 (1995) 5007-5013
141. Lee J.Y., Hannun Y.A., and Obeid L.M. Ceramide inactivates cellular protein kinase Calpha. J. Biol. Chem. 271 (1996) 13169-13174
142. Jin J.S., Tsai C.S., Si X., and Webb R.C. Endothelium dependent and independent relaxations induced by ceramide in vascular smooth muscles. Chin. J. Physiol. 42 (1999) 47-51
143. Gallinat S., Busche S., Schutze S., Kronke M., and Unger T. AT2 receptor stimulation induces generation of ceramides in PC12W cells. FEBS Lett. 443 (1999) 75-79
144. Lehtonen J.Y., Horiuchi M., Daviet L., Akishita M., and Dzau V.J. Activation of the de novo biosynthesis of sphingolipids mediates angiotensin II type 2 receptor-induced apoptosis. J. Biol. Chem. 274 (1999) 16901-16906
145. Berry C., Touyz R., Dominiczak A.F., Webb R.C., and Johns D.G. Angiotensin receptors: signaling, vascular pathophysiology, and interactions with ceramide. Am. J. Physiol. Heart Circ. Physiol. 281 (2001) H2337-H2365
146. Barsacchi R., Perrotta C., Bulotta S., Moncada S., Borgese N., and Clementi E. Activation of endothelial nitric-oxide synthase by tumor necrosis factor-alpha: a novel pathway involving sequential activation of neutral sphingomyelinase, phosphatidylinositol-3′ kinase, and Akt. Mol. Pharmacol. 63 (2003) 886-895
147. Arena S., Pattarozzi A., Thellung S., Villa V., Corsaro A., Massa A., Diana F., Spoto G., Forcella S., Damonte G., Filocamo M., Benatti U., Schettini G., and Florioa T. Nitric oxide production stimulated by the basic fibroblast growth factor requires the synthesis of ceramide. Ann. N. Y. Acad. Sci. 973 (2002) 94-104
148. Florio T., Arena S., Pattarozzi A., Thellung S., Corsaro A., Villa V., Massa A., Diana F., Spoto G., Forcella S., Damonte G., Filocamo M., Benatti U., and Schettini G. Basic fibroblast growth factor activates endothelial nitric-oxide synthase in CHO-K1 cells via the activation of ceramide synthesis. Mol. Pharmacol. 63 (2003) 297-310
149. Zhang D.X., Zou A.P., and Li P.L. Ceramide reduces endothelium-dependent vasodilation by increasing superoxide production in small bovine coronary arteries. Circ. Res. 88 (2001) 824-831
150. Didion S.P., and Faraci F.M. Ceramide-induced impairment of endothelial function is prevented by CuZn superoxide dismutase overexpression. Arterioscler. Thromb. Vasc. Biol. 25 (2005) 90-95
151. Li H., Junk P., Huwiler A., Burkhardt C., Wallerath T., Pfeilschifter J., and Forstermann U. Dual effect of ceramide on human endothelial cells: induction of oxidative stress and transcriptional upregulation of endothelial nitric oxide synthase. Circulation 106 (2002) 2250-2256
152. Li H., Wallerath T., Munzel T., and Forstermann U. Regulation of endothelial-type NO synthase expression in pathophysiology and in response to drugs. Nitric Oxide 7 (2002) 149-164
153. Hatanaka Y., Fujii J., Fukutomi T., Watanabe T., Che W., Sanada Y., Igarashi Y., and Taniguchi N. Reactive oxygen species enhances the induction of inducible nitric oxide synthase by sphingomyelinase in RAW264.7 cells. Biochim. Biophys. Acta 1393 (1998) 203-210
154. Knapp K.M., and English B.K. Ceramide-mediated stimulation of inducible nitric oxide synthase (iNOS) and tumor necrosis factor (TNF) accumulation in murine macrophages requires tyrosine kinase activity. J. Leukoc. Biol. 67 (2000) 735-741
155. Manthey C.L., and Schuchman E.H. Acid sphingomyelinase-derived ceramide is not required for inflammatory cytokine signalling in murine macrophages. Cytokine 10 (1998) 654-661
156. Mathias S., Dressler K.A., and Kolesnick R.N. Characterization of a ceramide-activated protein kinase: stimulation by tumor necrosis factor alpha. Proc. Natl. Acad. Sci. USA 88 (1991) 10009-10013
157. Zhang Y., Yao B., Delikat S., Bayoumy S., Lin X.H., Basu S., McGinley M., Chan-Hui P.Y., Lichenstein H., and Kolesnick R. Kinase suppressor of Ras is ceramide-activated protein kinase. Cell 89 (1997) 63-72
158. Dobrowsky R.T., Kamibayashi C., Mumby M.C., and Hannun Y.A. Ceramide activates heterotrimeric protein phosphatase 2A. J. Biol. Chem. 268 (1993) 15523-15530
159. Muller G., Ayoub M., Storz P., Rennecke J., Fabbro D., and Pfizenmaier K. PKC zeta is a molecular switch in signal transduction of TNF-alpha, bifunctionally regulated by ceramide and arachidonic acid. EMBO J. 14 (1995) 1961-1969
160. Grassme H., Bock J., Kun J., and Gulbins E. Clustering of CD40 ligand is required to form a functional contact with CD40. J. Biol. Chem. 277 (2002) 30289-30299
161. Grassme H., Jekle A., Riehle A., Schwarz H., Berger J., Sandhoff K., Kolesnick R., and Gulbins E. CD95 signaling via ceramide-rich membrane rafts. J. Biol. Chem. 276 (2001) 20589-20596
162. Grassme H., Jendrossek V., Bock J., Riehle A., and Gulbins E. Ceramide-rich membrane rafts mediate CD40 clustering. J. Immunol. 168 (2002) 298-307
163. Cremesti A.E., Goni F.M., and Kolesnick R. Role of sphingomyelinase and ceramide in modulating rafts: do biophysical properties determine biologic outcome?. FEBS Lett. 531 (2002) 47-53
164. Holopainen J.M., Subramanian M., and Kinnunen P.K. Sphingomyelinase induces lipid microdomain formation in a fluid phosphatidylcholine/sphingomyelin membrane. Biochemistry 37 (1998) 17562-17570
165. Hanissian S.H., and Geha R.S. Jak3 is associated with CD40 and is critical for CD40 induction of gene expression in B cells. Immunity 6 (1997) 379-387
166. Veiga M.P., Arrondo J.L., Goni F.M., and Alonso A. Ceramides in phospholipid membranes: effects on bilayer stability and transition to nonlamellar phases. Biophys. J. 76 (1999) 342-350
167. Pannu R., Singh A.K., and Singh I. A novel role of lactosylceramide in the regulation of tumor necrosis factor alpha-mediated proliferation of rat primary astrocytes. Implications for astrogliosis following neurotrauma. J. Biol. Chem. 280 (2005) 13742-13751
168. Mattson M.P., Goodman Y., Luo H., Fu W., and Furukawa K. Activation of NF-kappaB protects hippocampal neurons against oxidative stress-induced apoptosis: evidence for induction of manganese superoxide dismutase and suppression of peroxynitrite production and protein tyrosine nitration. J. Neurosci. Res. 49 (1997) 681-697
169. Fridovich I. Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64 (1995) 97-112
170. Marklund S.L. Extracellular superoxide dismutase and other superoxide dismutase isoenzymes in tissues from nine mammalian species. Biochem. J. 222 (1984) 649-655
171. Sandstrom J., Carlsson L., Marklund S.L., and Edlund T. The heparin-binding domain of extracellular superoxide dismutase C and formation of variants with reduced heparin affinity. J. Biol. Chem. 267 (1992) 18205-18209
172. Jung O., Marklund S.L., Geiger H., Pedrazzini T., Busse R., and Brandes R.P. Extracellular superoxide dismutase is a major determinant of nitric oxide bioavailability: in vivo and ex vivo evidence from ecSOD-deficient mice. Circ. Res. 93 (2003) 622-629
173. Didion S.P., Ryan M.J., Didion L.A., Fegan P.E., Sigmund C.D., and Faraci F.M. Increased superoxide and vascular dysfunction in CuZnSOD-deficient mice. Circ. Res. 91 (2002) 938-944
174. Fukai T., Galis Z.S., Meng X.P., Parthasarathy S., and Harrison D.G. Vascular expression of extracellular superoxide dismutase in atherosclerosis. J. Clin. Invest. 101 (1998) 2101-2111
175. Li Y., Huang T.T., Carlson E.J., Melov S., Ursell P.C., Olson J.L., Noble L.J., Yoshimura M.P., Berger C., Chan P.H., Wallace D.C., and Epstein C.J. Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase. Nat. Genet. 11 (1995) 376-381
176. Pahan K., Dobashi K., Ghosh B., and Singh I. Induction of the manganese superoxide dismutase gene by sphingomyelinase and ceramide. J. Neurochem. 73 (1999) 513-520
177. Manna S.K., Zhang H.J., Yan T., Oberley L.W., and Aggarwal B.B. Overexpression of manganese superoxide dismutase suppresses tumor necrosis factor-induced apoptosis and activation of nuclear transcription factor-kappaB and activated protein-1. J. Biol. Chem. 273 (1998) 13245-13254
178. Reth M. Hydrogen peroxide as second messenger in lymphocyte activation. Nat. Immunol. 3 (2002) 1129-1134
179. Rhee S.G., Chang T.S., Bae Y.S., Lee S.R., and Kang S.W. Cellular regulation by hydrogen peroxide. J. Am. Soc. Nephrol. 14 (2003) S211-S215
180. Traber D.L., Adams Jr. T., Sziebert L., Stein M., and Traber L. Potentiation of lung vascular response to endotoxin by superoxide dismutase. J. Appl. Physiol. 58 (1985) 1005-1009
181. Kannan R., Jin M., Gamulescu M.A., and Hinton D.R. Ceramide-induced apoptosis: role of catalase and hepatocyte growth factor. Free Radic. Biol. Med. 37 (2004) 166-175
182. Sheikh F.G., Pahan K., Khan M., Barbosa E., and Singh I. Abnormality in catalase import into peroxisomes leads to severe neurological disorder. Proc. Natl. Acad. Sci. USA 95 (1998) 2961-2966
183. Singh I. Peroxisomal fatty acid oxidation and cellular redox. Methods Enzymol. 352 (2002) 361-372
184. Baumgart E., Vanhorebeek I., Grabenbauer M., Borgers M., Declercq P.E., Fahimi H.D., and Baes M. Mitochondrial alterations caused by defective peroxisomal biogenesis in a mouse model for Zellweger syndrome (PEX5 knockout mouse). Am. J. Pathol. 159 (2001) 1477-1494
185. Suzuki K. Twenty five years of the "psychosine hypothesis": a personal perspective of its history and present status. Neurochem. Res. 23 (1998) 251-259
186. Khan M., Haq E., Giri S., Singh I., and Singh A.K. Peroxisomal participation in psychosine-mediated toxicity: implications for Krabbe's disease. J. Neurosci. Res. 80 (2005) 845-854
187. Kajita K., Mune T., Kanoh Y., Natsume Y., Ishizawa M., Kawai Y., Yasuda K., Sugiyama C., and Ishizuka T. TNFalpha reduces the expression of peroxisome proliferator-activated receptor gamma (PPARgamma) via the production of ceramide and activation of atypical PKC. Diabetes Res. Clin. Pract. 66 Suppl. 1 (2004) S79-S83
188. Cimini A., Bernardo A., Cifone M.G., Di Marzio L., and Di Loreto S. TNFalpha downregulates PPARdelta expression in oligodendrocyte progenitor cells: implications for demyelinating diseases. Glia 41 (2003) 3-14
189. Yasmineh W.G., Parkin J.L., Caspers J.I., and Theologides A. Tumor necrosis factor/cachectin decreases catalase activity of rat liver. Cancer Res. 51 (1991) 3990-3995