Sphingolipid and Glycosphingolipid Metabolic Pathways in the Era of Sphingolipidomics

Macrophage Sphingomyelin Synthase 2 Deficiency Decreases Atherosclerosis in Mice

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A mouse B16 melanoma mutant deficient in glycolipids.

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Sphingolipidomics: a valuable tool for understanding the roles of sphingolipids in biology and disease

Merrill, A. H., Stokes, T. H., Momin, A. A., Park, H. J., Portz, B. J., Kelly, S. L., Wang, E. L., Sullards, M. C., & Wang, M. D. (2008) · Journal of Lipid Research · doi:10.1194/jlr.r800073-jlr200 · Cited by 151

Acylation of Naturally Occurring and Synthetic 1-Deoxysphinganines by Ceramide Synthase

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Fumonisins: fungal toxins that shed light on sphingolipid function

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Cancer Treatment Strategies Targeting Sphingolipid Metabolism

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The Reverse Activity of Human Acid Ceramidase

Okino, N., He, X., Gátt, S., Sandhoff, K., Ito, M., & Schuchman, E. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303310200 · Cited by 147

The marine compound spisulosine, an inhibitor of cell proliferation, promotes the disassembly of actin stress fibers

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CERT and intracellular trafficking of ceramide

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Salvage pathways in glycosphingolipid metabolism

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A Novel Inhibitor of Ceramide Trafficking from the Endoplasmic Reticulum to the Site of Sphingomyelin Synthesis

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Acid sphingomyelinase, cell membranes and human disease: Lessons from Niemann–Pick disease

Schuchman, E. H. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.11.083 · Cited by 146

The Structure of Serine Palmitoyltransferase; Gateway to Sphingolipid Biosynthesis

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Profiling and Imaging of Lipids on Brain and Liver Tissue by Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry Using 2-Mercaptobenzothiazole as a Matrix

Astigarraga, E., Barreda‐Gómez, G., Lombardero, L., Fresnedo, O., Castaño, F., Giralt, M. T., Ochoa, B., Rodríguez‐Puertas, R., & Fernández, J. A. (2008) · Analytical Chemistry · doi:10.1021/ac801662n · Cited by 145

Analysis of mammalian sphingolipids by liquid chromatography tandem mass spectrometry (LC-MS/MS) and tissue imaging mass spectrometry (TIMS)

Sullards, M. C., Liu, Y., Chen, Y., & Merrill, A. H. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2011.06.027 · Cited by 145

Control of metabolism and signaling of simple bioactive sphingolipids: Implications in disease

Gangoiti, P., Camacho, L., Arana, L., Ouro, A., Granado, M. H., Brizuela, L., Casas, J., Fabriàs, G., Abad, J. L., Delgado, A., et al. (2010) · Progress in Lipid Research · doi:10.1016/j.plipres.2010.02.004 · Cited by 144

Sphingomyelin and Cholesterol: From Membrane Biophysics and Rafts to Potential Medical Applications

Barenholz, Y. (2004) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4757-5806-1_5 · Cited by 143

Analysis of Sphingosine 1-Phosphate, Ceramides, and Other Bioactive Sphingolipids by High-Performance Liquid Chromatography-Tandem Mass Spectrometry

Sullards, M. C., & Merrill, A. H. (2001) · Science s STKE · doi:10.1126/stke.2001.67.pl1 · Cited by 143

Sphingolipids with inositolphosphate-containing head groups.

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A Mammalian Homolog of the Yeast LCB1 Encodes a Component of Serine Palmitoyltransferase, the Enzyme Catalyzing the First Step in Sphingolipid Synthesis

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C‐Myc is a Nrf2‐interacting protein that negatively regulates phase II genes through their electrophile responsive elements

Levy, S., & Forman, H. J. (2010) · IUBMB Life · doi:10.1002/iub.314 · Cited by 142

Handbook of Glycosyltransferases and Related Genes

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Imaging Mass Spectrometry Technology and Application on Ganglioside Study; Visualization of Age-Dependent Accumulation of C20-Ganglioside Molecular Species in the Mouse Hippocampus

Sugiura, Y., Shimma, S., Konishi, Y., Yamada, M., & Setou, M. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003232 · Cited by 141

Characterization of a novel, potent, and specific inhibitor of serine palmitoyltransferase.

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Sphingosine-1-phosphate phosphohydrolase-1 regulates ER stress-induced autophagy

Lépine, S., Allegood, J. C., Park, M., Dent, P., Milstien, S., & Spiegel, S. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.104 · Cited by 139

Sphingolipidomics: Methods for the comprehensive analysis of sphingolipids

Haynes, C. A., Allegood, J. C., Park, H. J., & Sullards, M. C. (2009) · Journal of Chromatography B · doi:10.1016/j.jchromb.2008.12.057 · Cited by 138

From Whole-body Sections Down to Cellular Level, Multiscale Imaging of Phospholipids by MALDI Mass Spectrometry

Chaurand, P., Cornett, D. S., Angel, P. M., & Caprioli, R. M. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o110.004259 · Cited by 136

Lactosylceramide-enriched glycosphingolipid signaling domain mediates superoxide generation from human neutrophils

Iwabuchi, K., & Nagaoka, I. (2002) · Blood · doi:10.1182/blood.v100.4.1454.h81602001454_1454_1464 · Cited by 133

Potent Immunosuppressants, 2-Alkyl-2-aminopropane-1,3-diols

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Modulation of intracellular beta-catenin localization and intestinal tumorigenesis in vivo and in vitro by sphingolipids.

Schmelz, E.-M., Roberts, P. C., Kustin, E. M., Lemonnier, L. A., Sullards, M. C., Dillehay, D. L., & Merrill, A. H. (2001) · PubMed · Cited by 133

Brain Tissue Lipidomics: Direct Probing Using Matrix-assisted Laser Desorption/Ionization Mass Spectrometry

Woods, A. S., & Jackson, S. N. (2006) · The AAPS Journal · doi:10.1007/bf02854910 · Cited by 132

GM3 directly inhibits tyrosine phosphorylation and De-N-acetyl-GM3 directly enhances serine phosphorylation of epidermal growth factor receptor, independently of receptor–receptor interaction

Zhou, Q., Hakomori, S., Kitamura, K., & Igarashi, Y. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42121-1 · Cited by 131

Selective knockdown of ceramide synthases reveals complex interregulation of sphingolipid metabolism

Mullen, T. D., Spassieva, S. D., Jenkins, R. W., Kitatani, K., Bielawski, J., Hannun, Y. A., & Obeid, L. M. (2010) · Journal of Lipid Research · doi:10.1194/jlr.m009142 · Cited by 131

Kdo2-Lipid A, a TLR4-specific Agonist, Induces de Novo Sphingolipid Biosynthesis in RAW264.7 Macrophages, Which Is Essential for Induction of Autophagy

Sims, K. H., Haynes, C. A., Kelly, S. L., Allegood, J. C., Wang, E. L., Momin, A. A., Leipelt, M., Reichart, D. R., Glass, C. K., Sullards, M. C., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.170621 · Cited by 130

Imaging of Lipids in Atheroma by Desorption Electrospray Ionization Mass Spectrometry

Manicke, N. E., Nefliu, M., Wu, C., Woods, J. W., Reiser, V., Hendrickson, R. C., & Cooks, R. G. (2009) · Analytical Chemistry · doi:10.1021/ac901739s · Cited by 130

Very long chain sphingolipids: Tissue expression, function and synthesis

Sandhoff, R. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.12.032 · Cited by 130

Elevation of sulfatides in ovarian cancer: An integrated transcriptomic and lipidomic analysis including tissue-imaging mass spectrometry

Liu, Y., Chen, Y., Momin, A. A., et al. (2010) · Molecular Cancer · doi:10.1186/1476-4598-9-186 · Cited by 130

Molecular Cloning and Characterization of UDP-GlcNAc:Lactosylceramide β1,3-N-Acetylglucosaminyltransferase (β3Gn-T5), an Essential Enzyme for the Expression of HNK-1 and Lewis X Epitopes on Glycolipids

Togayachi, A., Akashima, T., Ookubo, R., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011369200 · Cited by 130

Lipid and glycolipid antigens of CD1d-restricted natural killer T cells

Venkataswamy, M. M., & Porcelli, S. A. (2009) · Seminars in Immunology · doi:10.1016/j.smim.2009.10.003 · Cited by 129

Sphingomyelin: biophysical aspects

Barenholz, Y., & Thompson, T. E. (1999) · Chemistry and Physics of Lipids · doi:10.1016/s0009-3084(99)00072-9 · Cited by 129

Intracellular Generation of Sphingosine 1-Phosphate in Human Lung Endothelial Cells

Zhao, Y., Kalari, S. K., Usatyuk, P. V., Gorshkova, I. A., He, D., Watkins, T., Brindley, D. N., Sun, C., Bittman, R., Garcia, J. G. N., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701279200 · Cited by 128

Chapter 5 Maternal Fumonisin Exposure as a Risk Factor for Neural Tube Defects

Waes, J. G., Voss, K. A., Stevens, V. L., Speer, M. C., & Riley, R. T. (2009) · Advances in food and nutrition research · doi:10.1016/s1043-4526(08)00605-0 · Cited by 127

The Acid Sphingomyelinase/Ceramide Pathway: Biomedical Significance and Mechanisms of Regulation

Zeidan, Y. H., & Hannun, Y. A. (2010) · Current Molecular Medicine · doi:10.2174/156652410791608225 · Cited by 126

Sphingolipids in Inflammation: Roles and Implications

Pettus, B. J., Chalfant, C. E., & Hannun, Y. A. (2004) · Current Molecular Medicine · doi:10.2174/1566524043360573 · Cited by 126

Collision‐induced dissociation pathways of yeast sphingolipids and their molecular profiling in total lipid extracts: a study by quadrupole TOF and linear ion trap–orbitrap mass spectrometry

Ejsing, C. S., Moehring, T., Bahr, U., Duchoslav, E., Karas, M., Simons, K., & Shevchenko, A. (2006) · Journal of Mass Spectrometry · doi:10.1002/jms.997 · Cited by 126

Validation of a new procedure to determine plasma fatty acid concentration and isotopic enrichment

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The presence of free D-serine, D-alanine and D-proline in human plasma

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Identification of Dihydroceramide Desaturase as a Direct in Vitro Target for Fenretinide

Rahmaniyan, M., Curley, R. W., Obeid, L. M., Hannun, Y. A., & Kraveka, J. M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.250779 · Cited by 125

(Glyco)sphingolipidology: an amazing challenge and opportunity for systems biology

Merrill, A. H., Wang, M. D., Park, M., & Sullards, M. C. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.09.004 · Cited by 125

Novel Ceramide Analogs as Potential Chemotherapeutic Agents in Breast Cancer

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B cell antigen receptor signal strength and peripheral B cell development are regulated by a 9-O-acetyl sialic acid esterase

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Glucosylceramide modulates membrane traffic along the endocytic pathway

Sillence, D. J., Puri, V., Marks, D. L., Butters, T. D., Dwek, R. A., Pagano, R. E., & Platt, F. M. (2002) · Journal of Lipid Research · doi:10.1194/jlr.m200232-jlr200 · Cited by 124

Targeted analysis of ganglioside and sulfatide molecular species by LC/ESI-MS/MS with theoretically expanded multiple reaction monitoring

Ikeda, K., Shimizu, T., & Taguchi, R. (2008) · Journal of Lipid Research · doi:10.1194/jlr.d800038-jlr200 · Cited by 124

LASS5 Is a Bona Fide Dihydroceramide Synthase That Selectively Utilizes Palmitoyl-CoA as Acyl Donor

Lahiri, S., & Futerman, A. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506485200 · Cited by 123

Globotriaosyl ceramide receptor function – Where membrane structure and pathology intersect

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Structure‐Specific, Quantitative Methods for Analysis of Sphingolipids by Liquid Chromatography–Tandem Mass Spectrometry: “Inside‐Out” Sphingolipidomics

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Sphingolipid Biosynthesis de Novo by Rat Hepatocytes in Culture.

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Recycling of Sphingosine Is Regulated by the Concerted Actions of Sphingosine-1-phosphate Phosphohydrolase 1 and Sphingosine Kinase 2

Stunff, H. L., Giussani, P., Maceyka, M. W., Lépine, S., Milstien, S., & Spiegel, S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703329200 · Cited by 120

Molecular Cloning and Expression of cDNA Encoding Human 3′-Phosphoadenylylsulfate:galactosylceramide 3′-Sulfotransferase

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Humans Lack iGb3 Due to the Absence of Functional iGb3-Synthase: Implications for NKT Cell Development and Transplantation

Christiansen, D., Milland, J., Mouhtouris, E., Vaughan, H. A., Pellicci, D. G., McConville, M. J., Godfrey, D. I., & Sandrin, M. S. (2008) · PLoS Biology · doi:10.1371/journal.pbio.0060172 · Cited by 119

DES2 protein is responsible for phytoceramide biosynthesis in the mouse small intestine

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Transport of lipids by ABC proteins: Interactions and implications for cellular toxicity, viability and function

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Identification of the human sphingolipid C4‐hydroxylase, hDES2, and its up‐regulation during keratinocyte differentiation

Mizutani, Y., Kihara, A., & Igarashi, Y. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00274-1 · Cited by 117

Electron Transfer Dissociation of Milk Oligosaccharides

Han, L., & Costello, C. E. (2011) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-011-0117-9 · Cited by 113

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

Véret, J., Coant, N., Berdyshev, E. V., Skobeleva, A., Therville, N., Bailbé, D., Gorshkova, I. A., Natarajan, V., Portha, B., & Stunff, H. L. (2011) · Biochemical Journal · doi:10.1042/bj20101386 · Cited by 112

Quantitation of fatty acyl-coenzyme As in mammalian cells by liquid chromatography-electrospray ionization tandem mass spectrometry

Haynes, C. A., Allegood, J. C., Sims, K. H., Wang, E. W., Sullards, M. C., & Merrill, A. H. (2008) · Journal of Lipid Research · doi:10.1194/jlr.d800001-jlr200 · Cited by 112

A new 6-hydroxy-4-sphingenine-containing ceramide in human skin

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Glycosphingolipids and drug resistance

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Ceramide kinase uses ceramide provided by ceramide transport protein: localization to organelles of eicosanoid synthesis

Lamour, N. F., Stahelin, R. V., Wijesinghe, D. S., Maceyka, M. W., Wang, E. L., Allegood, J. C., Merrill, A. H., Cho, W., & Chalfant, C. E. (2007) · Journal of Lipid Research · doi:10.1194/jlr.m700083-jlr200 · Cited by 111

Male Germ Cells Require Polyenoic Sphingolipids with Complex Glycosylation for Completion of Meiosis

Rabionet, M., van der Spoel, A. C., Chuang, C., von Tümpling-Radosta, B., Litjens, M., Bouwmeester, D., Hellbusch, C. C., Körner, C., Wiegandt, H., Gorgas, K., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800870200 · Cited by 111

Asymmetric Addition of Ceramides but not Dihydroceramides Promotes Transbilayer (Flip-Flop) Lipid Motion in Membranes

Contreras, F. ‐., Basáñez, G., Alonso, A., Herrmann, A., & Goñi, F. M. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.050690 · Cited by 110

Structure determination of soybean and wheat glucosylceramides by tandem mass spectrometry

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Determination of d-serine and related neuroactive amino acids in human plasma by high-performance liquid chromatography with fluorimetric detection

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Association of the Golgi UDP-Galactose Transporter with UDP-Galactose:Ceramide Galactosyltransferase Allows UDP-Galactose Import in the Endoplasmic Reticulum

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2-Hydroxy-ceramide synthesis by ceramide synthase family: enzymatic basis for the preference of FA chain length

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BIOCHEMISTRY OF THE SPHINGOLIPIDES

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Properties of Ceramides and Their Impact on the Stratum Corneum Structure: A Review

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A Disease-causing Mutation in the Active Site of Serine Palmitoyltransferase Causes Catalytic Promiscuity

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Ceramidase Regulates Synaptic Vesicle Exocytosis and Trafficking

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FVT-1 Is a Mammalian 3-Ketodihydrosphingosine Reductase with an Active Site That Faces the Cytosolic Side of the Endoplasmic Reticulum Membrane

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Differential expression of (dihydro)ceramide synthases in mouse brain: oligodendrocyte-specific expression of CerS2/Lass2

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Metabolism of cerebroside in the intestinal tract of the rat

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Thematic Review Series: Sphingolipids. Nuclear sphingolipids: metabolism and signaling

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MALDI mass spectrometry imaging of gangliosides in mouse brain using ionic liquid matrix

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A view on sphingolipids and disease

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Lactosylceramide is synthesized in the lumen of the Golgi apparatus

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N-(4-Hydroxyphenyl)retinamide increases dihydroceramide and synergizes with dimethylsphingosine to enhance cancer cell killing

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Effect of ceramide N-acyl chain and polar headgroup structure on the properties of ordered lipid domains (lipid rafts)

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