Compositions and methods for the treatment and prevention of cancer, angiogenesis, and inflammation

Patent Citations (86)

Non-Patent Literature (264)

• Granziero, Krajewski, Farness, Yuan, Courtney, Jackson, Peterson, and Vitiello. Adoptive immunotherapy prevents prostate cancer in a transgenic animal model. European Journal of Immunology, 1999. vol. 29, pp. 1127-1138.Examiner
• Byers. What can randomized control trials tell us about nutrition and cancer prevention? CA Cancer Journal, 1999. vol. 49, pp. 353-361.Examiner
• Wright, Shin, and Morrison. Genetically engineered antibodies: progress and prospects. Critical Reviews in Immunology, 1992. vol. 12, pp. 125-168.Examiner
• MSNBC News Services. Mixed results on new cancer drug. Nov. 9, 2000.Examiner
• Gura. Systems for identifying new drugs are often faulty. Science, 1997. vol. 278, pp. 1041-1042.Examiner
• Sabbadini. Targeting sphingosine-1-phosphate for cancer therapy. British Journal of Cancer, 2006. vol. 95, pp. 1131-1135.Examiner
• Forni, Lollini, Musiani, and Colombo. Immunoprevention of cancer: is the time ripe? Cancer Research, 2000. vol. 60, pp. 2571-2575.Examiner
• De Gruijl and Curiel. Cancer vaccine strategies get bigger and better. Nature Medicine, 1999. vol. 5, pp. 1124-1125.Examiner
• Chatterjee, Foon, and Kohler. Idiotypic antibody immunotherapy of cancer. Cancer Immunology Immunotherapy, 1994. vol. 38, pp. 75-82.Examiner
• Bodey, Bodey, Siegel, and Kaiser. Failure of cancer vaccines: the significant limitations of this approach to immunotherapy. Anticancer Research, 2000. vol. 20, pp. 2665-2676.Examiner
• Abe et al., “Structural and stereochemical studies of potent inhibitors and glucosylceramide synthase and tumor cell growth,” J. Lipid Res. 36(3):611-621 (1995).Applicant
• Abe et al., “Glycosphingolipid depletion in Fabry disease lymphoblasts with potent inhibitors of glucosylceramide synthase,” Kidney Int. 57(2):446-454 (2000).Applicant
• Abe et al., “Use of Sulfobutyl Ether-Cyclodextrin as a Vehicle for D-threo-1-Phenyl-2-decanoylamino-3-morpholinopropanol-Related Glucosylceramide Synthase Inhibitors,” Anal. Biochem. 287(2):344-347 (2000).Applicant
• Ambati, “Age-related macular degeneration: etiology, pathogenesis, and therapeutic strategies,” Surv. Ophthalmol. 48(3):257-293 (2003) (Abstract Only).Applicant
• An et al., “Identification of cDNAs encoding two G protein-coupled receptors for lysosphingolipids,” FEBS Letts. 417(3):279-282 (1997).Applicant
• An et al., “Characterization of a Novel Subtype of Human G Protein-coupled Receptor for Lysophosphotatidic Acid,” J. Biol. Chem. 273(14):7906-7910 (1998).Applicant
• An et al., “Sphingosine 1-phosphate-induced cell proliferation, survival, and related signaling events mediated by G protein-coupled receptors Edg3 and Edg5,” J. Biol. Chem. 275(1):288-296 (2000).Applicant
• Ancellin et al., “Extracelluar export of sphingosine kinase-1 enzyme: Sphingosine 1 phosphate generation and the induction of angiogenic vascular maturation,” J. Biol. Chem. 277(8):6667-6675 (2001).Applicant
• Andrieu-Abadie et al., “L-camitine prevents doxorubicin-induced apoptosis of cardiac myocytes: role of inhibition of ceramide generation,” FASEB J. 13(12):1501-1510 (1999).Applicant
• Arenz et al., “Synthese des ersten selektiven irreverilben Inhibitors der neutralen Sphingomyelinase,” Angew Chem. 112:1498-1500 (2000) (GERMAN); “Synthesis of the First Selective Irreversible Inhibitor of Neutral Sphingomyelinase,” Angew. Chem. Int. Ed. 39(8):1440-1442 (2000) (English Equivalent).Applicant
• Arenz et al., “Manumycin A and its Analogues Are Irreversible Inhibitors of Neutral Sphingomyelinase,” Chem. Biochem. 2(2):141-143 (2001).Applicant
• Arenz et al., “Synthesis and Biochemical Investigation of Scyphostatin Analogues as Inhibitors of Neutral Sphingomyelinase,” Bioorg. Medicinal Chem. 9(11):2901-2904 (2001).Applicant
• Arenz et al., “Synthesis of the First Selective Irreversible Inhibitor of Neutral Sphingomyelinase,” Eur. J. Org. Chem. 2001(1):137-140 (2001).Applicant
• Ariga et al., “Role of Sphingolipid-mediated cell death in neurodegenerative diseases,” J. Lip. Res. 39(1):1-16 (1998).Applicant
• Bajjalieh at al., “Ceramide Kinase,” Methods Enzymol. 311:207-215 (1999).Applicant
• Barbone et al., “Robotic Assay of Sphingomyelinase Activity for High Throughput Screening,” Meth. Enzymol. 311:168-176 (1999).Applicant
• Bawab et al., “Molecular Clonging and Characterization of a Human Mitochondrial Ceramidase,” J. Biol. Chem. 275(28):21508-21513 (2000).Applicant
• Bernardo et al., “Purification and Characterization of Magnesium-dependent Neutral Sphingomyelinase from Bovine Brain,” J. Biol. Chem. 275(11):7641-7647 (2000).Applicant
• Betto et al., “Sphingosylphosphocholine modulates the ryanodine receptor/calcium-release channel of cardiac sarcoplasmic reticulum memberances,” Biochem. J. 322(1):327-333 (1997).Applicant
• Bielawska et al., “(1S,2R)-D-erhthro-2-(N-My- ristoylamino) -1-phenyl-1-propanol as an Inhibitor of Ceramidase,” J. Biol. Chem. 271(21):12646-12654 (1996).Applicant
• Cain et al., “Therapeutic Strategies to Reduce TNF-a Mediated Cardiac Contractile Depression Following Ischemia and Reperfusion,” J. Mol. Cell. Cardiol. 31(5):931-947 (1999).Applicant
• Boudker et al., “Detection and Characterization of Ceramide-1-phosphate Phosphatase Activity in Rat Liver Plasma Membrane,” J. Biol. Chem. 268(29):22150-22155 (1993).Applicant
• Brady et al., “The metabolism of sphingomyelin. II. Evidence of an enzymatic deficiency in Niemann-Pick disease,” Proc. Natl. Acad. Sci. USA 55(2):366-369 (1966).Applicant
• Brindley et al., “Analysis of Ceramide 1-phosphate and Sphingosine-1-phosphate Phosphatase Activities,” Methods Enzymol. 311:233-244 (1999).Applicant
• Brownlee, “Intracellular signalling: sphingosine-1 -phosphate branches out,” Current Biol. 11(13):R535-R538 (2001).Applicant
• Burton et al., “Human antibodies from combinatorial libraries,” Adv. Immunol. 57:191-280 (1994).Applicant
• Cain et al., “Therapeutic Strategies to Reduce TNF-a Mediated Cardiac Contractile Depression Following Ischemia and Reperfusion,” J. Mol. Celt Cardiol. 31(5):931-947 (1999).Applicant
• Caligan et al., “A High-Performance Liquid Chromatographic Method to Measure Sphingosine 1-Phosphate and Related Compounds from Sphingosine Kinase Assays and Other Biological Samples,” Anal. Biochem. 281(1):36-44 (2000).Applicant
• Chan et al., “Ceramide Path in Human Lung Cell Death,” Am. J. Respir. Cell Mol. Biol. 22(4):460-468 (2000).Applicant
• Chan et al., “Purification and Characterization of Neutral Sphingomyelinase from Helicobacter pylori,” Biochemistry 39(16):4838-4845 (2000).Applicant
• Chatterjee, “Sphingolipids in Atherosclerosis and Vascular Biology,” Arterioscler. Throm. Vasc. Biol. 18(10):1523-1533 (1998).Applicant
• Chatterjee, “Neutral Sphingomyelinase,” Adv. Lip. Res. 26:25-48 (1993).Applicant
• Chatterjee, “Neutral Sphingomyelinase: past, present, and future,” Chem. Phys. Lipids 102(1):79-96 (1999).Applicant
• Chatterjee et al., “Molecular Cloning, Characterization, and Expression of a Novel Human Neutral Sphingomyelinase,” J. Biol. Chem. 274(52):37407-37412 (1999).Applicant
• Chau et al., “Synthesis of Simple Aryl Neutral Sphingomyelinase Inhibitors,” Am. Chem. Soc. (2001) (Abstract Only).Applicant
• Chun, “Lysophospholipid receptors: implications for neural signaling,” Crit. Rev. Neuro. 13(2):151-168 (1999).Applicant
• Chun et al., “A Growing Family of Receptor Genes for Lysophosphatidic Acid (LPA) and other Lysophospholipids (LPs),” Cell Biochem. Biophys. 30(2):213-242 (1999).Applicant
• Cordis et al:, “HPTLC analysis of sphingomylein, ceramide and sphingosine in ischemic/reperfused rat heart,” J. Pharm. Biomed. Anal. 16(7):1189-1193 (1998).Applicant
• Cuvlilier et al., “Suppression of ceramide-mediated programmed cell death by sphingosine-1-phosphate,” Nature 381(6585):800-803 (1996).Applicant
• Dickson et al., “Serine Palmitoyltransferase,” Methods Enzymol. 311:3-9 (1999).Applicant
• Edsall et al., “N, N-Dimethylsphingosine is a potent competitive inhibitor of sphingosine kinase but not of protein kinase C: modulation of cellular levels of sphingosine 1-phosphate and ceramide,” Biochem. 37(37):12892-12898 (1998).Applicant
• Edson et al., “The Aminoglycosides,” Mayo Clin. Proc. 74(5):519-528 (1999).Applicant
• Eichler et al., “Peptide, peptidomimetic, and organic synthetic combinatorial libraries,” Med. Res. Rev. 15(6):481-496 (1995).Applicant
• Fensome et al., “A Neutral Magnesium-dependent Sphingomyelinase Isoform Associated with Intracellular Membranes and Reversibly Inhibited by Reactive Oxygen Species,” J. Biol. Chem. 275(2):1128-1136 (2000).Applicant
• Fujii et al., “Mg2+ binding and catalytic function of sphingomyelinase from Bacillus cereus,” J. Biochem (Tokyo) 124(6):1178-1187 (1998).Applicant
• Fukushima et al., “A single receptor encoded by vzg-1llpA1/edg-2 couples to G proteins and mediates multiple cellular responses to lysophosphatidic acid,” Proc. Natl. Acad. Sci. USA 95(11):6151-6156 (1998).Applicant
• Furneisen et al., “Enzymological properties of the LPP1-encoded lipid phosphatase from Saccharomyces cerevisiae” Biochim. Biophys. Acta 1484(1):71-82 (2000).Applicant
• Garcia-Ruiz, “Human placenta sphingomyelinase, an exogenous acidic pH-optimum sphingomyelinase, induces oxidative stress, glutathione depletion, and apoptosis in rat hepatocytes,” Hepatology 32(1):56-65 (2000).Applicant
• Gates et al., “Serum amyloid p component: its role in platelet activation stimulated by sphingomyelinase d purified from the venom of the brown recluse spider (Loxosceles reclusa),” Toxicon. 28(11):1303-1315 (1990).Applicant
• Gatt et al., “Niemann Pick disease: presence of the magnesium-dependent sphingomyelinase in brain of the infantile form of the disease,” J. Neurochem. 31(2):547-550 (1978).Applicant
• Gavrilenko et al., “Nucleotide sequence of phospholipase C and sphingomyelinase genes from Bacillus cereus BKM-B164,” Bioorg. Khim. 19(1):133-138 (1993).Applicant
• Geeraert et al., “Conversion of dihydroceramide into ceramide: involvement of a desaturase,” Biochem. J. 327(125):125-132 (1997).Applicant
• Ghosh et al., “Effects of gentamicin on sphingomyelinase activity in cultured human renal proximal tubular cells,” J. Biol. Chem. 262(26):12550-12556 (1987).Applicant
• Ghosh et al., “Identification, partial purification, and localization of a neutral sphingomyelinase in rabbit skeletal muscle: Neutral sphingomyelinase in skeletal muscle,” Mol. Cell. Biochem. 189(1-2):161-168 (1998).Applicant
• Gilmore et al., “A Bacillus cereus cytolytic determinant, cereolysin AB, which comprises the phospholipase C and sphingomyelinase genes: a nucleotide sequence and genetic linkage,” J. Bacterial. 171(2):744-753 (1989).Applicant
• Glickman et al., “Molecular Cloning, Tissue-Specific Expression, and Chromosomal Localization of a Novel Nerve Growth Factor-Regulated G-Protein-Coupled Receptor, nrg-1,” Mol. Cel. Neurosci. 14(2):141-152 (1999).Applicant
• Goetzl et al., “Diversity of cellular receptors and functions for the lysophospholipid growth factors lysophosphatidic acid and sphingosine 1-phosphate,” Faseb J. 12(15)1589-1598 (1998).Applicant
• Goetzl et al., “Eicosanoids and Other Bioactive Lipids in Cancer, Inflammation, and Radiation Injury, 4. 38: A Subfamily of G Protein-Coupled Cellular Receptors for Lysophospholipids and Lysosphingolipids, Introduction: The Biochemistry and Biology of Lipid Phosphoric Acids,” Adv. Exp. Med. Biol. 469:259-264 (1999).Applicant
• Gonda, et al., “The novel sphingosine 1-phosphate receptor AGR16 is coupled via pertussis toxin-sensitive and -insensitive G-proteins to multiple signalling pathways,” Biochem. J. 337(Part 1):67-75 (1999).Applicant
• Gonzalez-Zorn et al., “The smcL gene of Listeria ivanovii encodes a sphingomyelinase C that mediates bacterial escape from the phagocytic vacuole,” Mol. Microbial. 33(3):510-523 (1999).Applicant
• Graler et al., “EDG6, a Novel G-Protein-Coupled Receptor Related to Receptors for Bioactive Lysophospholipids, Is Specifically Expressed in Lymphoid Tissue, ” Genomics 53(2):164-169 (1998).Applicant
• Gunther, “Myocardial contractility after infarction and carnitine palmitoyltransferase I inhibition in rats,” Eur. J. Pharma. 406(1):123-126 (2000).Applicant
• Hakogi et al., “Stereocontrolled synthesis of a sphingomyelin methylene analogue as a sphingomyelinase inhibitor,” Org. Lett. 2(17):2627-2629 (2000).Applicant
• Hanada et al., “Specificity of Inhibitors of Seine Palmitoyltransferase (SPT), a Key Enzyme in Sphingolipid Biosynthesis in Intact Cells: A novel evaluation system using an SPT-defective mammalian cell mutant,” Biochem. Pharmacol. 59(10):1211-1216 (2000).Applicant
• Hannun et al., “Functions of Sphingolipids and Sphingolipid Breakdown Products in Cellular Regulation,” Science 243(4890):500-507 (1989).Applicant
• Hannun et al.., “The Sphingomyelin Cycle: A Prototypic Sphingolipid Signaling Pathway,” Adv. Lipid Res. 25:27-41. (1993).Applicant
• Hannun, “Functions of Ceramide in Coordinating Cellular Responses to Stress,” Science 274(5294):1855-1859 (1996).Applicant
• Hannun at al, “Ceramide in the eukaryotic stress response,” Trends Cell Biol. 10(2):73-80 (2000).Applicant
• He et al., “A Fluorescence-Based High-Performance Liquid Chromatography Assay to Determine Acid Ceramidase Activity,” Anal. Biochem. 274(2):264-269 (1999).Applicant
• Heringdorf et al., “Stimulation of intracellular sphingosine-1 -phosphate production by G-protein-coupled sphingosine-1 -phosphate receptors,” Eur. J. Pharmacol. 414(2-3):145-154 (2001).Applicant
• Hernandez et al., “Rapid Activation of Neutral Sphingomyelinase by Hypoxia-Reoxygenation of Cardiac Myocytes,” Circ. Res. 86(2):198-204 (2000).Applicant
• Hetland et al., “Phospholipase C from Bacillus cereus has sphingomyelinase activity,” Scand. J. Clin. Lab. Invest. 42(1):57-61 (1982).Applicant
• Higuchi et al., “Acidic sphingomyelinase-generated ceramide is needed but not sufficient for TNF-induced apoptosis and nuclear factor-kappa B activation,” J. Immunol. 157(1):297-304 (1996).Applicant
• Hinkovska-Glacheva et al., “Activation of a Plasma Membrane-Associated Neutral Sphingomyelinase and Concomitant Ceramide Accumulation During IgG-Dependent Phagocytosis in Human Polymorphonuclear Leukocytes,” Blood 91(12):4761-4769 (1998).Applicant
• Hise et al., “Fatty Acyl Chain Composition in the Determination of Renal Membrane Order,” J. Clin. Invest. 77(3):768-773 (1986).Applicant
• Hla et al., “An Abundant Transcript Induced in Differentiating Human Endothelial Cells Encodes a Polypeptide with Structural Similarities to G-Protein-coupled Receptors,” J. Biol. Chem. 265(16):9308-9313 (1990).Applicant
• Hofmann et al., “Cloning and characterization of the mammalian brain-specific, Mg2+-dependent neutral sphingomyelinase,” Proc. Natl. Acad. Sci. USA 97(11):5895-5900 (2000).Applicant
• Hofstadler et al., “Multiplexed Screening of Neutral Mass-Tagged RNA Targets against Ligand Libraries with Electrospray Ionization FTICR MS: a Paradigm for High-Throughput Affinity Screening,” Anal. Chem. 71(16):3436-3440 (1999).Applicant
• Holopainen et al., “Sphingomyelinase Activity. Associated with Human Plasma Low Density Lipoprotein,” J Biol. Chem. 275(22):16484-16489 (2000).Applicant
• Horn et al., “Sphingofungins E and F: Novel Serinepalmitoyl Trans-Ferase Inhibitors From Paecilomyces variotii,” J. Antibiot. (Tokyo) 45(10):1692-1696 (1992).Applicant
• Hoye et al., “Synthesis (and Alternative Proof of Configuration) of the Scyphostatin C(1′)-C(20′) Trienoyl Fragment,” Organic Letts. 2(10):1481-1483 (2000).Applicant
• Hudson, “Recombinant antibody fragments,” Curr. Op. Biotechnol. 9(4):395-402 (1999).Applicant
• Humpf et al., “Acylation of naturally occurring and synthetic 1-deoxysphinganines by ceramide synthase. Formation of N-palmitoyl-aminopentol produces a toxic metabolite of hydrolyzed fumonisin, AP1, and a new category of ceramide synthase inhibitor,” J. Biol. Chem. 273(30):19060-19064 (1998).Applicant
• Huwiler et al., “Physiology and pathophysiology of sphingolipid metabolism and signling,” Biochim. Biophys. Acta 1485(2-3):63-99 (2000).Applicant
• Igarashi, “Functional Roles of Sphingosine, Sphingosine 1-Phosphate, and Methylsphingosines: In Regard to Membrane Sphingolipid Signaling Pathways,” J. Biochem. 122(6):1080-1087 (1997).Applicant
• Ikezawa et al., “Studies on Sphingomyelinase of Bacillus cereus. 1. Purification and Properties,” Biochim. Biophys. Acta 528(2):247-256 (1978).Applicant
• Im et al., “Characterization of a novel sphingosine 1-phosphate receptor, Edg-8,” J. Biol. Chem. 275(19):14281-14286 (2000).Applicant
• Im et al., “Molecular Cloning and Characterization of a Lysophosphatidic Acid Receptor, Edg-7, Expressed in Prostate,” Mol. Pharmacol. 57(4):753-759 (2000).Applicant
• Izuhara et al., “Studies toward the Total Synthesis of Scyphostatin: First Entry to the Highly Functionalized Cyclohexenone Segment,” Organic Lett. 3(11):1653-1656 (2001).Applicant
• Jimbo et al., “Development of a New Inhibitor of Glucosylceramide Synthase,” J. Biochem. 127(3):485-491 (2000).Applicant
• Johansen et al., “Bacillus cereus strain SE-1: nucleotide sequence of the sphingomyelinase C gene,” Nucl. Acids Res. 16(21)10370 (1998).Applicant
• Jonghe et al., “Structure-Activity Relationship of Short-Chain Sphingoid Bases As Inhibitors of Sphingosine Kinase”, Bioorg. Medicinal Chem. Lett. 9(21):3175-3180 (1999).Applicant
• Kajstura et al., “Apoptotic and Necrotic Myocyte Cell Deaths Are Independent Contributing Variables of Infarct Size in Rats,” Lab. Invest. 74(1):86-107 (1996).Applicant
• Kanfer et al., “The Metabolism of Sphingomyelin. I. Purification and properties of a sphingomyelin-cleaving enzyme from rat liver tissue,” J. Biol. Chem. 241(5):1081-1084 (1966).Applicant
• Katircioglu et al., “Myocardial preservation in acute coronary artery occlusion with coronary sinus retroperfusion and camitine,” J. Cardiovasc. Surg. (Torino) 41(1):45-50 (1999.Applicant
• Kay et al., “Identification of enzyme inhibitors from phage-displayed combinatorial peptide libraries,” Comb. Chem. High Throughput Screen 4(7):535-543 (2001).Applicant
• Kester, “Sphingolipid Metabolites and the Cellular Phenotype,” Trends Glycosci. Glycotechnol. 9(50):447-460 (1997).Applicant
• Kihara et al,, “Direct Measurement of Changes in Intercellular Calcium Transients During Hypoxia, Ischemia, and Reperfusion of the Intact Mammalian Heart,” Circ. Res. 65(4):1029-1044 (1989).Applicant
• Kimura et al., “Two Novel Xenopus Homologs of Mammalian LPA1/EDG-2 Function as Lysophosphatidic Acid Receptors in Xenopus oocytes and Mammalian Cells,” J. Biol. Chem. 276(18):15208-15215 (2001).Applicant
• Kita et al., “Reverse hydrolysis reaction of a recombinant alkaline ceramidase of Pseudomonas aeruginosa,” Biochim. Biophys. Acta 1485(2-3):111-120 (2000).Applicant
• Kohama et al., “Molecular cloning and functional characterization of murine sphingosine kinase,” J. Biol. Chem. 273(37):23722-23728 (1998).Applicant
• Kolesnick et al., “Characterization of a Ceramide Kinase Activity from Human Leukemia (HL-60) Cells: Separation From Diacylglycerol Kinase Activity,” J. Biol. Chem. 265(31):18803-18808 (1990).Applicant
• Kolesnick, “The thereapeutic potential of modulating the ceramide/sphingomyelin pathway,” J. Clin. Inv. 110(1):3-8 (2002).Applicant
• Krown et al., “Tumor necrosis factor alpha-induced apoptosis in cardiac myocytes. Involvement of the sphingolipid signaling cascade in cardiac cell death,” J. Clin. Invest. 98(12):2854-2865 (1996).Applicant
• Kubota et al., “Accumulation of ceramide in ischemic human brain of an acute case of cerebral occlusion,” Japan J. Exp. Med. 59(2):59-64 (1989).Applicant
• Kubota et al., “Sphingomyelin changes in rat cerebral cortex during focal ischemia,” Neurol. Res. 18(4):337-341 (1996).Applicant
• Lanterman et al., “Characterization of sphingosine kinase (SK) activity in Saccharomyces cerevisiae and isolation of SK-deficient mutants,” Biochem. J. 332(Part 2):525-531 (1998).Applicant
• Lee et al., “Effect of Ischemia on Calcium-Dependent Fluorescence Transients in Rabbit Hearts Containing Indo 1. Correlation with Monophasic Action Potentials and Contraction,” Circ. 78(4):1047-1059 (1988).Applicant
• Lee et al., “Cell-cycle-dependent changes in ceramide levels preceding retinoblastoma protein dephosphorylation in G2/M,” Biochem. J. 334(Part 2):457-461 (1998).Applicant
• Lee et at, “Improved Inhibitors of Glucosylceramide Synthase,” J. Bio. Chem. 274(21):14662-14669 (1999).Applicant
• Lee et al., “Sphingosine 1-Phosphate Induces Angiogenesis: Its Angiogenic Action and Signaling Mechanism in Human Umbilical Endothelial Cells,” Biochem. Biophys. Res. Commun. 264(3):743-750 (1999).Applicant
• Lee et al., “Lysophosphatidic acid and sphingosine 1-phosphate stimulate endothelial cell wound healing,” Am. J. Physiol. Cell Physiol. 278(3):C612-C618 (2000).Applicant
• Levade, et al., “Sphingomyelinases and Niemann-Pick disease,” J. Clin. Chem. Clin. Biochem. 24(4):205-220 (1986).Applicant
• Li et al., “The Human Acid Ceramidase Genes (ASAH): Structure, Chromosomal Location, Mutation Analysis, and Expression,” Genomics 62(2):223-231 (1999).Applicant
• Liliom at al, “Sphingosylphosphocholine is a naturally occurring lipid mediator in blood plasma: a possible role in regulating cardiac function via sphingolipid receptors,” Biochem. J. 355(Part 1):189-197(2001).Applicant
• Lin et al., “Identification of neutral and acidic sphingomyelinases in Helicobacter pylori,” FEBS Lett. 423(2):249-253 (1998).Applicant
• Linn et al., “Regulation of de nova sphingolipid biosynthesis and the toxic consequences of its disruption,” Biochem. Soc. 29(Part 6):831-835 (2001).Applicant
• Lister et al., “Interaction of sphingomyelinase with sphingomyelin analogs modified at the G1 and C-3 positions of the sphingosine backbone,” Biochim. Biophys. Acta 1256(1):25-30 (1995).Applicant
• Little at al, “Surface display of antibodies,” Biotechn. Adv. 12(3):539-555 (1994).Applicant
• Liu et al., “Inhibition of the neutral magnesium-dependent sphingomyelinase by glutathione,” J. Biol. Chem. 272(26):16281-16287 (1997).Applicant
• Liu et al., “Purification and Characterization of a Membrane Bound Neutral pH Optimum Magnesium-dependent and Phosphatidylserine-stimulated Sphingomyelinase from Rat Brain,” J. Biol. Chem. 273(51):34472-34479 (1998).Applicant
• Liu et al., “Glutathione regulation of neutral sphingomyelinase in tumor necrosis factor-alpha-induced cell death,” J. Biol. Chem. 273(18):11313-11320 (1998).Applicant
• Liu at al, “Advances in the signal transduction of ceramide and related sphingolipids,” Crit. Rev. Clin. Lab. Sci. 36(6):511-573 (1999).Applicant
• Liu et al., “Molecular Cloning and Functional Characterization of a Novel Mammalian Sphingosine Kinase Type 2 Isoform,” J. Biol. Chem. 275(26):19513-19520 (2000).Applicant
• Liu et al., “Sphingomyelinase Assay Using Radiolabeled Substrate,” Meth. Enzymol. 311:164-167 (2000).Applicant
• Lochhead at al, “Fluorinated anesthetic exposure “activates” the renal cortical sphingomyelinase cascade,” Kidney Int. 54(2):373-381 (1998).Applicant
• Luberto et al., “Sphingomyelin synthase, a potential regulator of intracellular levels of ceramide and diacylglycerol during SV40 transformation. Does sphingomyelin synthase account for the putative phosphatidylcholine-specific phopholipase C?,” J. Biol. Chem. 273(23):14550-14559 (1998).Applicant
• Luberto at al, “Sphingolipid Metabolism in the Regulation of Bioactive Molecules,” Lipids 34(Supp. 1):S5-S11 (1999).Applicant
• Lynch at al, “Life on the edg,” Trends Pharmacol. Sci. 20(12):473-475 (1999).Applicant
• Magnelli et al., “BCL-2 Overexpression Abolishes Early Calcium Waving Preceding Apoptosis in NIH-3T3 Murine,” Biochem. Biophys. Res. Comm. 204(1):84-90 (1994).Applicant
• Mandala et al., “Inhibition of Serine Palmitoyl-Transferase Activity by Lipoxamycin,” J. Antibiot. (Tokyo) 47(3):376-379 (1994).Applicant
• Mandala et al., “The Discovery of Australifungin, a novel Inhibitor of Sphinganine N-Acyltransferase from Sporormiella australis. Producing Organism, Fermentation, Isolation, and Biological Activity,” J. Antibiot. (Tokyo) 48(5):349-356 (1995).Applicant
• Mandala et al., “Khafrefungin, a novel inhibitor of sphingolipid synthesis,” J. Biol. Chem. 272(51):32709-32714 (1997).Applicant
• Mandala et al., “Viridiofungins, Novel Inhibitors of Sphingolipid Synthesis,” J. Antibiot. (Tokyo) 50(4):339-343 (1997).Applicant
• Mandala et al., “Sphingoid base 1-phosphate phosphatase: a key regulator of sphingolipid metabolism and stress response,” Proc. Natl. Acad. Sci. USA 95(1 ):150-155 (1998).Applicant
• Mandala et al., “Isolation and Characterization of Novel Inhibitors of Sphingolipid Synthesis: Australifungin, Viridiofungins, Rustmicin, and Khafrefungin,” Methods Enzymol. 311:335-348 (1999).Applicant
• Mandala et al., “Molecular cloning and characterization of a lipid phosphohydrolase that degrades sphingosine-1-phosphate and induces cell death,” Proc. Natl. Acad. Sci. USA 97(14):7859-7864 (2000).Applicant
• Mandala et al., “Sphingosine-1-Phosphate Phosphatases,” Prostaglandins & Other Lipid Mediators 64(1-4):143-156 (2001).Applicant
• Mao et al., “Molecular cloning and characterization of SCaMPER, a Sphingolipid Ca2+ release-mediating protein from endoplasmic reticulum,” Proc. Natl. Acad. Sci. USA 93(5):1993-1996 (1996).Applicant
• Mao et al., “Cloning of an Alkaline Ceramidase from Saccharomyces cerevisiae: An Enzyme with Reverse (CoA-Independent) Ceramide Synthase Activity,” J. Biol. Chem. 275(10):6876-6884 (2000).Applicant
• Mao et al., “Cloning and Characterization of a Saccharomyces cerevisiae Alkaliine Ceramidase with Specificity for Dihydroceramide,” J. Biol. Chem. 275(40):31369-31378 (2000).Applicant
• Mao et al., “Cloning and Characterization of a Novel Human Alkaline Ceramidase: A Mammalian Enzyme That Hydrolyzes Phytoceramide,” J. Biol. Chem. 276(28):26577-26588 (2001).Applicant
• Marks et al., “Methods for Studying Glucosylceramide Synthase,” Methods Enzymol.311:50-59 (1999).Applicant
• Martin et al., “Neutral Magnesium-Dependent Sphingomyelinase from Liver Plasma Membrane: Purification and Inhibition by Ubiquinol,” J. Bioenerg. Biomember. 33(2):143-153 (2001).Applicant
• Meacci et al., “Receptor-mediated activation of phospholipase D by sphingosine 1-phosphate in skeletal muscle C2C12 cells: A role for protein kinase C,” FEBS Lett. 457(2):184-188 (1999).Applicant
• Meldrum, “Tumor necrosis factor in the heart” Am. J. Physiol. 274(3):R577-R595 (1998).Applicant
• Melendez et al., “Human sphingosine kinase: molecular cloning, functional characterization and tissue distribution,” Gene 251(1):19-26 (2000).Applicant
• Meroni et al., “Effect of N-Acetylsphingosine (C2) and the Ceramidase Inhibitor (1S,2R)-D-erythro-2-(n-myristoylamino)-1 phenyl-1-propanol on the Regulation of Sertoli Cell Function,” J. Androl. 20(5):619-625 (1999).Applicant
• Merrill et al., “Activities of serine palmitoyltransferase (3-ketosphinganine synthase) in microsomes from different rat tissues,” J. Lipid Res. 26(5):617-622 (1993) .Applicant
• Michel et al., “Characterization of Ceramide Synthesis. A Dihydroceramide Desaturase Introduces the 4,5-Trans-Double Bond of Sphingosine at the Level of Dihydroceramide,” J. Biol. Chem. 272(36):22432-22437 (1997).Applicant
• Milstien et at, “Targeting sphingosine-1-phosphate: A novel avenue for cancer therapeutics,” Cancer Cell. 9(3):148-150 (2006)(Abstract Only).Applicant
• Mingeot-Leclercq et al., “Aminoglycosides: activity and resistance,” Antimicrob. Agents Chemother. 43(4):727-737 (1999).Applicant
• Mingeot-Leclercq et al., “Aminoglycosides: nephrotoxicity,” Antimicrob. Agents Chemother. 43(5):1003-1012 (1999).Applicant
• Mitsutake et al., “Purification, Characterization, Molecular Cloning, and Subcellular Distribution of Neutral Ceramidase of Rat Kidney,” J. Biol. Chem. 276(28):26249-26259 (2001).Applicant
• Miyake, “Serine palmitoyltransferase is the primary target of a sphingosine-like immunosuppressant, ISP-1/myriocin,” Biochem. Biophys. Res. Commun. 211(2):396-403 (1995).Applicant
• Mohan et al., “Evidence that Neutral Sphingomyelinase of Cultured Murine Neuroblastoma Cells is Oriented Externally on the Plasma Membrane,” Biochem. Biophys. Acta 777(2):339-342 (1984).Applicant
• Mohler et al., “Soluble Tumor Necrosis Factor (TNF) Receptors Are Effective Therapeutic Agents in Lethal Endotoxemia and Function Simultaneously as Both TNF Carries and TNF Antagonists,” J. Immunol. 151(3):1548-1561 (1993).Applicant
• Nakajima et al., “Expression and characterization of Edg-1 receptors in rat cardiomyocytes: Calcium deregulation in response to sphingosine 1-phosphate,” Eur. J. Biochem. 267(18):5679-5686 (2000).Applicant
• Nakajima et al., Biophysical J. 78:319 A (2000).Applicant
• Napoli et al., “Ischaemic preconditioning of rat myocardium: effects on postischaemic coronary endothelium hypermaebility and microcirculatory damage,” J. Clin. Bas. Cardiol. 1(1):37-42 (1998).Applicant
• Nikolova-Karakashian et al., “Ceramidases,” Meth. Enzymol. 311:194-201 (1999).Applicant
• Ohta et al., “A possible role of sphingosine in induction of apoptosis by tumor necrosis factor-a in human neutrophils,” FEBS Lett. 355(3):267-270 (1994).Applicant
• Ohta et al., “Induction of apoptosis by sphingosine in human leukemic HL-60 cells: a possible endogenous modulator of apoptotic DNA fragmentation occurring during phorbol ester-induced differentiation,” Cancer Res. 55(3):691-697 (1995).Applicant
• Okamoto et al., “EDG1 Is a Functional Sphingosine-1-phosphate Receptor That Is Linked via a Gi/o to Multiple Signaling Pathways, Including Phospholipase C Activation, Ca2+ Mobilization, Ras-Mitogen-activated Protein Kinase Activation, and Adenylate Cyclase Inhibition,” J. Biol. Chem. 273(42):27104-27110 (1998).Applicant
• Okamoto et al., “EDG3 Is a Functional Receptor Specific for Sphingosine 1-Phosphate and Sphingosylphosphorylcholine with Signaling Characteristics Distinct from EDG1 and AGR16,” Biochem. Biophys. Res. Commun. 260(1):203-208 (1999).Applicant
• Okazaki et al., “Characteristics and partial purification of a novel cytosolic, magnesium-independent, neutral sphingomyelinase activated in the early signal transduction of 1 alpha,25-dihydroxyvitamin D3-induced HL-60 cell differentiation,” J. Biol. Chem. 269(6):4070-4077 (1994).Applicant
• Okino et al., “Molecular Cloning, Sequencing, and Expression of the Gene Encoding Alkaline Ceramidase from Pseudomonas aeruginosa: Cloning of A Ceramidase Homologue from mycobacterium Tuberculosis,” J. Biol. Chem. 274(51):36616-36622 (1999).Applicant
• Olivera et al., “Sphingosine-1-phosphate as second messenger in cell proliferation induced by PDGF and FCS mitogens,” Nature 365(6446):557-560 (1993).Applicant
• Olivera et al., “Assaying Sphingosine Kinase Activity,” Methods Enzymol. 311:215-223 (1999).Applicant
• Olshefski et al., “Glucosylceramide Synthase Inhibition Enhances Vincristine-Induced Cytotoxicity,” Int, J. Cancer 93(1):131-138 (2001).Applicant
• Oral et al., “Sphingosine mediates the immediate negative inotropic effects of tumor necrosis factor-alpha in the adult mammalian cardiac myocyte,” J. Biol. Chem. 272(8):4836-4842 (1997).Applicant
• Parrill et al., “Identification of Edg1 Receptor Residues That Recognize Sphingosine 1-Phosphate,” J. Biol. Chem. 275(50):39379-39384 (2000).Applicant
• Pitson et al., “Human sphingosine kinase: purification, molecular cloning and characterization of the native and recombinant enzymes,” Biochem J. 350(Part 2):429-441 (2000).Applicant
• Pitson et al., “Expression of a catalytically inactive sphingosine kinase mutant blocks agonist-induced sphingosine kinase activation. A dominant-negative sphingosine kinase,” J. Biol. Chem. 275(43):33945-33950 (2000).Applicant
• Presta et al., “Humanization of an Anti-Vascular Endothelial Growth Factor Monoclonal Antibody for the Therapy of Solid Tumors and Other Disorders,” Canc. Res. 57(20):4593-4599 (1997).Applicant
• Raag et al., “Single-chain Fvs,” FASEB J. 9(1):73-80 (1995).Applicant
• Rani et al., “Cell Cycle Arrest Induced by an Inhibitor of Glucosylceramide Synthase,” J. Biol. Chem. 270(6):2859-2867 (1995).Applicant
• Riley et al., “Alteration of tissue and serum sphinganine to sphingosine ratio: an early biomarker of exposure to fumonisin-containing feeds in pigs,” Toxicol. Appl. Pharmacol. 118(1):105-112 (1993).Applicant
• Riley et al., “Fermentation, partial purification, and use of serine palmitoyltransferase inhibitors from Isaria (= Cordyceps) sinclairii,” Meth. Enzymol. 311:348-361 (1999).Applicant
• Romiti et al., “Characterization of sphingomyelinase activity released by thrombin-stimulated platelets,” Mol. Cell. Biochem. 205(1-2):75-81 (2000).Applicant
• Runcie at al, “A Short and Efficient Route to Novel Scyphostatin Analogues,” Organic Lett. 3(21):3237-3239 (2001).Applicant
• Sabbadini et al., “Sphingosine is endogenous to cardiac and skeletal muscle,” Biochem. Biophys. Res. Comm193(2):752-758 (1993).Applicant
• Sabbadini et al., “The Mirf trial: predicting the incidence and severity of CAD using serum sphingolipids,” Circ. 102(18):ll699 (2000).Applicant
• Saint-Joanis et al., “Gene cloning shows the alpha-toxin of Clostridium perfringens to contain both sphingomyelinase and lecithinase activities,” Mol. Gen. Genet. 219(3):453-60 (1989).Applicant
• Saito et al., “Absolute Configuration of Scyphostatin,” Organic Letts 2(4):505-506 (2000).Applicant
• Sakai et al., “A devise for recording left ventricular contraction and electrocardiogram in nonworking isolated perfused rat heart,” Jpn J. Pharmacol. 28(2):223-229 (1978).Applicant
• Sawada et al., “Ordering of ceramide formation, caspase activation, and Bax/Bcl-2 expression during etoposide-induced apoptosis in C6 glioma cells,” Cell Death Differentiation 7(9):761-7672 (2000).Applicant
• Sato, “A new role of lipid receptors in vascular and cardiac morphogenesis,” J. Clin. Invest. 106(8):939-940 (2000).Applicant
• Sawai et al., “Function of the Cloned Putative Neutral Sphingomyelinase as Lyso-platelet Activating FactorPhospholipase C,” J. Biol. Chem. 274(53):38131-38139 (1999).Applicant
• Sawai et al., “Identification of ISC1 (YER019w) as Inositol Phosphosphingolipid Phospholipase C Saccharomyces cerevisiae,” J. Biol. Chem. 275(50):39793-39798 (2000).Applicant
• Schissel et al., “Zn2+-stimulated Sphingomyelinase Is Secreted by Many Cell Types and Is a Product of the Acid Sphingomyelinase Gene,” J. Biol. Chem. 271(31):18431-18436 (1996).Applicant
• Sergeyev et al., “Lipid Spectrum of the Myocardium of White Rats Exposed to Hypoxic Hypoxia,” Kosm. Biol. Aviakosm. Med. (Russian) 15(6):71-74 (1981).Applicant
• Shayman et al., “Glucosylceramide Synthase: Assay and Properties,” Methods Enzymol. 311:42-49 (1999).Applicant
• Shayman et al., “Inhibitors of Glucosylceramide Synthase,” Methods Enzymol. 311:373-387 (1999).Applicant
• Shinghal et al., “Ceramide 1-Phosphate Phosphatase Activity in Brain,” J. Neurochem. 61(6):2279-2285 (1993).Applicant
• Siehler et al., “Sphingosine 1-Phosphate Activates Nuclear Factor-kappa B through Edg Receptors: Activation Through Edg-3 and Edg-5, but not Edg-1, in Human Embryonic Kidney 293 Cells,” J. Biol. Chem. 276(52):48733-48739 (2001).Applicant
• Siess et al., “Lysophosphatidic Acid and Sphingosine 1-Phosphate: Two Lipid Villains Provoking Cardiovascular Diseases?” IUBMB Life 49(3):161-171 (2000).Applicant
• Smith et al., “Hypoxia, calcium fluxes, and inotropic state: Studies in cultured heart cells,” Am. Heart J. 103(4 Part 2):716-723 (1982).Applicant
• Smith et al., “Purified Fumonisin B1 Decreases Cardiovascular Function but does not Alter Pulmonary Capillary Permeability in Swine,” Toxicol. Sci. 56(1):240-249 (2000).Applicant
• Spence, “Sphingomyelinases,” Adv. Lipid Res. 26:3-23 (1993).Applicant
• Spence et al., “A new Zn2+-stimulated sphingomyelinase in fetal bovine serum,” J. Biol. Chem. 264(10):5358-5363 (1989).Applicant
• Spiegel et al., “Sphingolipid metabolism and cell growth regulation,” FASEB J. 10(12):1388-1397 (1996).Applicant
• Spiegel et al., “Review: Roles of Sphingosine-1-phosphate in Cell Growth, Differentiation, and Death,” Biochemistry (Mosc). 63(1):69-83 (1998).Applicant
• Spiegel et al., “Functions of a new family of sphingosine-1-phosphate receptors,” Biochim. Biophys. Acta 1484(2-3):107-116 (2000).Applicant
• Sucheck et al., “Combinatorial synthesis of aminoglycoside libraries,” Curr. Opin. Drug Disc. Develop. 4(4):462-470 (2001).Applicant
• Sugita at al, “Ceramidase and ceramide synthesis in human kidney and cerebellum. Description of a new alkaline ceramidase,” Biochim. Biophys. Acta 398(1):125-131 (1975).Applicant
• Sugiyama et al., “Sphingosine 1-phosphate induces sinus tachycardia and coronary vasoconstriction in the canine heart,” Cardiovasc. Res. 46(1):119-125 (2000).Applicant
• Sumnicht et al., “Lipid Composition of Transverse Tubular Membranes from Normal and Dystrophic Skeletal Muscle,” Arch. Biochem. Biophys. 215(2):628-637. (1982).Applicant
• Szulc et al., “A facile regioselective synthesis of sphingosine 1-phosphate and ceramide 1-phosphate,” Tetrahedron Lett. 41(41):7821-7824 (2000).Applicant
• Tamura et al., “Mass Production of Sphingomyelinase of Bacillus cereus by a Protein-Hyperproducing Strain, Bacillus brevis 47, and Its Purification,” J. Biochem. (Tokyo) 112(4):488-491 (1992).Applicant
• Tanaka et al., “Structural Elucidation of Scyphostatin, an Inhibitor of Membrane-Bound Neutral Sphingomyelinase,” J. Am. Chem. Soc. 199(33):7871-7872 (1997).Applicant
• Tani et al., “Purification and Characterization of a Neutral Ceramidase from Mouse Liver: A single Protein Catalyzes the Reversible Reaction in Which Ceramide is Both Hydrolyzed and Synthesized,” J. Biol. Chem. 275(5):3462-3468 (2000).Applicant
• Tazabekova et al., “Synthesis of sphingomyelin phosphonate analogues and preparation of an affinity sorbent for the sphingomyelinase purification,” Bioorg. Khim. 13(5):648-653 (1987).Applicant
• Tomita et al.., “Secondary structure of sphingomyelinase from Bacillus cereus,” J. Biochem. (Tokyo) 108(5):811-815 (1990).Applicant
• Torley et al., “A turbidometric assay for phospholipase C and sphingomyelinase,” Anal. Biochem. 222(2):461-464 (1994).Applicant
• Tosaka et al., “Sphingosine 1-phosphate contracts canine basilar arteries in vitro and in vivo: possible role in pathogenesis of cerebral vasospasm,” Stroke 32(12):2913-2919 (2001).Applicant
• Triola et al., “Synthesis of a Cyclopropene Analogue of Ceramide, a Potent Inhibitor of Dihydroceramide Desaturase,” Angew. Chem. Int. Ed. 40(10):1960-1962 (2001).Applicant
• Tsunoda et al., “Early Fumonisin B1 Toxicity in Relation to Disrupted Sphingolipid Metabolism in Male BALB/c Mice,” J. Biochem. Mol. Toxicol. 12(5):281-289 (1998).Applicant
• Uchida et al., “Alutenusin, a Specific Neutral Sphingomyelinase Inhibitor, Produced by Penicillium sp. FO-7436,” J. Antibiot. (Tokyo) 52(6):572-574 (1999).Applicant
• Urdal, “The Biochemistry of Tumor Associated Gangliotriosylceramide and the Use of This Glycolipid as a Target for Antibody Dependent, Avidin Mediated Drug Killing of Tumor Cells,” Dissertation Abstracts Int. 41(11B):4062-4063 (1980).Applicant
• Usta et al., “Structural Requirements of Ceramide and Sphingosine Based Inhibitors of Mitochondrial Ceramidase,” Biochemistry 40(32):9657-9668 (2000).Applicant
• Van Brocklyn et al., “Sphingosine 1-phosphate-induced cell rounding and neurite retraction are mediated by the G protein-coupled receptor H218,” J. Biol. Chem. 274(8):4626-4632 (1999).Applicant
• Van Veldhoven et al., “Sphingosine-Phosphate Lyase,” Adv. Lipid Res. 26:69-98 (1993).Applicant
• Van Veldhoven, “Shingosine-l-phosphate Lyase,” Methods Enzymol. 311:244-254 (1999).Applicant
• Van Veldhoven et al., “Human sphingosine-1-phosphate lyase: cDNA cloning, functional expression studies and mapping to chromosome 10q22(1),” Biochim. Biophys. Acta 1487(2-3)128-134 (2000).Applicant
• Visentin et al., “Validation of an anti-sphingosine-1-phosphate antibody as a potential therapeutic in reducing growth, invasion, and angiogenesis in multiple tumor lineages,” Cancer Cell. 9(3):225-238 (2006).Applicant
• Vivekananda et al., “Sphingomyelin metabolites inhibit sphingomyelin synthase and CTP:phosphocholine cytidylyltransferase,” Am. J. Physiol. Lung Cell. Mol. Physiol. 228(1):L98-L107 (2001).Applicant
• Walev et al., “Selective killing of human monocytes and cytokine release provoked by sphingomyelinase (beta-toxin) of Staphylococcus aureus,” Infect. Immun. 64(8):2974-2979 (1996).Applicant
• Wang et al., “A Single Amino Acid Determines Lysophospholipid Specificity of the S1 P1 (EDG1) and LPA1 (EDG2) Phospholipid Growth Factor Receptors,” J. Biol. Chem. 276(52):49213-49220 (2001).Applicant
• Wang et al., “Fumonisins and other inhibitors of de novo sphingolipid biosynthesis,” Adv. Lipid Res. 26:215-234 (1993).Applicant
• Webster's Dictionary, p. 1135 (1990).Applicant
• Winter et al., “Making antibodies by phage display technology,” Annu. Rev. Immunol. 12:433-455 (1994).Applicant
• Xia et al., “Tumor necrosis factor-alpha induces adhesion molecule expression through the sphingosine kinase pathway,” Proc. Natl. Acad. Sci. (USA) 95(24):14196-14201 (1988).Applicant
• Xia et al., “High density lipoproteins (HDL) interrupt the sphingosine kinase signaling pathway. A possible mechanism for protection against atherosclerosis by HDL,” J. Biol. Chem. 274(46):33143-33147 (1999).Applicant
• Xu et al., “Involvement of de novo ceramide biosynthesis in tumor necrosis factor-alpha/cycloheximide-induced cerebral endothelial cell death,” J. Biol. Chem. 273(26):16521-16526 (1998).Applicant
• Xu et al., “Sphingosylphosphorylcholine is a ligand for ovarian cancer G-protein-coupled receptor 1,” Nat. Cell Biol. 2(5):261-267 (2000).Applicant
• Yada et al., “Purification and biochemical characterization of membrane-bound epidermal ceramidases from guinea pig skin,” J. Biol. Chem. 270(21):12677-12684 (1995).Applicant
• Yamada et al., “Nucleotide sequence and expression in Escherichia coli of the gene coding for sphingomyelinase of Bacillus cereus,” Eur. J. Biochem. 175(2):213-220 (1988).Applicant
• Yamaji et al., “Lysenin, a novel sphingomyelin-specific binding protein,” J. Biol. Chem. 273(9):5300-5306 (1998).Applicant
• Yamanaka et al., “Acid Sphingomyelinase of Human Brain: Purification to Homogeneity,” J. Neurochem, 38(6):1753-1764 (1982).Applicant
• Yamazaki et al., “Edg-6 as a Putative Sphingosine 1-Phosphate Receptor Coupling to Ca2+ Signaling Pathway,” Biochem. Biophys. Res. Commun. 268(2):583-589 (2000).Applicant
• Yatomi et al., “Sphiongosine-l-Phosphate: A Platelet-Activating Sphingolipid Released from Agonist Stimulated Human Platelets,” Blood 86(1):193-202 (1995).Applicant
• Yatomi et al., “Sphingosine 1-phosphate, a bioactive sphingolipid abundantly stored in platelets, is a normal constituent of human plasma and serum,” J. Biochem. 121(5):969-973 (1997).Applicant
• Yatomi et al., “Sphingosine 1-phosphate induces platelet activation through an extracellular action and shares a platelet surface receptor with lysophosphatidic acid,” J. Biol. Chem. 272(8):5291-5297 (1997).Applicant
• Yellon et al., “Ischaemic preconditioning limits infarct size in the rat heart,” Cardiovasc. Res. 26(10):983-987 (1992).Applicant
• Yoshimura et al., “Inhibition of Neutral Sphingomyelinase Activation and Ceramide Formation by Glutathione in Hypoxic PC12 Cell Death,” J. Neurochem. 73(2):675-683 (1999) .Applicant
• Yu et al., “Picotal role for acidic sphingomyelinase in cerebral ischemia-induced ceramide and cytokine production, and neuronal apoptosis,” J. Mol. Neurosci. 15(2):85-97 (2000).Applicant
• Zager et al., “Decreased expression of mitochondrial-derived H2O2 and hydroxyl radical in cytoresistant proximal tubules,” Kidney Int. 52(4):942-952 (1997).Applicant
• Zechner et al., “MKK6 inhibits myocardial cell apoptosis via a p38 MAP kinase-dependent pathway,” J. Biol. Chem. 273(14):8232-8239 (1998).Applicant
• Zelinski et al., “Phosphatidylcholine biosynthesis in isolated hamster heart,” J. Biol. Chem. 255(23):11423-11428 (1980).Applicant
• Zhang et al., “Comparative analysis of three murine G-protein coupled receptors activated by sphingosine-1-phosphate,” Gene 227(1):89-99 (1999).Applicant
• Zhang et al., “Human Acid Ceramidase Gene: Novel Mutations in Farber Disease,” Mol. Genet. Metab. 70(4):301-309 (2000).Applicant
• Zhou et al., “Identification of the First Mammalian Sphingosine Phosphate Lyase Gene and its Functional Expression in Yeast,” Biochem. Biophys. Res. Comm. 242(3):502-507 (1998).Applicant
• Zweerink et al., “Characterization of a Novel, Potent, and Specific Inhibitor of Serine Palmitoyltransferase,” J. Biol. Chem. 267(35):25032-25038 (1992).Applicant