메뉴 건너뛰기




Volumn 1262, Issue 1, 2012, Pages 85-92

Effects of plasmalogens on systemic lipopolysaccharide-induced glial activation and β-amyloid accumulation in adult mice

Author keywords

Alzheimer's disease; Microglia; Neuroinflammation; Phospholipids

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-16]; CORN OIL; LIPOPOLYSACCHARIDE; PLASMALOGEN; UNCLASSIFIED DRUG;

EID: 84864132951     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2012.06641.x     Document Type: Article
Times cited : (60)

References (52)
  • 1
    • 15744382068 scopus 로고    scopus 로고
    • Effects of intraperitoneal lipopolysaccharide on Morris maze performance in year-old and 2-month-old female C57BL/6J mice
    • Boehm, G.W. et al. 2005. Effects of intraperitoneal lipopolysaccharide on Morris maze performance in year-old and 2-month-old female C57BL/6J mice. Behav. Brain Res. 159: 145-151.
    • (2005) Behav. Brain Res. , vol.159 , pp. 145-151
    • Boehm, G.W.1
  • 2
    • 53349129897 scopus 로고    scopus 로고
    • Neuro-inflammation induced by lipopolysaccharide causes cognitive impairment through enhancement of β-amyloid generation
    • Lee, J.W., et al. 2008. Neuro-inflammation induced by lipopolysaccharide causes cognitive impairment through enhancement of β-amyloid generation. J. Neuroinflammation 5: 37.
    • (2008) J. Neuroinflammation , vol.5 , pp. 37
    • Lee, J.W.1
  • 3
    • 0034990845 scopus 로고    scopus 로고
    • Lipopolysaccharide causes deficits in spatial learning in the watermaze but not in BDNF expression in the rat dentate gyrus
    • O'mara, S.M., K.N. Shaw & S. Commins. 2001. Lipopolysaccharide causes deficits in spatial learning in the watermaze but not in BDNF expression in the rat dentate gyrus. Behav. Brain Res. 124: 47-54.
    • (2001) Behav. Brain Res. , vol.124 , pp. 47-54
    • O'mara, S.M.1    Shaw, K.N.2    Commins, S.3
  • 4
    • 0035660484 scopus 로고    scopus 로고
    • Ibuprofen decreases cytokine-induced amyloid β production in neuronal cells
    • Blasko, I., et al. 2001. Ibuprofen decreases cytokine-induced amyloid β production in neuronal cells. Neurobiol. Dis. 8: 1094-1101.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 1094-1101
    • Blasko, I.1
  • 5
    • 0242609178 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs and peroxisome proliferator-activated receptor-γ agonists modulate immunostimulated processing of amyloid precursor protein through regulation of β-secretase
    • Sastre, M., et al. 2003. Nonsteroidal anti-inflammatory drugs and peroxisome proliferator-activated receptor-γ agonists modulate immunostimulated processing of amyloid precursor protein through regulation of β-secretase. J. Neurosci. 23: 9796-9804.
    • (2003) J. Neurosci. , vol.23 , pp. 9796-9804
    • Sastre, M.1
  • 6
    • 0041921071 scopus 로고    scopus 로고
    • Anti-inflammatory drug therapy alters β-amyloid processing and deposition in an animal model of Alzheimer's disease
    • Yan, Q., et al. 2003. Anti-inflammatory drug therapy alters β-amyloid processing and deposition in an animal model of Alzheimer's disease. J. Neurosci. 23: 7504-7509.
    • (2003) J. Neurosci. , vol.23 , pp. 7504-7509
    • Yan, Q.1
  • 7
    • 0034997561 scopus 로고    scopus 로고
    • Plasmalogens: workhorse lipids of membranes in normal and injured neurons and glia
    • Farooqui, A.A. & L.A. Horrocks. 2001. Plasmalogens: workhorse lipids of membranes in normal and injured neurons and glia. Neuroscientist 7: 232-245.
    • (2001) Neuroscientist , vol.7 , pp. 232-245
    • Farooqui, A.A.1    Horrocks, L.A.2
  • 8
    • 0035317548 scopus 로고    scopus 로고
    • Plasmalogens, phospholipase A2, and docosahexaenoic acid turnover in brain tissue
    • discussion 279-284.
    • Farooqui, A.A. & L.A. Horrocks. 2001. Plasmalogens, phospholipase A2, and docosahexaenoic acid turnover in brain tissue. J. Mol. Neurosci. 16: 263-272; discussion 279-284.
    • (2001) J. Mol. Neurosci. , vol.16 , pp. 263-272
    • Farooqui, A.A.1    Horrocks, L.A.2
  • 9
    • 77955087025 scopus 로고    scopus 로고
    • Studies on plasmalogen-selective phospholipase A2 in brain
    • Farooqui, A.A. 2010. Studies on plasmalogen-selective phospholipase A2 in brain. Mol. Neurobiol. 41: 267-273.
    • (2010) Mol. Neurobiol. , vol.41 , pp. 267-273
    • Farooqui, A.A.1
  • 10
    • 0032953013 scopus 로고    scopus 로고
    • Susceptibility of plasmenyl glycerophosphoethanolamine lipids containing arachidonate to oxidative degradation
    • Khaselev, N. & R.C. Murphy. 1999. Susceptibility of plasmenyl glycerophosphoethanolamine lipids containing arachidonate to oxidative degradation. Free Radic. Biol. Med. 26: 275-284.
    • (1999) Free Radic. Biol. Med. , vol.26 , pp. 275-284
    • Khaselev, N.1    Murphy, R.C.2
  • 11
    • 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
  • 12
    • 0037428255 scopus 로고    scopus 로고
    • Ethanolamine plasmalogen and cholesterol reduce the total membrane oxidizability measured by the oxygen uptake method
    • Maeba, R. & N. Ueta. 2003. Ethanolamine plasmalogen and cholesterol reduce the total membrane oxidizability measured by the oxygen uptake method. Biochem. Biophys. Res. Commun. 302: 265-270.
    • (2003) Biochem. Biophys. Res. Commun. , vol.302 , pp. 265-270
    • Maeba, R.1    Ueta, N.2
  • 13
    • 0015297279 scopus 로고
    • Oxygen-dependent cleavage of the vinyl -ether linkage of plasmalogens: 2. Identification of the low-molecular-weight active component and the reaction mechanism
    • Yavin, E. & S. Gatt. 1972. Oxygen-dependent cleavage of the vinyl -ether linkage of plasmalogens: 2. Identification of the low-molecular-weight active component and the reaction mechanism. Eur. J. Biochem. 25: 437-446.
    • (1972) Eur. J. Biochem. , vol.25 , pp. 437-446
    • Yavin, E.1    Gatt, S.2
  • 14
    • 0028809962 scopus 로고
    • Disease and anatomic specificity of ethanolamine plasmalogen deficiency in Alzheimer's disease brain
    • Ginsberg, L., et al. 1995. Disease and anatomic specificity of ethanolamine plasmalogen deficiency in Alzheimer's disease brain. Brain Res. 698: 223-226.
    • (1995) Brain Res. , vol.698 , pp. 223-226
    • Ginsberg, L.1
  • 15
    • 0032770167 scopus 로고    scopus 로고
    • Decrease and structural modifications of phosphatidylethanolamine plasmalogen in the brain with Alzheimer disease
    • Guan, Z., et al. 1999. Decrease and structural modifications of phosphatidylethanolamine plasmalogen in the brain with Alzheimer disease. J. Neuropathol. Exp. Neurol. 58: 740-747.
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 740-747
    • Guan, Z.1
  • 16
    • 0035023152 scopus 로고    scopus 로고
    • Plasmalogen deficiency in early Alzheimer's disease subjects and in animal models: molecular characterization using electrospray ionization mass spectrometry
    • Han, X., D.M. Holtzman & D.W. McKeel, Jr. 2001. Plasmalogen deficiency in early Alzheimer's disease subjects and in animal models: molecular characterization using electrospray ionization mass spectrometry. J. Neurochem. 77: 1168-1180.
    • (2001) J. Neurochem. , vol.77 , pp. 1168-1180
    • Han, X.1    Holtzman, D.M.2    McKeel Jr., D.W.3
  • 17
    • 0031745753 scopus 로고    scopus 로고
    • Membrane instability, plasmalogen content, and Alzheimer's disease
    • Ginsberg, L., J.H. Xuereb & N.L. Gershfeld. 1998. Membrane instability, plasmalogen content, and Alzheimer's disease. J. Neurochem. 70: 2533-2538.
    • (1998) J. Neurochem. , vol.70 , pp. 2533-2538
    • Ginsberg, L.1    Xuereb, J.H.2    Gershfeld, N.L.3
  • 18
    • 35848965696 scopus 로고    scopus 로고
    • Peripheral ethanolamine plasmalogen deficiency: a logical causative factor in Alzheimer's disease and dementia
    • Goodenowe, D.B., et al. 2007. Peripheral ethanolamine plasmalogen deficiency: a logical causative factor in Alzheimer's disease and dementia. J. Lipid Res. 48: 2485-2498.
    • (2007) J. Lipid Res. , vol.48 , pp. 2485-2498
    • Goodenowe, D.B.1
  • 19
    • 75449092205 scopus 로고    scopus 로고
    • Circulating plasmalogen levels and Alzheimer disease assessment scale-cognitive scores in Alzheimer patients
    • Wood, P.L., et al. 2010. Circulating plasmalogen levels and Alzheimer disease assessment scale-cognitive scores in Alzheimer patients. J. Psychiat. Neurosci. 35: 59-62.
    • (2010) J. Psychiat. Neurosci. , vol.35 , pp. 59-62
    • Wood, P.L.1
  • 20
    • 74349084174 scopus 로고    scopus 로고
    • Simultaneous preparation of purified plasmalogens and sphingomyelin in human erythrocytes with phospholipase A1 from Aspergillus orizae
    • Mawatari, S., et al. 2009. Simultaneous preparation of purified plasmalogens and sphingomyelin in human erythrocytes with phospholipase A1 from Aspergillus orizae. Biosci. Biotechnol. Biochem. 73: 2621-2625.
    • (2009) Biosci. Biotechnol. Biochem. , vol.73 , pp. 2621-2625
    • Mawatari, S.1
  • 21
    • 34548646523 scopus 로고    scopus 로고
    • Separation of intact plasmalogens and all other phospholipids by a single run of high-performance liquid chromatography
    • Mawatari, S., Y. Okuma & T. Fujino. 2007. Separation of intact plasmalogens and all other phospholipids by a single run of high-performance liquid chromatography. Anal. Biochem. 370: 54-59.
    • (2007) Anal. Biochem. , vol.370 , pp. 54-59
    • Mawatari, S.1    Okuma, Y.2    Fujino, T.3
  • 22
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipides from animal tissues
    • Folch, J., M. Lees & G.H. Sloane Stanley. 1957. A simple method for the isolation and purification of total lipides from animal tissues. J. Biol. Chem. 226: 497-509.
    • (1957) J. Biol. Chem. , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Sloane Stanley, G.H.3
  • 24
    • 0032621790 scopus 로고    scopus 로고
    • TNFα plus IFNγ induce the production of Alzheimer β-amyloid peptides and decrease the secretion of APPs
    • Blasko, I., et al. 1999. TNFα plus IFNγ induce the production of Alzheimer β-amyloid peptides and decrease the secretion of APPs. FASEB J. 13: 63-68.
    • (1999) FASEB J. , vol.13 , pp. 63-68
    • Blasko, I.1
  • 25
    • 0030908591 scopus 로고    scopus 로고
    • Delayed oxidative degradation of polyunsaturated diacyl phospholipids in the presence of plasmalogen phospholipids in vitro
    • Reiss, D., K. Beyer & B. Engelmann. 1997. Delayed oxidative degradation of polyunsaturated diacyl phospholipids in the presence of plasmalogen phospholipids in vitro. Biochem. J. 323(Pt 3): 807-814.
    • (1997) Biochem. J. , vol.323 , Issue.PART 3 , pp. 807-814
    • Reiss, D.1    Beyer, K.2    Engelmann, B.3
  • 26
    • 0036073192 scopus 로고    scopus 로고
    • Increasing plasmalogen levels protects human endothelial cells during hypoxia
    • Zoeller, R.A., et al. 2002. Increasing plasmalogen levels protects human endothelial cells during hypoxia. Am. J. Physiol. Heart Circ. Physiol. 283: H671-H679.
    • (2002) Am. J. Physiol. Heart Circ. Physiol. , vol.283
    • Zoeller, R.A.1
  • 27
    • 0030969328 scopus 로고    scopus 로고
    • Oxidative injury of synapse and alteration of antioxidative defense systems in rats, and its prevention by vitamin E
    • Urano, S., et al. 1997. Oxidative injury of synapse and alteration of antioxidative defense systems in rats, and its prevention by vitamin E. Eur. J Biochem./FEBS 245: 64-70.
    • (1997) Eur. J Biochem./FEBS , vol.245 , pp. 64-70
    • Urano, S.1
  • 28
    • 0025968822 scopus 로고
    • Stabilization of non-bilayer structures by the etherlipid ethanolamine plasmalogen
    • Lohner, K., et al. 1991. Stabilization of non-bilayer structures by the etherlipid ethanolamine plasmalogen. Biochim. Biophys. Acta 1061: 132-140.
    • (1991) Biochim. Biophys. Acta , vol.1061 , pp. 132-140
    • Lohner, K.1
  • 29
    • 0015900528 scopus 로고
    • Adult rat brain synaptic vesicles. II. Lipid composition
    • Breckenridge, W.C., et al. 1973. Adult rat brain synaptic vesicles. II. Lipid composition. Biochim. Biophys. Acta 320: 681-686.
    • (1973) Biochim. Biophys. Acta , vol.320 , pp. 681-686
    • Breckenridge, W.C.1
  • 30
    • 0141482022 scopus 로고    scopus 로고
    • Exclusively targeting β-secretase to lipid rafts by GPI-anchor addition up-regulates β-site processing of the amyloid precursor protein
    • Cordy, J.M., et al. 2003. Exclusively targeting β-secretase to lipid rafts by GPI-anchor addition up-regulates β-site processing of the amyloid precursor protein. Proc. Natl. Acad. Sci. U.S.A. 100: 11735-11740.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 11735-11740
    • Cordy, J.M.1
  • 31
    • 0035928732 scopus 로고    scopus 로고
    • Compartmentalization of β-secretase (Asp2) into low-buoyant density, noncaveolar lipid rafts
    • Riddell, D.R., et al. 2001. Compartmentalization of β-secretase (Asp2) into low-buoyant density, noncaveolar lipid rafts. Curr. Biol. 11: 1288-1293.
    • (2001) Curr. Biol. , vol.11 , pp. 1288-1293
    • Riddell, D.R.1
  • 32
    • 0036591849 scopus 로고    scopus 로고
    • Lipid peroxidation and protein oxidation in Alzheimer's disease brain: potential causes and consequences involving amyloid β-peptide-associated free radical oxidative stress
    • Butterfield, D.A. & C.M. Lauderback. 2002. Lipid peroxidation and protein oxidation in Alzheimer's disease brain: potential causes and consequences involving amyloid β-peptide-associated free radical oxidative stress. Free Radic. Biol. Med. 32: 1050-1060.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1050-1060
    • Butterfield, D.A.1    Lauderback, C.M.2
  • 33
    • 0033954991 scopus 로고    scopus 로고
    • Oxidative stress and Alzheimer disease
    • Christen, Y. 2000. Oxidative stress and Alzheimer disease. Am. J. Clin. Nutr. 71: 621S-629S.
    • (2000) Am. J. Clin. Nutr. , vol.71
    • Christen, Y.1
  • 34
    • 79851471469 scopus 로고    scopus 로고
    • Plasmalogen synthesis is regulated via alkyl-dihydroxyacetonephosphate-synthase by amyloid precursor protein processing and is affected in Alzheimer's disease
    • Grimm, M.O.W., et al. 2011. Plasmalogen synthesis is regulated via alkyl-dihydroxyacetonephosphate-synthase by amyloid precursor protein processing and is affected in Alzheimer's disease. J. Neurochem. 116: 916-925.
    • (2011) J. Neurochem. , vol.116 , pp. 916-925
    • Grimm, M.O.W.1
  • 35
    • 0037207510 scopus 로고    scopus 로고
    • TNFα downregulates PPARδ expression in oligodendrocyte progenitor cells: implications for demyelinating diseases
    • Cimini, A., et al. 2003. TNFα downregulates PPARδ expression in oligodendrocyte progenitor cells: implications for demyelinating diseases. Glia 41: 3-14.
    • (2003) Glia , vol.41 , pp. 3-14
    • Cimini, A.1
  • 36
    • 78049367417 scopus 로고    scopus 로고
    • Mouse brain plasmalogens are targets for hypochlorous acid-mediated modification in vitro and in vivo
    • Üllen, A., et al. 2010. Mouse brain plasmalogens are targets for hypochlorous acid-mediated modification in vitro and in vivo. Free Rad. Biol. Med. 49: 1655-1665.
    • (2010) Free Rad. Biol. Med. , vol.49 , pp. 1655-1665
    • Üllen, A.1
  • 37
    • 0037219040 scopus 로고    scopus 로고
    • Signaling events mediating activation of brain ethanolamine plasmalogen hydrolysis by ceramide
    • Latorre, E., et al. 2003. Signaling events mediating activation of brain ethanolamine plasmalogen hydrolysis by ceramide. Eur. J. Biochem. 270: 36-46.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 36-46
    • Latorre, E.1
  • 38
    • 0037244159 scopus 로고    scopus 로고
    • Deficiency in ethanolamine plasmalogen leads to altered cholesterol transport
    • Munn, N.J., et al. 2003. Deficiency in ethanolamine plasmalogen leads to altered cholesterol transport. J. Lipid Res. 44: 182-192.
    • (2003) J. Lipid Res. , vol.44 , pp. 182-192
    • Munn, N.J.1
  • 39
    • 0033519601 scopus 로고    scopus 로고
    • The role of cholesterol in the biosynthesis of β-amyloid
    • Frears, E.R., et al. 1999. The role of cholesterol in the biosynthesis of β-amyloid. Neuroreport 10: 1699-1705.
    • (1999) Neuroreport , vol.10 , pp. 1699-1705
    • Frears, E.R.1
  • 40
    • 0345669752 scopus 로고    scopus 로고
    • Alzheimer's disease: the cholesterol connection
    • Puglielli, L., R.E. Tanzi & D.M. Kovacs. 2003. Alzheimer's disease: the cholesterol connection. Nat. Neurosci. 6: 345-351.
    • (2003) Nat. Neurosci. , vol.6 , pp. 345-351
    • Puglielli, L.1    Tanzi, R.E.2    Kovacs, D.M.3
  • 41
    • 0032568552 scopus 로고    scopus 로고
    • Cholesterol depletion inhibits the generation of β-amyloid in hippocampal neurons
    • Simons, M., et al. 1998. Cholesterol depletion inhibits the generation of β-amyloid in hippocampal neurons. Proc. Natl. Acad. Sci. U.S.A. 95: 6460-6464.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6460-6464
    • Simons, M.1
  • 42
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10
    • Kojro, E., et al. 2001. Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10. Proc. Natl. Acad. Sci. U.S.A. 98: 5815-5820.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 5815-5820
    • Kojro, E.1
  • 43
    • 0344667494 scopus 로고    scopus 로고
    • Membrane dynamics, cholesterol homeostasis, and Alzheimer's disease
    • Chauhan, N.B. 2003. Membrane dynamics, cholesterol homeostasis, and Alzheimer's disease. J. Lipid. Res. 44: 2019-2029.
    • (2003) J. Lipid. Res. , vol.44 , pp. 2019-2029
    • Chauhan, N.B.1
  • 44
    • 34247330919 scopus 로고    scopus 로고
    • Modulation of inflammation in brain: a matter of fat
    • Farooqui, A.A., L.A. Horrocks & T. Farooqui. 2007. Modulation of inflammation in brain: a matter of fat. J. Neurochem. 101: 577-599.
    • (2007) J. Neurochem. , vol.101 , pp. 577-599
    • Farooqui, A.A.1    Horrocks, L.A.2    Farooqui, T.3
  • 45
    • 4444223956 scopus 로고    scopus 로고
    • Docosahexaenoic acid protects from dendritic pathology in an Alzheimer's disease mouse model
    • Calon, F., et al. 2004. Docosahexaenoic acid protects from dendritic pathology in an Alzheimer's disease mouse model. Neuron 43: 633-645.
    • (2004) Neuron , vol.43 , pp. 633-645
    • Calon, F.1
  • 46
    • 77955089907 scopus 로고    scopus 로고
    • Omega-3 essential fatty acids modulate initiation and progression of neurodegenerative disease
    • Palacios-Pelaez, R., W.J. Lukiw & N.G. Bazan. 2010. Omega-3 essential fatty acids modulate initiation and progression of neurodegenerative disease. Mol. Neurobiol. 41: 367-374.
    • (2010) Mol. Neurobiol. , vol.41 , pp. 367-374
    • Palacios-Pelaez, R.1    Lukiw, W.J.2    Bazan, N.G.3
  • 47
    • 39749122734 scopus 로고    scopus 로고
    • The opposing effects of n-3 and n-6 fatty acids
    • Schmitz, G. & J. Ecker. 2008. The opposing effects of n-3 and n-6 fatty acids. Prog. Lipid Res. 47: 147-155.
    • (2008) Prog. Lipid Res. , vol.47 , pp. 147-155
    • Schmitz, G.1    Ecker, J.2
  • 48
    • 79954592687 scopus 로고    scopus 로고
    • Docosahexaenoic acid reduces amyloid beta production via multiple pleiotropic mechanisms
    • Grimm, M.O.W., et al. 2011. Docosahexaenoic acid reduces amyloid beta production via multiple pleiotropic mechanisms. J. Biol. Chem. 286: 14028-14039.
    • (2011) J. Biol. Chem. , vol.286 , pp. 14028-14039
    • Grimm, M.O.W.1
  • 49
    • 5344277556 scopus 로고    scopus 로고
    • Deciphering the molecular basis of memory failure in Alzheimer's disease
    • Walsh, D.M. & D.J. Selkoe. 2004. Deciphering the molecular basis of memory failure in Alzheimer's disease. Neuron 44: 181-193.
    • (2004) Neuron , vol.44 , pp. 181-193
    • Walsh, D.M.1    Selkoe, D.J.2
  • 50
    • 33747180133 scopus 로고    scopus 로고
    • Impact of different saturated fatty acid, polyunsaturated fatty acid and cholesterol containing diets on β-amyloid accumulation in APP/PS1 transgenic mice
    • Oksman, M., et al. 2006. Impact of different saturated fatty acid, polyunsaturated fatty acid and cholesterol containing diets on β-amyloid accumulation in APP/PS1 transgenic mice. Neurobiol. Dis. 23: 563-572.
    • (2006) Neurobiol. Dis. , vol.23 , pp. 563-572
    • Oksman, M.1
  • 51
    • 0039369595 scopus 로고
    • Membrane docosahexaenoate is supplied to the developing brain and retina by the liver
    • Scott, B.L. & N.G. Bazan. 1989. Membrane docosahexaenoate is supplied to the developing brain and retina by the liver. Proc. Natl. Acad. Sci. U.S.A. 86: 2903-2907.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 2903-2907
    • Scott, B.L.1    Bazan, N.G.2
  • 52
    • 0032948007 scopus 로고    scopus 로고
    • Preferential transfer of 2-docosahexaenoyl-1-lysophosphatidylcholine through an in vitro blood-brain barrier over unesterified docosahexaenoic acid
    • Bernoud, N., et al. 1999. Preferential transfer of 2-docosahexaenoyl-1-lysophosphatidylcholine through an in vitro blood-brain barrier over unesterified docosahexaenoic acid. J. Neurochem. 72: 338-345.
    • (1999) J. Neurochem. , vol.72 , pp. 338-345
    • Bernoud, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.