메뉴 건너뛰기




Volumn 28, Issue 2, 2011, Pages 67-87

Systematic analyses of free ceramide species and ceramide species comprising neutral glycosphingolipids by MALDI-TOF MS with high-energy CID

Author keywords

Ceramides; High energy collision induced dissociation; Hydroxy ceramides; MALDI TOF MS; Neutral glycosphingolipids; Nona octadeca ceramides

Indexed keywords

CERAMIDE; FORSSMAN ANTIGEN; GALACTOSYLCERAMIDE; GLOBOTRIAOSYLCERAMIDE; GLUCOSYLCERAMIDE; GLYCOSPHINGOLIPID; ION; LACTOSYLCERAMIDE; NEUTRAL GLYCOSPHINGOLIPID; UNCLASSIFIED DRUG;

EID: 79953744097     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-011-9325-6     Document Type: Article
Times cited : (17)

References (54)
  • 1
    • 66249084549 scopus 로고    scopus 로고
    • Sphingolipids synthesis, transport and cellular signaling
    • Hirabayashi, Y., et al. (eds.). Springer, Tokyo
    • Hirabayashi, Y., Igarashi, Y., Merrill Jr., A.H.: Sphingolipids synthesis, transport and cellular signaling. In: Hirabayashi, Y., et al. (eds.) Sphingolipid Biology, pp. 3-22. Springer, Tokyo (2006)
    • (2006) Sphingolipid Biology , pp. 3-22
    • Hirabayashi, Y.1    Igarashi, Y.2    Merrill Jr., A.H.3
  • 2
    • 38549152194 scopus 로고    scopus 로고
    • Principles of bioactive lipid signalling: Lessons from sphingolipids
    • Hannun, Y.A., Obeid, L.M.: Principles of bioactive lipid signalling: lessons from sphingolipids. Nat. Rev. Mol. Cell Biol. 9, 139-150 (2008)
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 139-150
    • Hannun, Y.A.1    Obeid, L.M.2
  • 3
    • 40749132024 scopus 로고    scopus 로고
    • Functional role of glycosphingolipids and gangliosides in control of cell adhesion, motility, and growth, through glycosynaptic microdomains
    • Regina Todeschini, A., Hakomori, S.I.: Functional role of glycosphingolipids and gangliosides in control of cell adhesion, motility, and growth, through glycosynaptic microdomains. Biochim. Biophys. Acta. 1780, 421-433 (2008)
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 421-433
    • Regina Todeschini, A.1    Hakomori, S.I.2
  • 4
    • 36448943234 scopus 로고    scopus 로고
    • Glycosignaling in neural stem cells: Involvement of glycoconjugates in signal transduction modulating the neural stem cell fate
    • Yu, R.K., Yanagisawa, M.: Glycosignaling in neural stem cells: involvement of glycoconjugates in signal transduction modulating the neural stem cell fate. J Neurochem. 103(Suppl 1), 39-46 (2007)
    • (2007) J Neurochem. , vol.103 , Issue.SUPPL. 1 , pp. 39-46
    • Yu, R.K.1    Yanagisawa, M.2
  • 7
    • 0038728628 scopus 로고    scopus 로고
    • Structure of the ceramide moiety of GM1 ganglioside determines its occurrence in different detergent-resistant membrane domains in HL-60 cells
    • Panasiewicz, M., Domek, H., Hoser, G., Kawalec, M., Pacuszka, T.: Structure of the ceramide moiety of GM1 ganglioside determines its occurrence in different detergent-resistant membrane domains in HL-60 cells. Biochemistry 42, 6608-6619 (2003)
    • (2003) Biochemistry , vol.42 , pp. 6608-6619
    • Panasiewicz, M.1    Domek, H.2    Hoser, G.3    Kawalec, M.4    Pacuszka, T.5
  • 8
    • 63449111670 scopus 로고    scopus 로고
    • The ceramide structure of GM1 ganglioside differently affects its recovery in low-density membrane fractions prepared from HL-60 cells with or without triton- X100
    • Panasiewicz, M., Domek, H., Hoser, G., Fedoryszak, N., Kawalec, M., Pacuszka, T.: The ceramide structure of GM1 ganglioside differently affects its recovery in low-density membrane fractions prepared from HL-60 cells with or without triton- X100. Cell Mol Biol Lett. 14, 175-189 (2009)
    • (2009) Cell Mol Biol Lett. , vol.14 , pp. 175-189
    • Panasiewicz, M.1    Domek, H.2    Hoser, G.3    Fedoryszak, N.4    Kawalec, M.5    Pacuszka, T.6
  • 9
    • 33750361922 scopus 로고    scopus 로고
    • C16:0 sulfatide inhibits insulin secretion in rat beta-cells by reducing the sensitivity of KATP channels to ATP inhibition
    • Buschard, K., Blomqvist, M., Månsson, J.E., Fredman, P., Juhl, K., Gromada, J.: C16:0 sulfatide inhibits insulin secretion in rat beta-cells by reducing the sensitivity of KATP channels to ATP inhibition. Diabetes 55, 2826-2834 (2006)
    • (2006) Diabetes , vol.55 , pp. 2826-2834
    • Buschard, K.1    Blomqvist, M.2    Månsson, J.E.3    Fredman, P.4    Juhl, K.5    Gromada, J.6
  • 11
    • 70350389557 scopus 로고    scopus 로고
    • Fatty acid-dependent globotriaosyl ceramide receptor function in detergent resistant model membranes
    • Mahfoud, R., Manis, A., Lingwood, C.A.: Fatty acid-dependent globotriaosyl ceramide receptor function in detergent resistant model membranes. J. Lipid Res. 50, 1744-1755 (2009)
    • (2009) J. Lipid Res. , vol.50 , pp. 1744-1755
    • Mahfoud, R.1    Manis, A.2    Lingwood, C.A.3
  • 12
    • 0036585050 scopus 로고    scopus 로고
    • Characterization of ceramides by low energy collisional-activated dissociation tandem mass spectrometry with negative-ion electrospray ionization
    • Hsu, F.F., Turk, J.: Characterization of ceramides by low energy collisional-activated dissociation tandem mass spectrometry with negative-ion electrospray ionization. J. Am. Soc. Mass Spectrom. 13, 558-570 (2002)
    • (2002) J. Am. Soc. Mass Spectrom. , vol.13 , pp. 558-570
    • Hsu, F.F.1    Turk, J.2
  • 13
    • 0031568259 scopus 로고    scopus 로고
    • Ceramide profiling of complex lipid mixtures by electrospray ionization mass spectrometry
    • Gu, M., Kerwin, J.L., Watts, J.D., Aebersold, R.: Ceramide profiling of complex lipid mixtures by electrospray ionization mass spectrometry. Anal. Biochem. 244, 347-356 (1997)
    • (1997) Anal. Biochem. , vol.244 , pp. 347-356
    • Gu, M.1    Kerwin, J.L.2    Watts, J.D.3    Aebersold, R.4
  • 14
    • 74949097878 scopus 로고    scopus 로고
    • Comprehensive quantitative analysis of bioactive sphingolipids by high-performance liquid chromatographytandem mass spectrometry
    • Bielawski, J., Pierce, J.S., Snider, J., Rembiesa, B., Szulc, Z.M., Bielawska, A.: Comprehensive quantitative analysis of bioactive sphingolipids by high-performance liquid chromatographytandem mass spectrometry. Methods Mol. Biol. 579, 443-467 (2009)
    • (2009) Methods Mol. Biol. , vol.579 , pp. 443-467
    • Bielawski, J.1    Pierce, J.S.2    Snider, J.3    Rembiesa, B.4    Szulc, Z.M.5    Bielawska, A.6
  • 15
    • 58149492631 scopus 로고    scopus 로고
    • 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.: Targeted analysis of ganglioside and sulfatide molecular species by LC/ESI-MS/MS with theoretically expanded multiple reaction monitoring. J. Lipid Res. 49, 2678-2689 (2008)
    • (2008) J. Lipid Res. , vol.49 , pp. 2678-2689
    • Ikeda, K.1    Shimizu, T.2    Taguchi, R.3
  • 16
    • 67849111947 scopus 로고    scopus 로고
    • Sphingolipidomics: Methods for the comprehensive analysis of sphingolipids
    • Haynes, C.A., Allegood, J.C., Park, H., Sullards, M.C.: Sphingolipidomics: methods for the comprehensive analysis of sphingolipids. J. Chromatogr. B 877, 2696-2708 (2009)
    • (2009) J. Chromatogr. B , vol.877 , pp. 2696-2708
    • Haynes, C.A.1    Allegood, J.C.2    Park, H.3    Sullards, M.C.4
  • 18
    • 30544433842 scopus 로고    scopus 로고
    • Glycosphingolipid structural analysis and glycosphingolipidomics
    • Levery, S.B.: Glycosphingolipid structural analysis and glycosphingolipidomics. Methods Enzymol. 405, 300-369 (2005)
    • (2005) Methods Enzymol. , vol.405 , pp. 300-369
    • Levery, S.B.1
  • 19
    • 33747880286 scopus 로고    scopus 로고
    • Rapid demonstration of diversity of sulfatide molecular species from biological materials by MALDI-TOF MS
    • Kyogashima, M., Tamiya-Koizumi, K., Ehara, T., Li, G., Hu, R., Hara, A., Aoyama, T., Kannagi, R.: Rapid demonstration of diversity of sulfatide molecular species from biological materials by MALDI-TOF MS. Glycobiology 16, 719-728 (2006)
    • (2006) Glycobiology , vol.16 , pp. 719-728
    • Kyogashima, M.1    Tamiya-Koizumi, K.2    Ehara, T.3    Li, G.4    Hu, R.5    Hara, A.6    Aoyama, T.7    Kannagi, R.8
  • 20
    • 33747586562 scopus 로고    scopus 로고
    • Structural characterization of neutral glycosphingolipids by thin-layer chromatography coupled to matrix-assisted laser desorption/ionization quadrupole ion trap time-of-flight MS/MS
    • Nakamura, K., Suzuki, Y., Goto-Inoue, N., Yoshida-Noro, C., Suzuki, A.: Structural characterization of neutral glycosphingolipids by thin-layer chromatography coupled to matrix-assisted laser desorption/ionization quadrupole ion trap time-of-flight MS/MS. Anal. Chem. 78, 5736-5743 (2006)
    • (2006) Anal. Chem. , vol.78 , pp. 5736-5743
    • Nakamura, K.1    Suzuki, Y.2    Goto-Inoue, N.3    Yoshida-Noro, C.4    Suzuki, A.5
  • 21
    • 33947114884 scopus 로고    scopus 로고
    • Novel free ceramides as components of the soldier defense gland of the Formosan subterranean termite (Coptotermes formosanus)
    • Ohta, M., Matsuura, F., Henderson, G., Laine, R.A.: Novel free ceramides as components of the soldier defense gland of the Formosan subterranean termite (Coptotermes formosanus). J. Lipid Res. 48, 656-664 (2007)
    • (2007) J. Lipid Res. , vol.48 , pp. 656-664
    • Ohta, M.1    Matsuura, F.2    Henderson, G.3    Laine, R.A.4
  • 22
    • 34447320480 scopus 로고    scopus 로고
    • Integrated mass spectrometric strategy for characterizing the glycans from glycosphingolipids and glycoproteins: Direct identification of sialyl Le(x) in mice
    • Parry, S., Ledger, V., Tissot, B., Haslam, S.M., Scott, J., Morris, H.R., Dell, A.: Integrated mass spectrometric strategy for characterizing the glycans from glycosphingolipids and glycoproteins: direct identification of sialyl Le(x) in mice. Glycobiology 17, 646-654 (2007)
    • (2007) Glycobiology , vol.17 , pp. 646-654
    • Parry, S.1    Ledger, V.2    Tissot, B.3    Haslam, S.M.4    Scott, J.5    Morris, H.R.6    Dell, A.7
  • 23
    • 59249099294 scopus 로고    scopus 로고
    • Structural and functional glycosphingolipidomics by glycoblotting with an aminooxyfunctionalized gold nanoparticle
    • Nagahori, N., Abe, M., Nishimura, S.: Structural and functional glycosphingolipidomics by glycoblotting with an aminooxyfunctionalized gold nanoparticle. Biochemistry 48, 583-594 (2009)
    • (2009) Biochemistry , vol.48 , pp. 583-594
    • Nagahori, N.1    Abe, M.2    Nishimura, S.3
  • 24
    • 0016827855 scopus 로고
    • Long chain base and fatty acid compositions of equine kidney sphingolipids
    • Hara, A., Taketomi, T.: Long chain base and fatty acid compositions of equine kidney sphingolipids. J. Biochem. 78, 527-536 (1975)
    • (1975) J. Biochem. , vol.78 , pp. 527-536
    • Hara, A.1    Taketomi, T.2
  • 25
    • 0014682240 scopus 로고
    • A modified column chromatographic method for the recovery of the glycerogalactolipid fraction of nerve tissue. Some observations on the fractionation of nerve tissue glycolipids on silicic acid with chloroform and acetone mixtures
    • Rumsby, M.G.: A modified column chromatographic method for the recovery of the glycerogalactolipid fraction of nerve tissue. Some observations on the fractionation of nerve tissue glycolipids on silicic acid with chloroform and acetone mixtures. J. Chromatogr. 42, 237-247 (1969)
    • (1969) J. Chromatogr. , vol.42 , pp. 237-247
    • Rumsby, M.G.1
  • 26
    • 0020315423 scopus 로고
    • Molecular properties and kinetic studies on sphingomyelinase of Bacillus cereus
    • Tomita, M., Taguchi, R., Ikezawa, H.: Molecular properties and kinetic studies on sphingomyelinase of Bacillus cereus. Biochim. Biophys. Acta. 704, 90-99 (1982)
    • (1982) Biochim. Biophys. Acta , vol.704 , pp. 90-99
    • Tomita, M.1    Taguchi, R.2    Ikezawa, H.3
  • 27
    • 0015026124 scopus 로고
    • Quantitative isolation of total glycosphingolipids from animal cells
    • Saito, T., Hakomori, S.I.: Quantitative isolation of total glycosphingolipids from animal cells. J. Lipid Res. 12, 257-259 (1971)
    • (1971) J. Lipid Res. , vol.12 , pp. 257-259
    • Saito, T.1    Hakomori, S.I.2
  • 28
    • 0021365069 scopus 로고
    • Abnormalities of glycosphingolipids in mucopolysaccharidosis type III B
    • Hara, A., Kitazawa, N., Taketomi, T.: Abnormalities of glycosphingolipids in mucopolysaccharidosis type III B. J. Lipid Res. 25, 175-184 (1984)
    • (1984) J. Lipid Res. , vol.25 , pp. 175-184
    • Hara, A.1    Kitazawa, N.2    Taketomi, T.3
  • 29
    • 0000582463 scopus 로고
    • α-Galatosidase from coffee beans
    • Courtois, J.E., Petek, F.: α-Galatosidase from coffee beans. Methods Enzymol. 8, 565-571 (1966)
    • (1966) Methods Enzymol. , vol.8 , pp. 565-571
    • Courtois, J.E.1    Petek, F.2
  • 30
    • 0001589151 scopus 로고
    • Isolation and characterization of a blood group A substance-degrading α-N-acetylgalactosaminidase from an Acremonium sp.
    • Kadowaki, S., Ueda, T., Yamamoto, K., Kumagai, H., Tochikura, T.: Isolation and characterization of a blood group A substance-degrading α-N-acetylgalactosaminidase from an Acremonium sp. Agric. Biol. Chem. 53, 111-120 (1989)
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 111-120
    • Kadowaki, S.1    Ueda, T.2    Yamamoto, K.3    Kumagai, H.4    Tochikura, T.5
  • 31
    • 0014940534 scopus 로고
    • Studies on the glycosidases of jack bean meal. 3. Crystallization and properties of beta-N-acetylhexosaminidase
    • Li, S.C., Li, Y.T.: Studies on the glycosidases of jack bean meal. 3. Crystallization and properties of beta-N-acetylhexosaminidase. J. Biol. Chem. 245, 5153-5160 (1970)
    • (1970) J. Biol. Chem. , vol.245 , pp. 5153-5160
    • Li, S.C.1    Li, Y.T.2
  • 32
    • 2942585313 scopus 로고    scopus 로고
    • Glycoform composition proWling of O-glycopeptides derived from human serum IgA1 by matrix-assisted laser desorption ionization-time of Xight-mass spectrometry
    • Pouria, S., Corran, P.H., Smith, A.C., Smith, H.W., Hendry, B.M., Challacombe, S.J., Tarelli, E.: Glycoform composition proWling of O-glycopeptides derived from human serum IgA1 by matrix-assisted laser desorption ionization-time of Xight-mass spectrometry. Anal. Biochem. 330, 257-263 (2004)
    • (2004) Anal. Biochem. , vol.330 , pp. 257-263
    • Pouria, S.1    Corran, P.H.2    Smith, A.C.3    Smith, H.W.4    Hendry, B.M.5    Challacombe, S.J.6    Tarelli, E.7
  • 33
    • 8444224225 scopus 로고    scopus 로고
    • Mutation in saposin D domain of sphingolipid activator protein gene causes urinary system defects and cerebellar Purkinje cell degeneration with accumulation of hydroxy fatty acid-containing ceramide in mouse
    • Matsuda, J., Kido, M., Tadano-Aritomi, K., Ishizuka, I., Tominaga, K., Toida, K., Takeda, E., Suzuki, K., Kuroda, Y.: Mutation in saposin D domain of sphingolipid activator protein gene causes urinary system defects and cerebellar Purkinje cell degeneration with accumulation of hydroxy fatty acid-containing ceramide in mouse. Hum. Mol. Genet. 13, 2709-2723 (2004)
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2709-2723
    • Matsuda, J.1    Kido, M.2    Tadano-Aritomi, K.3    Ishizuka, I.4    Tominaga, K.5    Toida, K.6    Takeda, E.7    Suzuki, K.8    Kuroda, Y.9
  • 34
    • 0025615844 scopus 로고
    • Tandem mass spectrometry of glycolipids
    • Costello, C.E., Vath, J.E.: Tandem mass spectrometry of glycolipids. Methods Enzymol. 193, 738-768 (1990)
    • (1990) Methods Enzymol. , vol.193 , pp. 738-768
    • Costello, C.E.1    Vath, J.E.2
  • 35
    • 0024206786 scopus 로고
    • A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates
    • Domonand, B., Costello, C.E.: A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates. Glycoconj. J. 5, 397-409 (1988)
    • (1988) Glycoconj. J. , vol.5 , pp. 397-409
    • Domonand, B.1    Costello, C.E.2
  • 36
    • 67649920937 scopus 로고    scopus 로고
    • Dihydroceramide intracellular increase in response to resveratrol treatment mediates autophagy in gastric cancer cells
    • Signorelli, P., Munoz-Olaya, J.M., Gagliostro, V., Casas, J., Ghidoni, R., Fabriàs, G.: Dihydroceramide intracellular increase in response to resveratrol treatment mediates autophagy in gastric cancer cells. Cancer Lett. 282, 238-243 (2009)
    • (2009) Cancer Lett. , vol.282 , pp. 238-243
    • Signorelli, P.1    Munoz-Olaya, J.M.2    Gagliostro, V.3    Casas, J.4    Ghidoni, R.5    Fabriàs, G.6
  • 37
    • 0000318650 scopus 로고
    • Charge-remote fragmentations of closedshell Ions. A thermolytic analogy
    • Adams, J., Gross, M.L.: Charge-remote fragmentations of closedshell Ions. A thermolytic analogy. J. Am. Chem. Soc. 111, 435-440 (1989)
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 435-440
    • Adams, J.1    Gross, M.L.2
  • 38
    • 13444282220 scopus 로고    scopus 로고
    • A new charge-associated mechanism to account for the production of fragment ions in the high-energy CID spectra of fatty acids
    • Harvey, D.J.: A new charge-associated mechanism to account for the production of fragment ions in the high-energy CID spectra of fatty acids. J. Am. Soc. Mass Spectrom. 16, 280-290 (2005)
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 280-290
    • Harvey, D.J.1
  • 39
    • 0003149032 scopus 로고
    • Structure-specific collision-induced fragmentations of ceramides cationized with alkali-metal ions
    • Qinghong, A., Adams, J.: Structure-specific collision-induced fragmentations of ceramides cationized with alkali-metal ions. Anal. Chem. 65, 7-13 (1993)
    • (1993) Anal. Chem. , vol.65 , pp. 7-13
    • Qinghong, A.1    Adams, J.2
  • 40
    • 0002905169 scopus 로고
    • Structure determination of sphingolipids by mass spectrometry
    • Adams, J., Qinghong, A.: Structure determination of sphingolipids by mass spectrometry. Mass Spectrum. Rev. 12, 51-85 (1993)
    • (1993) Mass Spectrum. Rev. , vol.12 , pp. 51-85
    • Adams, J.1    Qinghong, A.2
  • 41
    • 0023668209 scopus 로고
    • Analysis of long-chain bases in sphingolipids by positive ion fast atom bombardment or matrix-assisted secondary ion mass spectrometry
    • Ohashi, Y., Iwamori, M., Ogawa, T., Nagai, Y.: Analysis of long-chain bases in sphingolipids by positive ion fast atom bombardment or matrix-assisted secondary ion mass spectrometry. Biochemistry 26, 3990-3995 (1987)
    • (1987) Biochemistry , vol.26 , pp. 3990-3995
    • Ohashi, Y.1    Iwamori, M.2    Ogawa, T.3    Nagai, Y.4
  • 42
    • 6044274617 scopus 로고    scopus 로고
    • Structural characterization of N-glycopeptides by matrix-dependent selective fragmentation of MALDI-TOF/TOF tandem mass spectrometry
    • Kurogochi, M., Nishimura, S.-I.: Structural characterization of N-glycopeptides by matrix-dependent selective fragmentation of MALDI-TOF/TOF tandem mass spectrometry. Anal. Chem. 76, 6097-6101 (2004)
    • (2004) Anal. Chem. , vol.76 , pp. 6097-6101
    • Kurogochi, M.1    Nishimura, S.-I.2
  • 43
    • 0001061864 scopus 로고
    • Analysis of neutral oligosaccharides by matrix-assisted laser desorption/ionization mass spectrometry
    • Stahl, B., Steup, M., Karas, M., Hillenkamp, F.: Analysis of neutral oligosaccharides by matrix-assisted laser desorption/ionization mass spectrometry. Anal. Chem. 63, 1463-1466 (1991)
    • (1991) Anal. Chem. , vol.63 , pp. 1463-1466
    • Stahl, B.1    Steup, M.2    Karas, M.3    Hillenkamp, F.4
  • 44
    • 0014307325 scopus 로고
    • Studies on sphingosines. 13. The existence of phytosphingosine in bovine kidney sphingomyelins
    • Karlsson, K.A., Steen, G.O.: Studies on sphingosines. 13. The existence of phytosphingosine in bovine kidney sphingomyelins. Biochim. Biophys. Acta. 152, 798-800 (1968)
    • (1968) Biochim. Biophys. Acta , vol.152 , pp. 798-800
    • Karlsson, K.A.1    Steen, G.O.2
  • 45
    • 0016431378 scopus 로고
    • Presence of phytosphingosine combined with 2-hydroxy fatty acids in sphingomyelins of bovine kidney and intestinal mucosa
    • Breimer, M.E., Karlsson, K.A., Samuelsson, B.E.: Presence of phytosphingosine combined with 2-hydroxy fatty acids in sphingomyelins of bovine kidney and intestinal mucosa. Lipids. 10, 17-19 (1975)
    • (1975) Lipids , vol.10 , pp. 17-19
    • Breimer, M.E.1    Karlsson, K.A.2    Samuelsson, B.E.3
  • 46
    • 0014694670 scopus 로고
    • The presence of hydroxy fatty acids in sphingomyelins of bovine rennet stomach
    • Karlsson, K.A., Nilsson, K., Samuelsson, B.E., Steen, G.O.: The presence of hydroxy fatty acids in sphingomyelins of bovine rennet stomach. Biochim. Biophys. Acta. 176, 660-663 (1969)
    • (1969) Biochim. Biophys. Acta , vol.176 , pp. 660-663
    • Karlsson, K.A.1    Nilsson, K.2    Samuelsson, B.E.3    Steen, G.O.4
  • 47
    • 0029896555 scopus 로고    scopus 로고
    • Selective reduction in alpha-hydroxypalmitic acid-containing sphingomyelin and concurrent increase in hydroxylated ceramides in murine skin tumors induced by an initiation-promotion regimen
    • Kitano, Y., Iwamori, Y., Kiguchi, K., DiGiovanni, J., Takahashi, T., Kasama, K., Niwa, T., Harii, K., Iwamori, M.: Selective reduction in alpha-hydroxypalmitic acid-containing sphingomyelin and concurrent increase in hydroxylated ceramides in murine skin tumors induced by an initiation-promotion regimen. Jpn. J. Cancer Res. 87, 437-441 (1996)
    • (1996) Jpn. J. Cancer Res. , vol.87 , pp. 437-441
    • Kitano, Y.1    Iwamori, Y.2    Kiguchi, K.3    DiGiovanni, J.4    Takahashi, T.5    Kasama, K.6    Niwa, T.7    Harii, K.8    Iwamori, M.9
  • 48
    • 0026541438 scopus 로고
    • Novel molecular species of sphingomyelin containing 2-hydroxylated polyenoic very-long-chain fatty acids in mammalian testes and spermatozoa
    • Robinson, B.S., Johnson, D.W., Poulos, A.: Novel molecular species of sphingomyelin containing 2-hydroxylated polyenoic very-long-chain fatty acids in mammalian testes and spermatozoa. J. Biol. Chem. 267, 1746-1751 (1992)
    • (1992) J. Biol. Chem. , vol.267 , pp. 1746-1751
    • Robinson, B.S.1    Johnson, D.W.2    Poulos, A.3
  • 49
    • 0014472414 scopus 로고
    • Synthesis of cerebroside by brain from uridine diphosphate galactose and ceramide containing hydroxy fatty acid
    • Morell, P., Radin, N.S.: Synthesis of cerebroside by brain from uridine diphosphate galactose and ceramide containing hydroxy fatty acid. Biochemistry 8, 506-512 (1969)
    • (1969) Biochemistry , vol.8 , pp. 506-512
    • Morell, P.1    Radin, N.S.2
  • 50
    • 0028882458 scopus 로고
    • The UDP-galactose: Ceramide galactosyltransferase: expression pattern in oligodendrocytes and Schwann cells during myelination and substrate preference for hydroxyceramide
    • Schaeren-Wiemers, N., van der Bijl, P., Schwab, M.E.: The UDP-galactose: ceramide galactosyltransferase: expression pattern in oligodendrocytes and Schwann cells during myelination and substrate preference for hydroxyceramide. J. Neurochem. 65, 2267-2278 (1995)
    • (1995) J. Neurochem. , vol.65 , pp. 2267-2278
    • Schaeren-Wiemers, N.1    Van Der Bijl, P.2    Schwab, M.E.3
  • 53
    • 0032742601 scopus 로고    scopus 로고
    • Assay of lactosylceramide synthase and comments on its potential role in signal transduction
    • Chatterjee, S.: Assay of lactosylceramide synthase and comments on its potential role in signal transduction. Methods Enzymol. 311, 73-81 (2000)
    • (2000) Methods Enzymol. , vol.311 , pp. 73-81
    • Chatterjee, S.1
  • 54
    • 52449130577 scopus 로고    scopus 로고
    • 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.K., Setou, M.: Imaging mass spectrometry technology and application on ganglioside study; visualization of age-dependent accumulation of C20-ganglioside molecular species in the mouse hippocampus. PLoS One. 3, e3232 (2008)
    • (2008) PLoS One , vol.3
    • Sugiura, Y.1    Shimma, S.2    Konishi, Y.3    Yamada, M.K.4    Setou, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.