메뉴 건너뛰기




Volumn 21, Issue 12, 2012, Pages 2713-2724

Impaired neurotransmission in ether lipid-deficient nerve terminals

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CALCIUM ION; ETHER LIPID; GLUTAMIC ACID; MALONALDEHYDE; PLASMALOGEN; REACTIVE OXYGEN METABOLITE; SODIUM;

EID: 84861739965     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/dds097     Document Type: Article
Times cited : (46)

References (76)
  • 1
    • 33845339567 scopus 로고    scopus 로고
    • The ether lipid-deficient mouse: tracking down plasmalogen functions
    • Gorgas, K., Teigler, A., Komljenovic, D. and Just, W.W. (2006) The ether lipid-deficient mouse: tracking down plasmalogen functions. Biochim. Biophys. Acta, 1763, 1511-1526.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1511-1526
    • Gorgas, K.1    Teigler, A.2    Komljenovic, D.3    Just, W.W.4
  • 4
    • 0042131525 scopus 로고    scopus 로고
    • Inactivation of ether lipid biosynthesis causes male infertility, defects in eye development and optic nerve hypoplasia in mice
    • Rodemer, C., Thai, T.P., Brugger, B., Kaercher, T., Werner, H., Nave, K.A., Wieland, F., Gorgas, K. and Just, W.W. (2003) Inactivation of ether lipid biosynthesis causes male infertility, defects in eye development and optic nerve hypoplasia in mice. Hum. Mol. Genet., 12, 1881-1895.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1881-1895
    • Rodemer, C.1    Thai, T.P.2    Brugger, B.3    Kaercher, T.4    Werner, H.5    Nave, K.A.6    Wieland, F.7    Gorgas, K.8    Just, W.W.9
  • 5
    • 65549163117 scopus 로고    scopus 로고
    • Defects in myelination, paranode organization and Purkinje cell innervation in the ether lipid-deficient mouse cerebellum
    • Teigler, A., Komljenovic, D., Draguhn, A., Gorgas, K. and Just, W.W. (2009) Defects in myelination, paranode organization and Purkinje cell innervation in the ether lipid-deficient mouse cerebellum. Hum. Mol. Genet., 18, 1897-1908.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 1897-1908
    • Teigler, A.1    Komljenovic, D.2    Draguhn, A.3    Gorgas, K.4    Just, W.W.5
  • 7
    • 0034145724 scopus 로고    scopus 로고
    • Molecular genetics of peroxisomal disorders
    • Moser, H.W. (2000) Molecular genetics of peroxisomal disorders. Front. Biosci., 5, D298-D306.
    • (2000) Front. Biosci. , vol.5
    • Moser, H.W.1
  • 8
    • 14244267510 scopus 로고    scopus 로고
    • Peroxisomal disorders I: biochemistry and genetics of peroxisome biogenesis disorders
    • Wanders, R.J. and Waterham, H.R. (2005) Peroxisomal disorders I: biochemistry and genetics of peroxisome biogenesis disorders. Clin. Genet., 67, 107-133.
    • (2005) Clin. Genet. , vol.67 , pp. 107-133
    • Wanders, R.J.1    Waterham, H.R.2
  • 10
    • 34548565630 scopus 로고    scopus 로고
    • The neurotransmitter cycle and quantal size
    • Edwards, R.H. (2007) The neurotransmitter cycle and quantal size. Neuron, 55, 835-858.
    • (2007) Neuron , vol.55 , pp. 835-858
    • Edwards, R.H.1
  • 11
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • Sudhof, T.C. (2004) The synaptic vesicle cycle. Annu. Rev. Neurosci., 27, 509-547.
    • (2004) Annu. Rev. Neurosci. , vol.27 , pp. 509-547
    • Sudhof, T.C.1
  • 12
    • 0037444568 scopus 로고    scopus 로고
    • 2+ signal for phasic transmitter release at the rat calyx of Held
    • 2+ signal for phasic transmitter release at the rat calyx of Held. J. Physiol., 547, 665-689.
    • (2003) J. Physiol. , vol.547 , pp. 665-689
    • Meinrenken, C.J.1    Borst, J.G.2    Sakmann, B.3
  • 15
    • 58849092285 scopus 로고    scopus 로고
    • Membrane fusion: grappling with SNARE and SM proteins
    • Sudhof, T.C. and Rothman, J.E. (2009) Membrane fusion: grappling with SNARE and SM proteins. Science, 323, 474-477.
    • (2009) Science , vol.323 , pp. 474-477
    • Sudhof, T.C.1    Rothman, J.E.2
  • 16
    • 78149499345 scopus 로고    scopus 로고
    • New views of glutamate transporter structure and function: advances and challenges
    • Jiang, J. and Amara, S.G. (2011) New views of glutamate transporter structure and function: advances and challenges. Neuropharmacology, 60, 172-181.
    • (2011) Neuropharmacology , vol.60 , pp. 172-181
    • Jiang, J.1    Amara, S.G.2
  • 17
    • 34547969807 scopus 로고    scopus 로고
    • Endocytosis: clathrinmediated membrane budding
    • Ungewickell, E.J. and Hinrichsen, L. (2007) Endocytosis: clathrinmediated membrane budding. Curr. Opin. Cell Biol., 19, 417-425.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 417-425
    • Ungewickell, E.J.1    Hinrichsen, L.2
  • 19
    • 0029144334 scopus 로고
    • Bending membranes to the task: structural intermediates in bilayer fusion
    • Chernomordik, L.V. and Zimmerberg, J. (1995) Bending membranes to the task: structural intermediates in bilayer fusion. Curr. Opin. Struct. Biol., 5, 541-547.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 541-547
    • Chernomordik, L.V.1    Zimmerberg, J.2
  • 20
    • 0028301321 scopus 로고
    • Plasmenylethanolamine facilitates rapid membrane fusion: a stopped-flow kinetic investigation correlating the propensity of a major plasma membrane constituent to adopt an HII phase with its ability to promote membrane fusion
    • Glaser, P.E. and Gross, R.W. (1994) Plasmenylethanolamine facilitates rapid membrane fusion: a stopped-flow kinetic investigation correlating the propensity of a major plasma membrane constituent to adopt an HII phase with its ability to promote membrane fusion. Biochemistry, 33, 5805-5812.
    • (1994) Biochemistry , vol.33 , pp. 5805-5812
    • Glaser, P.E.1    Gross, R.W.2
  • 22
    • 0027362739 scopus 로고
    • Energetics of intermediates in membrane fusion: comparison of stalk and inverted micellar intermediate mechanisms
    • Siegel, D.P. (1993) Energetics of intermediates in membrane fusion: comparison of stalk and inverted micellar intermediate mechanisms. Biophys. J., 65, 2124-2140.
    • (1993) Biophys. J. , vol.65 , pp. 2124-2140
    • Siegel, D.P.1
  • 24
    • 0034637146 scopus 로고    scopus 로고
    • Uptake of glutamate into synaptic vesicles by an inorganic phosphate transporter
    • Bellocchio, E.E., Reimer, R.J., Fremeau, R.T. Jr and Edwards, R.H. (2000) Uptake of glutamate into synaptic vesicles by an inorganic phosphate transporter. Science, 289, 957-960.
    • (2000) Science , vol.289 , pp. 957-960
    • Bellocchio, E.E.1    Reimer, R.J.2    Fremeau Jr., R.T.3    Edwards, R.H.4
  • 25
    • 0021260660 scopus 로고
    • Studies on ether phospholipids. II. Comparative composition of various tissues from human, rat and guinea pig
    • Diagne, A., Fauvel, J., Record, M., Chap, H. and Douste-Blazy, L. (1984) Studies on ether phospholipids. II. Comparative composition of various tissues from human, rat and guinea pig. Biochim. Biophys. Acta, 793, 221-231.
    • (1984) Biochim. Biophys. Acta , vol.793 , pp. 221-231
    • Diagne, A.1    Fauvel, J.2    Record, M.3    Chap, H.4    Douste-Blazy, L.5
  • 26
    • 0035102918 scopus 로고    scopus 로고
    • Plasmalogens: biosynthesis and functions
    • Nagan, N. and Zoeller, R.A. (2001) Plasmalogens: biosynthesis and functions. Prog. Lipid Res., 40, 199-229.
    • (2001) Prog. Lipid Res. , vol.40 , pp. 199-229
    • Nagan, N.1    Zoeller, R.A.2
  • 27
    • 77951895530 scopus 로고    scopus 로고
    • Structural remodeling of GPI anchors during biosynthesis and after attachment to proteins
    • Fujita, M. and Kinoshita, T. (2010) Structural remodeling of GPI anchors during biosynthesis and after attachment to proteins. FEBS Lett., 584, 1670-1677.
    • (2010) FEBS Lett , vol.584 , pp. 1670-1677
    • Fujita, M.1    Kinoshita, T.2
  • 28
    • 5444244189 scopus 로고    scopus 로고
    • Biological roles of sulfoglycolipids and pathophysiology of their deficiency
    • Honke, K., Zhang, Y., Cheng, X., Kotani, N. and Taniguchi, N. (2004) Biological roles of sulfoglycolipids and pathophysiology of their deficiency. Glycoconj. J., 21, 59-62.
    • (2004) Glycoconj. J. , vol.21 , pp. 59-62
    • Honke, K.1    Zhang, Y.2    Cheng, X.3    Kotani, N.4    Taniguchi, N.5
  • 29
    • 0036547672 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol (GPI)-anchored proteins
    • Ikezawa, H. (2002) Glycosylphosphatidylinositol (GPI)-anchored proteins. Biol. Pharm. Bull., 25, 409-417.
    • (2002) Biol. Pharm. Bull. , vol.25 , pp. 409-417
    • Ikezawa, H.1
  • 30
    • 65249119361 scopus 로고    scopus 로고
    • Lipid mediators in health and disease: enzymes and receptors as therapeutic targets for the regulation of immunity and inflammation
    • Shimizu, T. (2009) Lipid mediators in health and disease: enzymes and receptors as therapeutic targets for the regulation of immunity and inflammation. Annu. Rev. Pharmacol. Toxicol., 49, 123-150.
    • (2009) Annu. Rev. Pharmacol. Toxicol. , vol.49 , pp. 123-150
    • Shimizu, T.1
  • 31
    • 77951908085 scopus 로고    scopus 로고
    • Formation and regulation of lipid microdomains in cell membranes: theory, modeling, and speculation
    • Fan, J., Sammalkorpi, M. and Haataja, M. (2010) Formation and regulation of lipid microdomains in cell membranes: theory, modeling, and speculation. FEBS Lett., 584, 1678-1684.
    • (2010) FEBS Lett , vol.584 , pp. 1678-1684
    • Fan, J.1    Sammalkorpi, M.2    Haataja, M.3
  • 33
    • 0037065727 scopus 로고    scopus 로고
    • Lipid rafts are enriched in arachidonic acid and plasmenylethanolamine and their composition is independent of caveolin-1 expression: a quantitative electrospray ionization/mass spectrometric analysis
    • Pike, L.J., Han, X., Chung, K.N. and Gross, R.W. (2002) Lipid rafts are enriched in arachidonic acid and plasmenylethanolamine and their composition is independent of caveolin-1 expression: a quantitative electrospray ionization/mass spectrometric analysis. Biochemistry, 41, 2075-2088.
    • (2002) Biochemistry , vol.41 , pp. 2075-2088
    • Pike, L.J.1    Han, X.2    Chung, K.N.3    Gross, R.W.4
  • 34
    • 0035826727 scopus 로고    scopus 로고
    • SNARE proteins are highly enriched in lipid rafts in PC12 cells: implications for the spatial control of exocytosis
    • Chamberlain, L.H., Burgoyne, R.D. and Gould, G.W. (2001) SNARE proteins are highly enriched in lipid rafts in PC12 cells: implications for the spatial control of exocytosis. Proc. Natl Acad. Sci. USA, 98, 5619-5624.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 5619-5624
    • Chamberlain, L.H.1    Burgoyne, R.D.2    Gould, G.W.3
  • 35
    • 0035341309 scopus 로고    scopus 로고
    • SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis
    • Lang, T., Bruns, D., Wenzel, D., Riedel, D., Holroyd, P., Thiele, C. and Jahn, R. (2001) SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis. EMBO J., 20, 2202-2213.
    • (2001) EMBO J , vol.20 , pp. 2202-2213
    • Lang, T.1    Bruns, D.2    Wenzel, D.3    Riedel, D.4    Holroyd, P.5    Thiele, C.6    Jahn, R.7
  • 36
    • 0141816763 scopus 로고    scopus 로고
    • Bioenergetics and transmitter release in the isolated nerve terminal
    • Nicholls, D.G. (2003) Bioenergetics and transmitter release in the isolated nerve terminal. Neurochem. Res., 28, 1433-1441.
    • (2003) Neurochem. Res. , vol.28 , pp. 1433-1441
    • Nicholls, D.G.1
  • 38
    • 0019406669 scopus 로고
    • Chemiluminescent determination of acetylcholine, and continuous detection of its release from torpedo electric organ synapses and synaptosomes
    • Israel, M. and Lesbats, B. (1981) Chemiluminescent determination of acetylcholine, and continuous detection of its release from torpedo electric organ synapses and synaptosomes. Neurochem. Int., 3, 81-90.
    • (1981) Neurochem. Int. , vol.3 , pp. 81-90
    • Israel, M.1    Lesbats, B.2
  • 39
    • 0023373705 scopus 로고
    • Characterization of the exocytotic release of glutamate from guinea-pig cerebral cortical synaptosomes
    • Sanchez-Prieto, J., Sihra, T.S. and Nicholls, D.G. (1987) Characterization of the exocytotic release of glutamate from guinea-pig cerebral cortical synaptosomes. J. Neurochem., 49, 58-64.
    • (1987) J. Neurochem. , vol.49 , pp. 58-64
    • Sanchez-Prieto, J.1    Sihra, T.S.2    Nicholls, D.G.3
  • 40
    • 1442333287 scopus 로고    scopus 로고
    • Plasmalogens: targets for oxidants and major lipophilic antioxidants
    • Engelmann, B. (2004) Plasmalogens: targets for oxidants and major lipophilic antioxidants. Biochem. Soc. Trans., 32, 147-150.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 147-150
    • Engelmann, B.1
  • 41
    • 0032934328 scopus 로고    scopus 로고
    • The protective role of plasmalogens in iron-induced lipid peroxidation
    • Sindelar, P.J., Guan, Z., Dallner, G. and Ernster, L. (1999) The protective role of plasmalogens in iron-induced lipid peroxidation. Free Radic. Biol. Med., 26, 318-324.
    • (1999) Free Radic. Biol. Med. , vol.26 , pp. 318-324
    • Sindelar, P.J.1    Guan, Z.2    Dallner, G.3    Ernster, L.4
  • 42
    • 33745850084 scopus 로고    scopus 로고
    • Peroxyl radicals: inductors of neurodegenerative and other inflammatory diseases. Their origin and how they transform cholesterol, phospholipids, plasmalogens, polyunsaturated fatty acids, sugars, and proteins into deleterious products
    • Spiteller, G. (2006) Peroxyl radicals: inductors of neurodegenerative and other inflammatory diseases. Their origin and how they transform cholesterol, phospholipids, plasmalogens, polyunsaturated fatty acids, sugars, and proteins into deleterious products. Free Radic. Biol. Med., 41, 362-387.
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 362-387
    • Spiteller, G.1
  • 43
    • 0028837204 scopus 로고
    • Evaluation of total antioxidant potential (TRAP) and total antioxidant reactivity from luminol-enhanced chemiluminescence measurements
    • Lissi, E., Salim-Hanna, M., Pascual, C. and del Castillo, M.D. (1995) Evaluation of total antioxidant potential (TRAP) and total antioxidant reactivity from luminol-enhanced chemiluminescence measurements. Free Radic. Biol. Med., 18, 153-158.
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 153-158
    • Lissi, E.1    Salim-Hanna, M.2    Pascual, C.3    del Castillo, M.D.4
  • 44
    • 0033876436 scopus 로고    scopus 로고
    • Glutathione metabolism and oxidative stress in neurodegeneration
    • Dringen, R. (2000) Glutathione metabolism and oxidative stress in neurodegeneration. Eur. J. Biochem., 267, 4903.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4903
    • Dringen, R.1
  • 45
    • 33947615665 scopus 로고    scopus 로고
    • Malondialdehyde as biomarker of oxidative damage to lipids caused by smoking
    • Lykkesfeldt, J. (2007) Malondialdehyde as biomarker of oxidative damage to lipids caused by smoking. Clin. Chim. Acta, 380, 50-58.
    • (2007) Clin. Chim. Acta , vol.380 , pp. 50-58
    • Lykkesfeldt, J.1
  • 46
    • 47349130525 scopus 로고    scopus 로고
    • Armet, a UPR-upregulated protein, inhibits cell proliferation and ER stress-induced cell death
    • Apostolou, A., Shen, Y., Liang, Y., Luo, J. and Fang, S. (2008) Armet, a UPR-upregulated protein, inhibits cell proliferation and ER stress-induced cell death. Exp. Cell Res., 314, 2454-2467.
    • (2008) Exp. Cell Res. , vol.314 , pp. 2454-2467
    • Apostolou, A.1    Shen, Y.2    Liang, Y.3    Luo, J.4    Fang, S.5
  • 49
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: from stress pathway to homeostatic regulation
    • Walter, P. and Ron, D. (2011) The unfolded protein response: from stress pathway to homeostatic regulation. Science, 334, 1081-1086.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 50
    • 0023823059 scopus 로고
    • 2+ concentration in isolated nerve terminals following metabolic inhibition: possible relevance to hypoglycaemia and anoxia
    • 2+ concentration in isolated nerve terminals following metabolic inhibition: possible relevance to hypoglycaemia and anoxia. Neuroscience, 27, 175-182.
    • (1988) Neuroscience , vol.27 , pp. 175-182
    • Kauppinen, R.A.1    McMahon, H.T.2    Nicholls, D.G.3
  • 51
    • 0034092375 scopus 로고    scopus 로고
    • Neurotransmitter release at rapid synapses
    • Dunant, Y. and Israel, M. (2000) Neurotransmitter release at rapid synapses. Biochimie, 82, 289-302.
    • (2000) Biochimie , vol.82 , pp. 289-302
    • Dunant, Y.1    Israel, M.2
  • 52
    • 56149119337 scopus 로고    scopus 로고
    • Glutamate forward and reverse transport: from molecular mechanism to transporter-mediated release after ischemia
    • Grewer, C., Gameiro, A., Zhang, Z., Tao, Z., Braams, S. and Rauen, T. (2008) Glutamate forward and reverse transport: from molecular mechanism to transporter-mediated release after ischemia. IUBMB Life, 60, 609-619.
    • (2008) IUBMB Life , vol.60 , pp. 609-619
    • Grewer, C.1    Gameiro, A.2    Zhang, Z.3    Tao, Z.4    Braams, S.5    Rauen, T.6
  • 53
    • 0020448447 scopus 로고
    • Binding order of substrates to the sodium and potassium ion coupled L-glutamic acid transporter from rat brain
    • Kanner, B.I. and Bendahan, A. (1982) Binding order of substrates to the sodium and potassium ion coupled L-glutamic acid transporter from rat brain. Biochemistry, 21, 6327-6330.
    • (1982) Biochemistry , vol.21 , pp. 6327-6330
    • Kanner, B.I.1    Bendahan, A.2
  • 54
    • 79952101282 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in brain aging: role of oxidative stress and cardiolipin
    • Paradies, G., Petrosillo, G., Paradies, V. and Ruggiero, F.M. (2011) Mitochondrial dysfunction in brain aging: role of oxidative stress and cardiolipin. Neurochem. Int., 58, 447-457.
    • (2011) Neurochem. Int. , vol.58 , pp. 447-457
    • Paradies, G.1    Petrosillo, G.2    Paradies, V.3    Ruggiero, F.M.4
  • 55
    • 67349122764 scopus 로고    scopus 로고
    • Over-expression of the anti-apoptotic protein Bcl-2 affects membrane lipid composition in HL-60 cells
    • Cantrel, C., Zachowski, A. and Geny, B. (2009) Over-expression of the anti-apoptotic protein Bcl-2 affects membrane lipid composition in HL-60 cells. Lipids, 44, 499-509.
    • (2009) Lipids , vol.44 , pp. 499-509
    • Cantrel, C.1    Zachowski, A.2    Geny, B.3
  • 57
    • 0041534405 scopus 로고    scopus 로고
    • Calcium dynamics and endoplasmic reticular function in the regulation of protein synthesis: implications for cell growth and adaptability
    • Brostrom, M.A. and Brostrom, C.O. (2003) Calcium dynamics and endoplasmic reticular function in the regulation of protein synthesis: implications for cell growth and adaptability. Cell Calcium, 34, 345-363.
    • (2003) Cell Calcium , vol.34 , pp. 345-363
    • Brostrom, M.A.1    Brostrom, C.O.2
  • 58
    • 46749121318 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress response in murine kidney exposed to acute hypobaric hypoxia
    • Karar, J., Dolt, K.S. and Qadar Pasha, M.A. (2008) Endoplasmic reticulum stress response in murine kidney exposed to acute hypobaric hypoxia. FEBS Lett., 582, 2521-2526.
    • (2008) FEBS Lett , vol.582 , pp. 2521-2526
    • Karar, J.1    Dolt, K.S.2    Qadar Pasha, M.A.3
  • 59
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron, D. and Walter, P. (2007) Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol., 8, 519-529.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 60
    • 0032579194 scopus 로고    scopus 로고
    • The selective activation of the cardiac sarcolemmal sodium-calcium exchanger by plasmalogenic phosphatidic acid produced by phospholipase D
    • Hale, C.C., Ebeling, E.G., Hsu, F.F. and Ford, D.A. (1998) The selective activation of the cardiac sarcolemmal sodium-calcium exchanger by plasmalogenic phosphatidic acid produced by phospholipase D. FEBS Lett., 422, 247-251.
    • (1998) FEBS Lett , vol.422 , pp. 247-251
    • Hale, C.C.1    Ebeling, E.G.2    Hsu, F.F.3    Ford, D.A.4
  • 61
    • 0023782245 scopus 로고
    • A possible role for plasmalogens in protecting animal cells against photosensitized killing
    • Zoeller, R.A., Morand, O.H. and Raetz, C.R. (1988) A possible role for plasmalogens in protecting animal cells against photosensitized killing. J. Biol. Chem., 263, 11590-11596.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11590-11596
    • Zoeller, R.A.1    Morand, O.H.2    Raetz, C.R.3
  • 62
    • 0033806740 scopus 로고    scopus 로고
    • Peroxidation of arachidonate containing plasmenyl glycerophosphocholine: facile oxidation of esterified arachidonate at carbon-5
    • Khaselev, N. and Murphy, R.C. (2000) Peroxidation of arachidonate containing plasmenyl glycerophosphocholine: facile oxidation of esterified arachidonate at carbon-5. Free Radic. Biol. Med., 29, 620-632.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 620-632
    • Khaselev, N.1    Murphy, R.C.2
  • 63
    • 0035890031 scopus 로고    scopus 로고
    • Plasmalogen degradation by oxidative stress: production and disappearance of specific fatty aldehydes and fatty alpha-hydroxyaldehydes
    • Stadelmann-Ingrand, S., Favreliere, S., Fauconneau, B., Mauco, G. and Tallineau, C. (2001) Plasmalogen degradation by oxidative stress: production and disappearance of specific fatty aldehydes and fatty alpha-hydroxyaldehydes. Free Radic. Biol. Med., 31, 1263-1271.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1263-1271
    • Stadelmann-Ingrand, S.1    Favreliere, S.2    Fauconneau, B.3    Mauco, G.4    Tallineau, C.5
  • 64
    • 0022531676 scopus 로고
    • A rapid method for isolation of synaptosomes on Percoll gradients
    • Dunkley, P.R., Jarvie, P.E., Heath, J.W., Kidd, G.J. and Rostas, J.A. (1986) A rapid method for isolation of synaptosomes on Percoll gradients. Brain Res., 372, 115-129.
    • (1986) Brain Res , vol.372 , pp. 115-129
    • Dunkley, P.R.1    Jarvie, P.E.2    Heath, J.W.3    Kidd, G.J.4    Rostas, J.A.5
  • 65
    • 13844272574 scopus 로고    scopus 로고
    • Synaptic proteins and SNARE complexes are localized in lipid rafts from rat brain synaptosomes
    • Gil, C., Soler-Jover, A., Blasi, J. and Aguilera, J. (2005) Synaptic proteins and SNARE complexes are localized in lipid rafts from rat brain synaptosomes. Biochem. Biophys. Res. Commun., 329, 117-124.
    • (2005) Biochem. Biophys. Res. Commun. , vol.329 , pp. 117-124
    • Gil, C.1    Soler-Jover, A.2    Blasi, J.3    Aguilera, J.4
  • 66
    • 12144291075 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef activates p21-activated kinase via recruitment into lipid rafts
    • Krautkramer, E., Giese, S.I., Gasteier, J.E., Muranyi, W. and Fackler, O.T. (2004) Human immunodeficiency virus type 1 Nef activates p21-activated kinase via recruitment into lipid rafts. J. Virol., 78, 4085-4097.
    • (2004) J. Virol. , vol.78 , pp. 4085-4097
    • Krautkramer, E.1    Giese, S.I.2    Gasteier, J.E.3    Muranyi, W.4    Fackler, O.T.5
  • 67
    • 0022476828 scopus 로고
    • Synaptosomal bioenergetics. The role of glycolysis, pyruvate oxidation and responses to hypoglycaemia
    • Kauppinen, R.A. and Nicholls, D.G. (1986) Synaptosomal bioenergetics. The role of glycolysis, pyruvate oxidation and responses to hypoglycaemia. Eur. J. Biochem., 158, 159-165.
    • (1986) Eur. J. Biochem. , vol.158 , pp. 159-165
    • Kauppinen, R.A.1    Nicholls, D.G.2
  • 68
    • 0033817427 scopus 로고    scopus 로고
    • Two mechanisms of synaptic vesicle recycling in rat brain nerve terminals
    • Cousin, M.A. and Robinson, P.J. (2000) Two mechanisms of synaptic vesicle recycling in rat brain nerve terminals. J. Neurochem., 75, 1645-1653.
    • (2000) J. Neurochem. , vol.75 , pp. 1645-1653
    • Cousin, M.A.1    Robinson, P.J.2
  • 69
    • 0028384726 scopus 로고
    • Enhanced chemiluminescent assays for acetylcholine
    • Ternaux, J.P. and Chamoin, M.C. (1994) Enhanced chemiluminescent assays for acetylcholine. J. Biolumin. Chemilumin., 9, 65-72.
    • (1994) J. Biolumin. Chemilumin. , vol.9 , pp. 65-72
    • Ternaux, J.P.1    Chamoin, M.C.2
  • 70
    • 0015384891 scopus 로고
    • Determination of protein: a modification of the Lowry method that gives a linear photometric response
    • Hartree, E.F. (1972) Determination of protein: a modification of the Lowry method that gives a linear photometric response. Anal. Biochem., 48, 422-427.
    • (1972) Anal. Biochem. , vol.48 , pp. 422-427
    • Hartree, E.F.1
  • 71
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E.G. and Dyer, W.J. (1959) A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol., 37, 911-917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 72
    • 0030962474 scopus 로고    scopus 로고
    • Quantitative analysis of biological membrane lipids at the low picomole level by nano-electrospray ionization tandem mass spectrometry
    • Brugger, B., Erben, G., Sandhoff, R., Wieland, F.T. and Lehmann, W.D. (1997) Quantitative analysis of biological membrane lipids at the low picomole level by nano-electrospray ionization tandem mass spectrometry. Proc. Natl Acad. Sci. USA, 94, 2339-2344.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 2339-2344
    • Brugger, B.1    Erben, G.2    Sandhoff, R.3    Wieland, F.T.4    Lehmann, W.D.5
  • 73
    • 1542379962 scopus 로고    scopus 로고
    • The membrane domains occupied by glycosylphosphatidylinositol-anchored prion protein and Thy-1 differ in lipid composition
    • Brugger, B., Graham, C., Leibrecht, I., Mombelli, E., Jen, A., Wieland, F. and Morris, R. (2004) The membrane domains occupied by glycosylphosphatidylinositol-anchored prion protein and Thy-1 differ in lipid composition. J. Biol. Chem., 279, 7530-7536.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7530-7536
    • Brugger, B.1    Graham, C.2    Leibrecht, I.3    Mombelli, E.4    Jen, A.5    Wieland, F.6    Morris, R.7
  • 74
    • 0014779155 scopus 로고
    • Two dimensional then layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots
    • Rouser, G., Fkeischer, S. and Yamamoto, A. (1970) Two dimensional then layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots. Lipids, 5, 494-496.
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rouser, G.1    Fkeischer, S.2    Yamamoto, A.3
  • 75
    • 0021913861 scopus 로고
    • Fatty acid metabolism and cell proliferation VII. Antioxidant effects of tocopherols and their quinones
    • Lindsey, J.A., Zhang, H.F., Kaseki, H., Morisaki, N., Sato, T. and Cornwell, D.G. (1985) Fatty acid metabolism and cell proliferation. VII. Antioxidant effects of tocopherols and their quinones. Lipids, 20, 151-157.
    • (1985) Lipids , vol.20 , pp. 151-157
    • Lindsey, J.A.1    Zhang, H.F.2    Kaseki, H.3    Morisaki, N.4    Sato, T.5    Cornwell, D.G.6
  • 76
    • 0015321948 scopus 로고
    • A methodology for analysis of tissue sulfhydryl components
    • Boyne, A.F. and Ellman, G.L. (1972) A methodology for analysis of tissue sulfhydryl components. Anal. Biochem., 46, 639-653.
    • (1972) Anal. Biochem. , vol.46 , pp. 639-653
    • Boyne, A.F.1    Ellman, G.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.