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Volumn 4, Issue 1 SUPPL. 1, 2008, Pages

Oral administration of circulating precursors for membrane phosphatides can promote the synthesis of new brain synapses

Author keywords

Alzheimer's disease; Dendritic spine; Docosahexaenoic acid; Phosphatide; Precursor; synaptic membrane; Uridine

Indexed keywords

ACETYLCHOLINE; ARACHIDONIC ACID; BETA TUBULIN; CHOLINE; CHOLINE KINASE; CHOLINE PHOSPHATE CYTIDYLYLTRANSFERASE; CHOLINEPHOSPHOTRANSFERASE; CYTIDINE DIPHOSPHATE; CYTIDINE TRIPHOSPHATE; DOCOSAHEXAENOIC ACID; DOPAMINE; GLUTAMATE RECEPTOR 1; ICOSAPENTAENOIC ACID; NEUROFILAMENT PROTEIN; NEUROTRANSMITTER; NEUROTRANSMITTER RECEPTOR; OMEGA 3 FATTY ACID; PHOSPHOLIPID; POSTSYNAPTIC DENSITY PROTEIN 95; SYNAPSIN I; SYNTAXIN; SYNTAXIN 3; UNCLASSIFIED DRUG; URIDINE; URIDINE PHOSPHATE;

EID: 38049116118     PISSN: 15525260     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jalz.2007.10.005     Document Type: Editorial
Times cited : (83)

References (170)
  • 1
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe D.J. Alzheimer's disease is a synaptic failure. Science 298 (2002) 789-791
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 2
    • 33646592555 scopus 로고    scopus 로고
    • Synaptic proteins and phospholipids are increased in gerbil brain by administering uridine plus docosahexaenoic acid orally
    • Wurtman R.J., Ulus I.H., Cansev M., Watkins C.J., Wang L., and Marzloff G. Synaptic proteins and phospholipids are increased in gerbil brain by administering uridine plus docosahexaenoic acid orally. Brain Res 1088 (2006) 83-92
    • (2006) Brain Res , vol.1088 , pp. 83-92
    • Wurtman, R.J.1    Ulus, I.H.2    Cansev, M.3    Watkins, C.J.4    Wang, L.5    Marzloff, G.6
  • 4
    • 0022302720 scopus 로고
    • Lipids of nervous tissue: composition and metabolism
    • Sastry P.S. Lipids of nervous tissue: composition and metabolism. Prog Lipid Res 24 (1985) 69-176
    • (1985) Prog Lipid Res , vol.24 , pp. 69-176
    • Sastry, P.S.1
  • 5
    • 21744445919 scopus 로고    scopus 로고
    • Uridine enhances neurite outgrowth in nerve growth factor-differentiated pheochromocytoma cells
    • Pooler A.M., Guez D.H., Benedictus R., and Wurtman R.J. Uridine enhances neurite outgrowth in nerve growth factor-differentiated pheochromocytoma cells. Neuroscience 134 (2005) 207-214
    • (2005) Neuroscience , vol.134 , pp. 207-214
    • Pooler, A.M.1    Guez, D.H.2    Benedictus, R.3    Wurtman, R.J.4
  • 6
    • 34548068288 scopus 로고    scopus 로고
    • Dietary polyunsaturated fat that is low in (n-3) and high in (n-6) fatty acids alters the SNARE protein complex and nitrosylation in rat hippocampus
    • Pongrac J.L., Slack P.J., and Innis S.M. Dietary polyunsaturated fat that is low in (n-3) and high in (n-6) fatty acids alters the SNARE protein complex and nitrosylation in rat hippocampus. J Nutr 137 (2007) 1852-1856
    • (2007) J Nutr , vol.137 , pp. 1852-1856
    • Pongrac, J.L.1    Slack, P.J.2    Innis, S.M.3
  • 7
    • 33645746320 scopus 로고    scopus 로고
    • Omega-3 and omega-6 fatty acids stimulate cell membrane expansion by acting on syntaxin 3
    • Darios F., and Davletov B. Omega-3 and omega-6 fatty acids stimulate cell membrane expansion by acting on syntaxin 3. Nature 440 (2006) 813-817
    • (2006) Nature , vol.440 , pp. 813-817
    • Darios, F.1    Davletov, B.2
  • 8
    • 34548430850 scopus 로고    scopus 로고
    • Chronic administration of docosahexaenoic acid or eicosapentaenoic acid, but not arachidonic acid, alone or in combination with uridine, increases brain phosphatide and synaptic protein levels in gerbils
    • Cansev M., and Wurtman R.J. Chronic administration of docosahexaenoic acid or eicosapentaenoic acid, but not arachidonic acid, alone or in combination with uridine, increases brain phosphatide and synaptic protein levels in gerbils. Neuroscience 148 (2007) 421-431
    • (2007) Neuroscience , vol.148 , pp. 421-431
    • Cansev, M.1    Wurtman, R.J.2
  • 9
    • 0000749205 scopus 로고
    • The function of cytidine coenzymes in the biosynthesis of phospholipids
    • Kennedy E.M., and Weiss S.B. The function of cytidine coenzymes in the biosynthesis of phospholipids. J Biol Chem 222 (1956) 193-214
    • (1956) J Biol Chem , vol.222 , pp. 193-214
    • Kennedy, E.M.1    Weiss, S.B.2
  • 10
    • 0034308088 scopus 로고    scopus 로고
    • Effect of oral CDP-choline on plasma choline and uridine levels in humans
    • Wurtman R.J., Regan M., Ulus I., and Yu L. Effect of oral CDP-choline on plasma choline and uridine levels in humans. Biochem Pharmacol 60 (2000) 989-992
    • (2000) Biochem Pharmacol , vol.60 , pp. 989-992
    • Wurtman, R.J.1    Regan, M.2    Ulus, I.3    Yu, L.4
  • 11
    • 26244466152 scopus 로고    scopus 로고
    • Oral uridine 5' monophosphate (UMP) increases brain CDP-choline levels in gerbils
    • Cansev M., Watkins C.J., van der Beek E.M., and Wurtman R.J. Oral uridine 5' monophosphate (UMP) increases brain CDP-choline levels in gerbils. Brain Res 1058 (2005) 101-108
    • (2005) Brain Res , vol.1058 , pp. 101-108
    • Cansev, M.1    Watkins, C.J.2    van der Beek, E.M.3    Wurtman, R.J.4
  • 12
    • 0020326450 scopus 로고
    • Choline administration elevates brain phosphorylcholine levels
    • Millington W.R., and Wurtman R.J. Choline administration elevates brain phosphorylcholine levels. J Neurochem 38 (1982) 1748-1752
    • (1982) J Neurochem , vol.38 , pp. 1748-1752
    • Millington, W.R.1    Wurtman, R.J.2
  • 14
    • 0018381197 scopus 로고
    • Choline kinase and ethanolamine kinase activity in the cytosol of nerve endings from rat forebrain
    • Spanner S., and Ansell G.B. Choline kinase and ethanolamine kinase activity in the cytosol of nerve endings from rat forebrain. Biochem J 178 (1979) 753-760
    • (1979) Biochem J , vol.178 , pp. 753-760
    • Spanner, S.1    Ansell, G.B.2
  • 15
    • 37049250508 scopus 로고
    • Choline content of rat brain
    • Stavinoha W.B., and Weintraub S.T. Choline content of rat brain. Science 183 (1974) 964-965
    • (1974) Science , vol.183 , pp. 964-965
    • Stavinoha, W.B.1    Weintraub, S.T.2
  • 16
    • 0027499332 scopus 로고
    • Free choline and choline metabolites in rat brain and body fluids: sensitive determination and implications for choline supply to the brain
    • Klein J., Gonzales R., Koppen A., and Loffelholz K. Free choline and choline metabolites in rat brain and body fluids: sensitive determination and implications for choline supply to the brain. Neurochem Int 22 (1993) 293-300
    • (1993) Neurochem Int , vol.22 , pp. 293-300
    • Klein, J.1    Gonzales, R.2    Koppen, A.3    Loffelholz, K.4
  • 18
    • 0040448196 scopus 로고
    • Enzyme translocation in the regulation of phosphatidylcholine biosynthesis
    • Vance D.E., and Pelech S.L. Enzyme translocation in the regulation of phosphatidylcholine biosynthesis. Trends Biochem Sci 9 (1984) 17-20
    • (1984) Trends Biochem Sci , vol.9 , pp. 17-20
    • Vance, D.E.1    Pelech, S.L.2
  • 19
    • 0022474730 scopus 로고
    • The supply of both CDP-choline and diacylglycerol can regulate the rate of phosphatidylcholine synthesis in HeLa cells
    • Lim P., Cornell R., and Vance D.E. The supply of both CDP-choline and diacylglycerol can regulate the rate of phosphatidylcholine synthesis in HeLa cells. Biochem Cell Biol 64 (1986) 692-698
    • (1986) Biochem Cell Biol , vol.64 , pp. 692-698
    • Lim, P.1    Cornell, R.2    Vance, D.E.3
  • 20
    • 0030726780 scopus 로고    scopus 로고
    • Control of membrane phosphatidylcholine synthesis by diacylglycerol levels in neuronal cells undergoing neurite outgrowth
    • Araki W., and Wurtman R.J. Control of membrane phosphatidylcholine synthesis by diacylglycerol levels in neuronal cells undergoing neurite outgrowth. Proc Natl Acad Sci U S A 94 (1997) 11946-11950
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 11946-11950
    • Araki, W.1    Wurtman, R.J.2
  • 21
    • 28444434796 scopus 로고    scopus 로고
    • Docosahexaenoic acid, fatty acid-interacting proteins, and neuronal function: breastmilk and fish are good for you
    • Marszalek J.R., and Lodish H.F. Docosahexaenoic acid, fatty acid-interacting proteins, and neuronal function: breastmilk and fish are good for you. Ann Rev Cell Dev Biol 21 (2005) 633-657
    • (2005) Ann Rev Cell Dev Biol , vol.21 , pp. 633-657
    • Marszalek, J.R.1    Lodish, H.F.2
  • 22
    • 0036237621 scopus 로고    scopus 로고
    • The synapsins: beyond the regulation of neurotransmitter release
    • Ferreira A., and Rapoport M. The synapsins: beyond the regulation of neurotransmitter release. Cell Mol Life Sci 59 (2002) 589-595
    • (2002) Cell Mol Life Sci , vol.59 , pp. 589-595
    • Ferreira, A.1    Rapoport, M.2
  • 25
    • 0020479710 scopus 로고
    • Kinetic studies of the choline acetyltransferase reaction using isotope exchange at equilibrium
    • Hersh L.B. Kinetic studies of the choline acetyltransferase reaction using isotope exchange at equilibrium. J Biol Chem 257 (1982) 12820-12834
    • (1982) J Biol Chem , vol.257 , pp. 12820-12834
    • Hersh, L.B.1
  • 26
    • 0025119804 scopus 로고
    • The synthesis of acetylcholine: twenty years of progress
    • Tucek S. The synthesis of acetylcholine: twenty years of progress. Prog Brain Res 84 (1990) 467-477
    • (1990) Prog Brain Res , vol.84 , pp. 467-477
    • Tucek, S.1
  • 27
    • 0017722681 scopus 로고
    • Acetyl-coenzyme A and coenzyme A analogues: their effects on rat brain choline acetyltransferase
    • Rossier J. Acetyl-coenzyme A and coenzyme A analogues: their effects on rat brain choline acetyltransferase. Biochem J 165 (1977) 321-326
    • (1977) Biochem J , vol.165 , pp. 321-326
    • Rossier, J.1
  • 28
    • 0016493524 scopus 로고
    • Brain acetylcholine: increase after systemic choline administration
    • Cohen E.L., and Wurtman R.J. Brain acetylcholine: increase after systemic choline administration. Life Sci 16 (1975) 1095-1102
    • (1975) Life Sci , vol.16 , pp. 1095-1102
    • Cohen, E.L.1    Wurtman, R.J.2
  • 29
    • 0016736953 scopus 로고
    • Distribution and metabolism of intravenously administered choline[methyl-3H] and synthesis in vivo of acetylcholine in various tissues of guinea pigs
    • Haubrich D.R., Wang P.F.L., and Wedeking P.W. Distribution and metabolism of intravenously administered choline[methyl-3H] and synthesis in vivo of acetylcholine in various tissues of guinea pigs. J Pharmacol Exp Ther 193 (1975) 246-255
    • (1975) J Pharmacol Exp Ther , vol.193 , pp. 246-255
    • Haubrich, D.R.1    Wang, P.F.L.2    Wedeking, P.W.3
  • 30
    • 0015216394 scopus 로고
    • Brain serotonin content: physiological dependence on plasma tryptophan levels
    • Fernstrom J.D., and Wurtman R.J. Brain serotonin content: physiological dependence on plasma tryptophan levels. Science 173 (1971) 149-152
    • (1971) Science , vol.173 , pp. 149-152
    • Fernstrom, J.D.1    Wurtman, R.J.2
  • 32
    • 0029896882 scopus 로고    scopus 로고
    • Choline's phosphorylation in rat striatal slices is regulated by the activity of cholinergic neurons
    • Farber S.A., Savci V., Wei A., Slack B.E., and Wurtman R.J. Choline's phosphorylation in rat striatal slices is regulated by the activity of cholinergic neurons. Brain Res 723 (1996) 90-99
    • (1996) Brain Res , vol.723 , pp. 90-99
    • Farber, S.A.1    Savci, V.2    Wei, A.3    Slack, B.E.4    Wurtman, R.J.5
  • 33
    • 37549068147 scopus 로고    scopus 로고
    • Cytidine and uridine increase striatal CDP-Choline levels without decreasing acetylcholine synthesis or release
    • Ulus I.H., Watkins C.J., Cansev M., and Wurtman R.J. Cytidine and uridine increase striatal CDP-Choline levels without decreasing acetylcholine synthesis or release. Cell Mol Neurobiol 26 (2006) 563-577
    • (2006) Cell Mol Neurobiol , vol.26 , pp. 563-577
    • Ulus, I.H.1    Watkins, C.J.2    Cansev, M.3    Wurtman, R.J.4
  • 34
    • 0021934139 scopus 로고
    • Effects of electrical stimulation and choline availability on the release and contents of acetylcholine and choline in superfused slices from rat striatum
    • Maire J.-C., and Wurtman R.J. Effects of electrical stimulation and choline availability on the release and contents of acetylcholine and choline in superfused slices from rat striatum. J Physiol 80 (1985) 189-195
    • (1985) J Physiol , vol.80 , pp. 189-195
    • Maire, J.-C.1    Wurtman, R.J.2
  • 36
    • 0024598955 scopus 로고
    • Choline increases acetylcholine release and protects against the stimulation-induced decrease in phosphatide levels within membranes of rat corpus striatum
    • Ulus I.H., Wurtman R.J., Mauron C., and Blusztajn J.K. Choline increases acetylcholine release and protects against the stimulation-induced decrease in phosphatide levels within membranes of rat corpus striatum. Brain Res 484 (1989) 217-227
    • (1989) Brain Res , vol.484 , pp. 217-227
    • Ulus, I.H.1    Wurtman, R.J.2    Mauron, C.3    Blusztajn, J.K.4
  • 37
    • 0001191635 scopus 로고
    • Intracellular distribution of some enzymes catalyzing reactions in the biosynthesis of complex lipids
    • Wilgram G.F., and Kennedy E.P. Intracellular distribution of some enzymes catalyzing reactions in the biosynthesis of complex lipids. J Biol Chem 238 (1963) 2615-2619
    • (1963) J Biol Chem , vol.238 , pp. 2615-2619
    • Wilgram, G.F.1    Kennedy, E.P.2
  • 38
    • 0028302144 scopus 로고
    • Phosphatidylcholine cycle and regulation of phosphatidylcholine biosynthesis by enzyme translocation
    • Tronchere H., Record M., Terce F., and Chap H. Phosphatidylcholine cycle and regulation of phosphatidylcholine biosynthesis by enzyme translocation. Biochim Biophys Acta 1212 (1994) 137-151
    • (1994) Biochim Biophys Acta , vol.1212 , pp. 137-151
    • Tronchere, H.1    Record, M.2    Terce, F.3    Chap, H.4
  • 39
    • 0019127792 scopus 로고
    • Regulation of phosphatidylcholine biosynthesis in cultured chick embryonic muscle treated with phospholipase C
    • Sleight R., and Kent C. Regulation of phosphatidylcholine biosynthesis in cultured chick embryonic muscle treated with phospholipase C. J Biol Chem 255 (1980) 10644-10650
    • (1980) J Biol Chem , vol.255 , pp. 10644-10650
    • Sleight, R.1    Kent, C.2
  • 40
    • 0020662973 scopus 로고
    • Regulation of phosphatidylcholine biosynthesis in mammalian cells: I-effects of phospholipase C treatment on phosphatidylcholine metabolism in Chinese hamster ovary cells and LM mouse fibroblasts
    • Sleight R., and Kent C. Regulation of phosphatidylcholine biosynthesis in mammalian cells: I-effects of phospholipase C treatment on phosphatidylcholine metabolism in Chinese hamster ovary cells and LM mouse fibroblasts. J Biol Chem 258 (1983) 824-830
    • (1983) J Biol Chem , vol.258 , pp. 824-830
    • Sleight, R.1    Kent, C.2
  • 41
    • 0021206880 scopus 로고
    • Membrane-bound CTP:phosphocholine cytidylyltransferase regulates the rate of phosphatidylcholine synthesis in HeLa cells treated with unsaturated fatty acids
    • Pelech S.L., Cook H.W., Paddon H.B., and Vance D.E. Membrane-bound CTP:phosphocholine cytidylyltransferase regulates the rate of phosphatidylcholine synthesis in HeLa cells treated with unsaturated fatty acids. Biochim Biophys Acta 795 (1984) 433-440
    • (1984) Biochim Biophys Acta , vol.795 , pp. 433-440
    • Pelech, S.L.1    Cook, H.W.2    Paddon, H.B.3    Vance, D.E.4
  • 42
    • 0034284083 scopus 로고    scopus 로고
    • Regulation of CTP:phosphocholine cytidylyltransferase by amphitropism and relocalization
    • Cornell R.B., and Northwood I.C. Regulation of CTP:phosphocholine cytidylyltransferase by amphitropism and relocalization. Trends Biochem Sci 25 (2000) 441-447
    • (2000) Trends Biochem Sci , vol.25 , pp. 441-447
    • Cornell, R.B.1    Northwood, I.C.2
  • 43
    • 0026346995 scopus 로고
    • Diacylglycerol signals the translocation of CTP:choline-phosphate cytidylyltransferase in HeLa cells treated with 12-O-tetradecanoylphorbol-13-acetate
    • Utal A.K., Jamil H., and Vance D.E. Diacylglycerol signals the translocation of CTP:choline-phosphate cytidylyltransferase in HeLa cells treated with 12-O-tetradecanoylphorbol-13-acetate. J Biol Chem 266 (1991) 24084-24091
    • (1991) J Biol Chem , vol.266 , pp. 24084-24091
    • Utal, A.K.1    Jamil, H.2    Vance, D.E.3
  • 44
    • 0025898441 scopus 로고
    • Control of phosphatidylcholine synthesis in Hep G2 cells: effect of fatty acids on the activity and immunoreactive content of choline phosphate cytidylyltransferase
    • Weinhold P.A., Charles L., Rounsifer M.E., and Feldman D.A. Control of phosphatidylcholine synthesis in Hep G2 cells: effect of fatty acids on the activity and immunoreactive content of choline phosphate cytidylyltransferase. J Biol Chem 266 (1991) 6093-6100
    • (1991) J Biol Chem , vol.266 , pp. 6093-6100
    • Weinhold, P.A.1    Charles, L.2    Rounsifer, M.E.3    Feldman, D.A.4
  • 45
    • 0025887424 scopus 로고
    • Regulation of CTP:phosphocholine cytidylyltransferase activity and subcellular location by phosphorylation in Chinese hamster ovary cells: the effect of phospholipase C treatment
    • Watkins J.D., and Kent C. Regulation of CTP:phosphocholine cytidylyltransferase activity and subcellular location by phosphorylation in Chinese hamster ovary cells: the effect of phospholipase C treatment. J Biol Chem 266 (1991) 21113-21117
    • (1991) J Biol Chem , vol.266 , pp. 21113-21117
    • Watkins, J.D.1    Kent, C.2
  • 46
    • 0024269943 scopus 로고
    • Kinetic and biochemical properties of CTP:choline-phosphate cytidylyltransferase from the rat brain
    • Mages F., Rey C., Fonlupt P., and Pacheco H. Kinetic and biochemical properties of CTP:choline-phosphate cytidylyltransferase from the rat brain. Eur J Biochem 178 (1988) 367-372
    • (1988) Eur J Biochem , vol.178 , pp. 367-372
    • Mages, F.1    Rey, C.2    Fonlupt, P.3    Pacheco, H.4
  • 47
    • 0013930222 scopus 로고
    • Free nucleotides in the rat brain during post-natal development
    • Mandel P., and Edel-Harth S. Free nucleotides in the rat brain during post-natal development. J Neurochem 13 (1966) 591-595
    • (1966) J Neurochem , vol.13 , pp. 591-595
    • Mandel, P.1    Edel-Harth, S.2
  • 48
    • 0023117863 scopus 로고
    • Mechanism of arachidonic acid liberation during ischemia in gerbil cerebral cortex
    • Abe K., Koqure K., Yamomoto H., Imazawa M., and Miyamoto K. Mechanism of arachidonic acid liberation during ischemia in gerbil cerebral cortex. J Neurochem 48 (1987) 503-509
    • (1987) J Neurochem , vol.48 , pp. 503-509
    • Abe, K.1    Koqure, K.2    Yamomoto, H.3    Imazawa, M.4    Miyamoto, K.5
  • 50
    • 0018832714 scopus 로고
    • An increase in cytoplasmic CTP accelerates the reaction catalyzed by CTP:phosphocholine cytidylyltransferase in poliovirus-infected HeLa cells
    • Choy P.C., Paddon H.B., and Vance D.E. An increase in cytoplasmic CTP accelerates the reaction catalyzed by CTP:phosphocholine cytidylyltransferase in poliovirus-infected HeLa cells. J Biol Chem 255 (1980) 1070-1073
    • (1980) J Biol Chem , vol.255 , pp. 1070-1073
    • Choy, P.C.1    Paddon, H.B.2    Vance, D.E.3
  • 51
    • 0026637566 scopus 로고
    • Enhancement by cytidine of membrane phospholipid synthesis
    • Lopez G., Coviella I., and Wurtman R.J. Enhancement by cytidine of membrane phospholipid synthesis. J Neurochem 59 (1992) 338-343
    • (1992) J Neurochem , vol.59 , pp. 338-343
    • Lopez, G.1    Coviella, I.2    Wurtman, R.J.3
  • 52
    • 0037427385 scopus 로고    scopus 로고
    • Stimulation of CDP-choline synthesis by uridine or cytidine in PC12 rat pheochromocytoma cells
    • Richardson U.I., Watkins C.J., Pierre C., Ulus I.H., and Wurtman R.J. Stimulation of CDP-choline synthesis by uridine or cytidine in PC12 rat pheochromocytoma cells. Brain Res 971 (2003) 161-167
    • (2003) Brain Res , vol.971 , pp. 161-167
    • Richardson, U.I.1    Watkins, C.J.2    Pierre, C.3    Ulus, I.H.4    Wurtman, R.J.5
  • 53
    • 0028835448 scopus 로고
    • Effect of cytidine on membrane phospholipid synthesis in rat striatal slices
    • Savci V., and Wurtman R.J. Effect of cytidine on membrane phospholipid synthesis in rat striatal slices. J Neurochem 64 (1995) 378-384
    • (1995) J Neurochem , vol.64 , pp. 378-384
    • Savci, V.1    Wurtman, R.J.2
  • 54
    • 0017645120 scopus 로고
    • Phospholipid synthesis in isolated fat cells: studies of microsomal diacylglycerol cholinephosphotransferase and diacylglycerol ethanolaminephosphotransferase activities
    • Coleman R., and Bell R.M.L. Phospholipid synthesis in isolated fat cells: studies of microsomal diacylglycerol cholinephosphotransferase and diacylglycerol ethanolaminephosphotransferase activities. J Biol Chem 252 (1977) 3050-3056
    • (1977) J Biol Chem , vol.252 , pp. 3050-3056
    • Coleman, R.1    Bell, R.M.L.2
  • 55
    • 0017062311 scopus 로고
    • Solubilization and purification of rat liver microsomal 1,2-diacylglycerol: CDP-choline cholinephosphotransferase and 1,2-diacylglycerol: CDP-ethanolamine ethanolaminephosphotransferase
    • Kanoh H., and Ohno K. Solubilization and purification of rat liver microsomal 1,2-diacylglycerol: CDP-choline cholinephosphotransferase and 1,2-diacylglycerol: CDP-ethanolamine ethanolaminephosphotransferase. Eur J Biochem 66 (1976) 201-210
    • (1976) Eur J Biochem , vol.66 , pp. 201-210
    • Kanoh, H.1    Ohno, K.2
  • 56
    • 0027450135 scopus 로고
    • CDP-choline:1,2-diacylglycerol cholinephosphotransferase from rat liver microsomes. I. Solubilization and characterization of the partially purified enzyme and the possible existence of an endogenous inhibitor
    • Ishidate K., Matsuo R., and Nakazawa Y. CDP-choline:1,2-diacylglycerol cholinephosphotransferase from rat liver microsomes. I. Solubilization and characterization of the partially purified enzyme and the possible existence of an endogenous inhibitor. Lipids 28 (1993) 89-96
    • (1993) Lipids , vol.28 , pp. 89-96
    • Ishidate, K.1    Matsuo, R.2    Nakazawa, Y.3
  • 57
    • 0024394843 scopus 로고
    • An improved procedure for the purification of ethanolaminephosphotransferase: reconstitution of the purified enzyme with lipids
    • Roberti R., Vecchini A., Freysz L., Masoom M., and Binaglia L. An improved procedure for the purification of ethanolaminephosphotransferase: reconstitution of the purified enzyme with lipids. Biochim Biophys Acta 1004 (1989) 80-88
    • (1989) Biochim Biophys Acta , vol.1004 , pp. 80-88
    • Roberti, R.1    Vecchini, A.2    Freysz, L.3    Masoom, M.4    Binaglia, L.5
  • 58
    • 0025174718 scopus 로고
    • Solubilization and partial purification of cholinephosphotransferase in hamster tissues
    • O K.-M., and Choy P.C. Solubilization and partial purification of cholinephosphotransferase in hamster tissues. Lipids 25 (1990) 122-124
    • (1990) Lipids , vol.25 , pp. 122-124
    • Choy, P.C.1
  • 59
    • 0033561020 scopus 로고    scopus 로고
    • Cloning and expression of a human choline/ethanolaminephosphotransferase: synthesis of phosphatidylcholine and phosphatidylethanolamine
    • Henneberry A.L., and McMaster C.R. Cloning and expression of a human choline/ethanolaminephosphotransferase: synthesis of phosphatidylcholine and phosphatidylethanolamine. Biochem J 339 (1999) 291-298
    • (1999) Biochem J , vol.339 , pp. 291-298
    • Henneberry, A.L.1    McMaster, C.R.2
  • 60
    • 0034703103 scopus 로고    scopus 로고
    • Cloning, genomic organization, and characterization of a human cholinephosphotransferase
    • Henneberry A.L., Wistow G., and McMaster C.R. Cloning, genomic organization, and characterization of a human cholinephosphotransferase. J Biol Chem 275 (2000) 29808-29815
    • (2000) J Biol Chem , vol.275 , pp. 29808-29815
    • Henneberry, A.L.1    Wistow, G.2    McMaster, C.R.3
  • 61
    • 0015934663 scopus 로고
    • Utilization of endogenous phospholipids by the backreaction of CDP-choline (-ethanolamine): 1,2-diglyceride choline (ethanolamine)-phosphotransferase in rat liver microsomes
    • Kanoh H., and Ohno K. Utilization of endogenous phospholipids by the backreaction of CDP-choline (-ethanolamine): 1,2-diglyceride choline (ethanolamine)-phosphotransferase in rat liver microsomes. Biochim Biophys Acta 306 (1973) 207-217
    • (1973) Biochim Biophys Acta , vol.306 , pp. 207-217
    • Kanoh, H.1    Ohno, K.2
  • 62
    • 0015819588 scopus 로고
    • Studies on 1,2-diglycerides formed from endogenous lecithins by the back-reaction of rat liver microsomal cdpcholine: 1,2-diacylglycerol cholinephosphotransferase
    • Kanoh H., and Ohno K. Studies on 1,2-diglycerides formed from endogenous lecithins by the back-reaction of rat liver microsomal cdpcholine: 1,2-diacylglycerol cholinephosphotransferase. Biochim Biophys Acta 326 (1973) 17-25
    • (1973) Biochim Biophys Acta , vol.326 , pp. 17-25
    • Kanoh, H.1    Ohno, K.2
  • 63
    • 0019886330 scopus 로고
    • The reverse reaction of cholinephosphotransferase in rat brain microsomes: a new pathway for degradation of phosphatidylcholine
    • Goracci G., Francescangeli E., Horrocks L.A., and Porcelatti G. The reverse reaction of cholinephosphotransferase in rat brain microsomes: a new pathway for degradation of phosphatidylcholine. Biochim Biophys Acta 664 (1981) 373-379
    • (1981) Biochim Biophys Acta , vol.664 , pp. 373-379
    • Goracci, G.1    Francescangeli, E.2    Horrocks, L.A.3    Porcelatti, G.4
  • 64
    • 0023054506 scopus 로고
    • A comparison of the reversibility of phosphoethanolamine transferase and phosphocholine transferase in rat brain microsomes
    • Goracci G., Francescangeli E., Horrocks L.A., and Porcelatti G. A comparison of the reversibility of phosphoethanolamine transferase and phosphocholine transferase in rat brain microsomes. Biochim Biophys Acta 876 (1986) 387-391
    • (1986) Biochim Biophys Acta , vol.876 , pp. 387-391
    • Goracci, G.1    Francescangeli, E.2    Horrocks, L.A.3    Porcelatti, G.4
  • 65
    • 0026474040 scopus 로고
    • Reversibility of the reactions catalyzed by cholinephosphotransferase and ethanolaminephosphotransferase solubilized from rat-brain microsomes
    • Roberti R., Mancini A., Freysz L., and Binaglia L. Reversibility of the reactions catalyzed by cholinephosphotransferase and ethanolaminephosphotransferase solubilized from rat-brain microsomes. Biochim Biophys Acta 1165 (1992) 183-188
    • (1992) Biochim Biophys Acta , vol.1165 , pp. 183-188
    • Roberti, R.1    Mancini, A.2    Freysz, L.3    Binaglia, L.4
  • 66
    • 0026596148 scopus 로고
    • Cholinephosphotransferase from mammalian sources
    • Cornell R.B. Cholinephosphotransferase from mammalian sources. Methods Enzymol 209 (1992) 267-272
    • (1992) Methods Enzymol , vol.209 , pp. 267-272
    • Cornell, R.B.1
  • 67
    • 0016577909 scopus 로고
    • Water-soluble phospholipid precursor pool-sizes in quick-frozen and unfrozen rat livers
    • Korniat E.K., and Beeler D.A. Water-soluble phospholipid precursor pool-sizes in quick-frozen and unfrozen rat livers. Anal Biochem 69 (1975) 300-305
    • (1975) Anal Biochem , vol.69 , pp. 300-305
    • Korniat, E.K.1    Beeler, D.A.2
  • 68
    • 0026335117 scopus 로고
    • 1,2-diacylglycerol and ceramide levels in rat liver and skeletal muscle in vivo
    • Turinsky J., Bayly B.P., and O'Sullivan D.M. 1,2-diacylglycerol and ceramide levels in rat liver and skeletal muscle in vivo. Am J Physiol 261 (1991) E620-E627
    • (1991) Am J Physiol , vol.261
    • Turinsky, J.1    Bayly, B.P.2    O'Sullivan, D.M.3
  • 69
    • 0019780295 scopus 로고
    • Pool size of CDP-choline in the brain, heart, and lung of normal hypoxic guinea pigs
    • Alberghina M., Viola M., and Giuffrida A.M. Pool size of CDP-choline in the brain, heart, and lung of normal hypoxic guinea pigs. J Neurosci Res 6 (1981) 719-722
    • (1981) J Neurosci Res , vol.6 , pp. 719-722
    • Alberghina, M.1    Viola, M.2    Giuffrida, A.M.3
  • 70
    • 0026500225 scopus 로고
    • Evidence that cyclic AMP-induced inhibition of phosphatidylcholine biosynthesis is caused by a decrease in cellular diacylglycerol levels in cultured rat hepatocytes
    • Jamil H., Utal A.K., and Vance D.E. Evidence that cyclic AMP-induced inhibition of phosphatidylcholine biosynthesis is caused by a decrease in cellular diacylglycerol levels in cultured rat hepatocytes. J Biol Chem 267 (1992) 1752-1760
    • (1992) J Biol Chem , vol.267 , pp. 1752-1760
    • Jamil, H.1    Utal, A.K.2    Vance, D.E.3
  • 71
    • 0036635372 scopus 로고    scopus 로고
    • PC and PE synthesis: mixed micellar analysis of the cholinephosphotransferase and ethanolaminephosphotransferase activities of human choline/ethanolamine phosphotransferase 1 (CEPT1)
    • Wright M.M., and McMaster C.R. PC and PE synthesis: mixed micellar analysis of the cholinephosphotransferase and ethanolaminephosphotransferase activities of human choline/ethanolamine phosphotransferase 1 (CEPT1). Lipids 37 (2002) 663-672
    • (2002) Lipids , vol.37 , pp. 663-672
    • Wright, M.M.1    McMaster, C.R.2
  • 72
    • 0027473820 scopus 로고
    • Kinetic selectivity of cholinephosphotransferase in mouse liver: the Km for CDP-choline depends on diacylglycerol structure
    • Mantel C.R., Schultz A.R., Miyazawa K., and Broxmeyer H.E. Kinetic selectivity of cholinephosphotransferase in mouse liver: the Km for CDP-choline depends on diacylglycerol structure. Biochem J 289 (1993) 815-820
    • (1993) Biochem J , vol.289 , pp. 815-820
    • Mantel, C.R.1    Schultz, A.R.2    Miyazawa, K.3    Broxmeyer, H.E.4
  • 73
    • 34047150513 scopus 로고    scopus 로고
    • Polyunsaturated fatty acids regulate phosphatidylcholine synthesis in PC12 cells
    • Richardson U.I., and Wurtman R.J. Polyunsaturated fatty acids regulate phosphatidylcholine synthesis in PC12 cells. Biochim Biophys Acta 1771 (2007) 558-563
    • (2007) Biochim Biophys Acta , vol.1771 , pp. 558-563
    • Richardson, U.I.1    Wurtman, R.J.2
  • 75
    • 1242340288 scopus 로고    scopus 로고
    • The concentrative nucleoside transporter family, SLC28
    • Gray J.H., Owen R.P., and Giacomini K.M. The concentrative nucleoside transporter family, SLC28. Pflugers Arch 447 (2004) 728-734
    • (2004) Pflugers Arch , vol.447 , pp. 728-734
    • Gray, J.H.1    Owen, R.P.2    Giacomini, K.M.3
  • 76
    • 33747886010 scopus 로고    scopus 로고
    • Uridine and cytidine in the brain: their transport and utilization
    • Cansev M. Uridine and cytidine in the brain: their transport and utilization. Brain Res Brain Res Rev 52 (2006) 389-397
    • (2006) Brain Res Brain Res Rev , vol.52 , pp. 389-397
    • Cansev, M.1
  • 77
    • 24144459853 scopus 로고    scopus 로고
    • Polarized distribution of nucleoside transporters in rat brain endothelial and choroid plexus epithelial cells
    • Redzic Z.B., Biringer J., Barnes K., Baldwin S.A., Al-Sarraf H., Nicola P.A., et al. Polarized distribution of nucleoside transporters in rat brain endothelial and choroid plexus epithelial cells. J Neurochem 94 (2005) 1420-1426
    • (2005) J Neurochem , vol.94 , pp. 1420-1426
    • Redzic, Z.B.1    Biringer, J.2    Barnes, K.3    Baldwin, S.A.4    Al-Sarraf, H.5    Nicola, P.A.6
  • 78
    • 12344335693 scopus 로고    scopus 로고
    • Functional characterization of adenosine transport across the BBB in mice
    • Murakami H., Ohkura A., Takanaga H., Matsuo H., Koyabu N., Naito M., et al. Functional characterization of adenosine transport across the BBB in mice. Int J Pharm 290 (2005) 37-44
    • (2005) Int J Pharm , vol.290 , pp. 37-44
    • Murakami, H.1    Ohkura, A.2    Takanaga, H.3    Matsuo, H.4    Koyabu, N.5    Naito, M.6
  • 79
    • 0032192444 scopus 로고    scopus 로고
    • Transport and mode of action of nucleoside derivatives used in chemical and antiviral therapies
    • Pastor-Anglada M., Felipe A., and Casado F.J. Transport and mode of action of nucleoside derivatives used in chemical and antiviral therapies. Trends Pharmacol Sci 19 (1998) 424-430
    • (1998) Trends Pharmacol Sci , vol.19 , pp. 424-430
    • Pastor-Anglada, M.1    Felipe, A.2    Casado, F.J.3
  • 81
    • 0030606020 scopus 로고    scopus 로고
    • Nucleoside and nucleobase transport systems of mammalian cells
    • Griffith D.A., and Jarvis S.M. Nucleoside and nucleobase transport systems of mammalian cells. Biochim Biophys Acta 1286 (1996) 153-181
    • (1996) Biochim Biophys Acta , vol.1286 , pp. 153-181
    • Griffith, D.A.1    Jarvis, S.M.2
  • 82
    • 0028143584 scopus 로고
    • Physiological concentrations of purines and pyrimidines
    • Traut T.W. Physiological concentrations of purines and pyrimidines. Mol Cell Biochem 140 (1994) 1-22
    • (1994) Mol Cell Biochem , vol.140 , pp. 1-22
    • Traut, T.W.1
  • 83
    • 33845330241 scopus 로고    scopus 로고
    • Characterization of the rat Na+/nucleoside cotransporter 2 (rCNT2) and transport of nucleoside-derived drugs using electrophysiological methods
    • Larrayoz I.M., Fernandez-Nistal A., Garces A., Gorraitz E., and Lostao M.P. Characterization of the rat Na+/nucleoside cotransporter 2 (rCNT2) and transport of nucleoside-derived drugs using electrophysiological methods. Am J Physiol Cell Physiol 291 (2006) C1395-C1404
    • (2006) Am J Physiol Cell Physiol , vol.291
    • Larrayoz, I.M.1    Fernandez-Nistal, A.2    Garces, A.3    Gorraitz, E.4    Lostao, M.P.5
  • 84
    • 33745876264 scopus 로고    scopus 로고
    • Cytidine is a novel substrate for wild-type concentrative nucleoside transporter 2
    • Nagai K., Nagasawa K., Koma M., Hotta A., and Fujimoto S. Cytidine is a novel substrate for wild-type concentrative nucleoside transporter 2. Biochem Biophys Res Commun 347 (2006) 439-443
    • (2006) Biochem Biophys Res Commun , vol.347 , pp. 439-443
    • Nagai, K.1    Nagasawa, K.2    Koma, M.3    Hotta, A.4    Fujimoto, S.5
  • 85
    • 31044433586 scopus 로고    scopus 로고
    • Contribution of an unidentified sodium-dependent nucleoside transport system to the uptake and cytotoxicity of anthracycline in mouse M5076 ovarian sarcoma cells
    • Nagai K., Nagasawa K., Koma M., Kihara Y., and Fujimoto S. Contribution of an unidentified sodium-dependent nucleoside transport system to the uptake and cytotoxicity of anthracycline in mouse M5076 ovarian sarcoma cells. Biochem Pharmacol 71 (2006) 565-573
    • (2006) Biochem Pharmacol , vol.71 , pp. 565-573
    • Nagai, K.1    Nagasawa, K.2    Koma, M.3    Kihara, Y.4    Fujimoto, S.5
  • 86
    • 33646555659 scopus 로고    scopus 로고
    • Exogenous cytidine-5'-diphosphocholine increases brain cytidine-5'-diphosphocholine levels in gerbils
    • Cansev M., and Wurtman R.J. Exogenous cytidine-5'-diphosphocholine increases brain cytidine-5'-diphosphocholine levels in gerbils. J Neurochem 94 Supp. 2 (2005) 105-106
    • (2005) J Neurochem , vol.94 , Issue.SUPPL. 2 , pp. 105-106
    • Cansev, M.1    Wurtman, R.J.2
  • 87
    • 0032777908 scopus 로고    scopus 로고
    • Distribution of equilibrative, nitrobenzylthioinosine-insensitive nucleoside transporters (ENT1) in rat brain
    • Anderson C.M., Xiong W., Geiger J.D., Young J.D., Cass C.E., Baldwin S.A., et al. Distribution of equilibrative, nitrobenzylthioinosine-insensitive nucleoside transporters (ENT1) in rat brain. J Neurochem 73 (1999) 867-873
    • (1999) J Neurochem , vol.73 , pp. 867-873
    • Anderson, C.M.1    Xiong, W.2    Geiger, J.D.3    Young, J.D.4    Cass, C.E.5    Baldwin, S.A.6
  • 88
    • 0032980763 scopus 로고    scopus 로고
    • Distribution of mRNA encoding a nitrobenzylthioinosine-insensitive nucleoside transporter (ENT2) in rat brain
    • Anderson C.M., Baldwin S.A., Young J.D., Cass C.E., and Parkinson F.E. Distribution of mRNA encoding a nitrobenzylthioinosine-insensitive nucleoside transporter (ENT2) in rat brain. Brain Res Mol Brain Res 70 (1999) 293-297
    • (1999) Brain Res Mol Brain Res , vol.70 , pp. 293-297
    • Anderson, C.M.1    Baldwin, S.A.2    Young, J.D.3    Cass, C.E.4    Parkinson, F.E.5
  • 89
    • 0026794356 scopus 로고
    • Sodium-dependent nucleoside transport in choroid plexus from rabbit. evidence for a single transporter for purine and pyrimidine nucleosides
    • Wu X., Yuan G., Brett C.M., Hui A.C., and Giacomini K.M. Sodium-dependent nucleoside transport in choroid plexus from rabbit. evidence for a single transporter for purine and pyrimidine nucleosides. J Biol Chem 267 (1992) 8813-8818
    • (1992) J Biol Chem , vol.267 , pp. 8813-8818
    • Wu, X.1    Yuan, G.2    Brett, C.M.3    Hui, A.C.4    Giacomini, K.M.5
  • 90
    • 0028293655 scopus 로고
    • Further characterization of the sodium-dependent nucleoside transporter (N3) in choroid plexus from rabbit
    • Wu X., Gutierrez M.M., and Giacomini K.M. Further characterization of the sodium-dependent nucleoside transporter (N3) in choroid plexus from rabbit. Biochim Biophys Acta 1191 (1994) 190-196
    • (1994) Biochim Biophys Acta , vol.1191 , pp. 190-196
    • Wu, X.1    Gutierrez, M.M.2    Giacomini, K.M.3
  • 92
    • 0242536493 scopus 로고
    • Pyrimidine metabolism. II. Enzymatic pathways of uracil anabolism
    • Canellakis E.S. Pyrimidine metabolism. II. Enzymatic pathways of uracil anabolism. J Biol Chem 227 (1957) 329-338
    • (1957) J Biol Chem , vol.227 , pp. 329-338
    • Canellakis, E.S.1
  • 93
    • 0005036870 scopus 로고
    • Uridine kinase from Erlich ascites tumor: purification and properties
    • Skold O. Uridine kinase from Erlich ascites tumor: purification and properties. J Biol Chem 235 (1960) 3273-3279
    • (1960) J Biol Chem , vol.235 , pp. 3273-3279
    • Skold, O.1
  • 94
    • 0014690439 scopus 로고
    • Regulation of enzymic activity by metabolites. I. Uridine-cytidine kinase of Novikoff ascites rat tumor
    • Orengo A. Regulation of enzymic activity by metabolites. I. Uridine-cytidine kinase of Novikoff ascites rat tumor. J Biol Chem 244 (1969) 2204-2209
    • (1969) J Biol Chem , vol.244 , pp. 2204-2209
    • Orengo, A.1
  • 95
    • 33846647534 scopus 로고    scopus 로고
    • Key role of uridine kinase and uridine phosphorylase in the homeostatic regulation of purine and pyrimidine salvage in brain
    • Balestri F., Barsotti C., Lutzemberger L., Camici M., and Ipata P.L. Key role of uridine kinase and uridine phosphorylase in the homeostatic regulation of purine and pyrimidine salvage in brain. Neurochem Int 51 (2007) 517-523
    • (2007) Neurochem Int , vol.51 , pp. 517-523
    • Balestri, F.1    Barsotti, C.2    Lutzemberger, L.3    Camici, M.4    Ipata, P.L.5
  • 96
    • 0015131363 scopus 로고
    • Multiple forms of uridine kinase in normal and neoplastic rat liver
    • Krystal G., and Webb T.E. Multiple forms of uridine kinase in normal and neoplastic rat liver. Biochem J 124 (1971) 943-947
    • (1971) Biochem J , vol.124 , pp. 943-947
    • Krystal, G.1    Webb, T.E.2
  • 97
    • 0018891218 scopus 로고
    • Electrophoretically distinct forms of uridine kinase in the rat: tissue distribution and age-dependence
    • Absil J., Tuilie M., and Roux J.-M. Electrophoretically distinct forms of uridine kinase in the rat: tissue distribution and age-dependence. Biochem J 185 (1980) 273-276
    • (1980) Biochem J , vol.185 , pp. 273-276
    • Absil, J.1    Tuilie, M.2    Roux, J.-M.3
  • 98
    • 0035458584 scopus 로고    scopus 로고
    • Cloning and expression of uridine/cytidine kinase cDNA from human fibrosarcoma cells
    • Koizumi K., Shimamoto Y., Azuma A., Wataya Y., Matsuda A., Sasaki T., et al. Cloning and expression of uridine/cytidine kinase cDNA from human fibrosarcoma cells. Int J Mol Med 8 (2001) 273-278
    • (2001) Int J Mol Med , vol.8 , pp. 273-278
    • Koizumi, K.1    Shimamoto, Y.2    Azuma, A.3    Wataya, Y.4    Matsuda, A.5    Sasaki, T.6
  • 99
    • 0035040209 scopus 로고    scopus 로고
    • Phosphorylation of uridine and cytidine analogs by two human uridine-cytidine kinases
    • Van Rompay A.R., Norda A., Linden K., Johansson M., and Karlsson A. Phosphorylation of uridine and cytidine analogs by two human uridine-cytidine kinases. Mol Pharmacol 59 (2001) 1181-1186
    • (2001) Mol Pharmacol , vol.59 , pp. 1181-1186
    • Van Rompay, A.R.1    Norda, A.2    Linden, K.3    Johansson, M.4    Karlsson, A.5
  • 100
    • 0346637526 scopus 로고
    • The enzymatic incorporation of ribonucleotides into polydeoxynucleotide material
    • Hurwitz J. The enzymatic incorporation of ribonucleotides into polydeoxynucleotide material. J Biol Chem 234 (1959) 2351-2358
    • (1959) J Biol Chem , vol.234 , pp. 2351-2358
    • Hurwitz, J.1
  • 101
    • 0014027054 scopus 로고
    • Metabolism of deoxyribonucleotides. I. Purification and properties of deoxycytidine monophosphokinase of calf thymus
    • Sugino Y., Teraoka H., and Shimono H. Metabolism of deoxyribonucleotides. I. Purification and properties of deoxycytidine monophosphokinase of calf thymus. J Biol Chem 241 (1966) 961-969
    • (1966) J Biol Chem , vol.241 , pp. 961-969
    • Sugino, Y.1    Teraoka, H.2    Shimono, H.3
  • 102
    • 0014670794 scopus 로고
    • Adenosine triphosphate: uridine monophosphate-cytidine monophosphate phosphotransferase from Tetrahymena pyriformis
    • Ruffner B.W., and Anderson E.P. Adenosine triphosphate: uridine monophosphate-cytidine monophosphate phosphotransferase from Tetrahymena pyriformis. J Biol Chem 244 (1969) 5994-6002
    • (1969) J Biol Chem , vol.244 , pp. 5994-6002
    • Ruffner, B.W.1    Anderson, E.P.2
  • 103
    • 0011822891 scopus 로고
    • Enzymatic phosphorylation of nucleoside diphosphates
    • Berg P., and Joklik W.K. Enzymatic phosphorylation of nucleoside diphosphates. J Biol Chem 210 (1954) 657-672
    • (1954) J Biol Chem , vol.210 , pp. 657-672
    • Berg, P.1    Joklik, W.K.2
  • 104
    • 77956920094 scopus 로고
    • Nucleoside diphosphokinases
    • Boyer P.D. (Ed), Academic Press, New York
    • Parks Jr. R.E., and Agarwal R.P. Nucleoside diphosphokinases. In: Boyer P.D. (Ed). The Eezymes (1973), Academic Press, New York 307-333
    • (1973) The Eezymes , pp. 307-333
    • Parks Jr., R.E.1    Agarwal, R.P.2
  • 105
    • 0032817023 scopus 로고    scopus 로고
    • Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the human enzyme
    • Van Rompay A.R., Johansson M., and Karlsson A. Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the human enzyme. Mol Pharmacol 56 (1999) 562-569
    • (1999) Mol Pharmacol , vol.56 , pp. 562-569
    • Van Rompay, A.R.1    Johansson, M.2    Karlsson, A.3
  • 107
    • 0036384213 scopus 로고    scopus 로고
    • Human brain nucleoside diphosphate kinase activity is decreased in Alzheimer's disease and Down syndrome
    • Kim S.H., Fountoulakis M., Cairns N.J., and Lubec G. Human brain nucleoside diphosphate kinase activity is decreased in Alzheimer's disease and Down syndrome. Biochem Biophys Res Commun 296 (2002) 970-975
    • (2002) Biochem Biophys Res Commun , vol.296 , pp. 970-975
    • Kim, S.H.1    Fountoulakis, M.2    Cairns, N.J.3    Lubec, G.4
  • 108
    • 13944278588 scopus 로고
    • Enzymatic deamination of cytosine nucleosides
    • Wang T.P., Sable H.Z., and Lampen J.O. Enzymatic deamination of cytosine nucleosides. J Biol Chem 184 (1950) 17-28
    • (1950) J Biol Chem , vol.184 , pp. 17-28
    • Wang, T.P.1    Sable, H.Z.2    Lampen, J.O.3
  • 109
    • 0037654338 scopus 로고
    • Enzymatic amination of uridine triphosphate to cytidine triphosphate
    • Lieberman I. Enzymatic amination of uridine triphosphate to cytidine triphosphate. J Biol Chem 222 (1956) 765-775
    • (1956) J Biol Chem , vol.222 , pp. 765-775
    • Lieberman, I.1
  • 110
    • 2542605056 scopus 로고
    • Formation of cytidine nucleotides from uridine nucleotides by soluble mammalian enzymes: requirements for glutamine and guanosine nucleotides
    • Hurlbert R.B., and Kammen H.O. Formation of cytidine nucleotides from uridine nucleotides by soluble mammalian enzymes: requirements for glutamine and guanosine nucleotides. J Biol Chem 235 (1960) 443-449
    • (1960) J Biol Chem , vol.235 , pp. 443-449
    • Hurlbert, R.B.1    Kammen, H.O.2
  • 111
    • 0022272455 scopus 로고
    • CTP synthase
    • Zalkin H. CTP synthase. Methods Enzymol 113 (1985) 282-287
    • (1985) Methods Enzymol , vol.113 , pp. 282-287
    • Zalkin, H.1
  • 112
    • 0016233993 scopus 로고
    • CTP synthetase activity in neonatal and adult rat brain
    • Genchev D.D., and Mandel P. CTP synthetase activity in neonatal and adult rat brain. J Neurochem 22 (1974) 1027-1030
    • (1974) J Neurochem , vol.22 , pp. 1027-1030
    • Genchev, D.D.1    Mandel, P.2
  • 113
    • 77956943185 scopus 로고
    • Nucleoside and nucleotide kinases
    • Boyer P.D. (Ed), Academic Press, New York
    • Anderson E.P. Nucleoside and nucleotide kinases. In: Boyer P.D. (Ed). The enzymes (1973), Academic Press, New York 49-96
    • (1973) The enzymes , pp. 49-96
    • Anderson, E.P.1
  • 114
    • 0017377834 scopus 로고
    • Uridine kinase activities and pyrimidine nucleoside phosphorylation in fluoropyrimidine-sensitive and -resistant cell lines of the Novikoff hepatoma
    • Greenberg N., Schumm D.E., and Webb T.E. Uridine kinase activities and pyrimidine nucleoside phosphorylation in fluoropyrimidine-sensitive and -resistant cell lines of the Novikoff hepatoma. Biochem J 164 (1977) 379-387
    • (1977) Biochem J , vol.164 , pp. 379-387
    • Greenberg, N.1    Schumm, D.E.2    Webb, T.E.3
  • 115
    • 0030446106 scopus 로고    scopus 로고
    • Cloning and expression of a cDNA encoding uridine kinase from mouse brain
    • Ropp P.A., and Traut T.W. Cloning and expression of a cDNA encoding uridine kinase from mouse brain. Arch Biochem Biophys 336 (1996) 105-112
    • (1996) Arch Biochem Biophys , vol.336 , pp. 105-112
    • Ropp, P.A.1    Traut, T.W.2
  • 116
    • 0032211190 scopus 로고    scopus 로고
    • Uridine kinase: altered enzyme with decreased affinities for uridine and CTP
    • Ropp P.A., and Traut T.W. Uridine kinase: altered enzyme with decreased affinities for uridine and CTP. Arch Biochem Biophys 359 (1998) 63-68
    • (1998) Arch Biochem Biophys , vol.359 , pp. 63-68
    • Ropp, P.A.1    Traut, T.W.2
  • 117
    • 0032828907 scopus 로고    scopus 로고
    • Ribose 1-phosphate and inosine activate uracil salvage in rat brain
    • Mascia L., Cotrufo T., Cappiello M., and Ipata P.L. Ribose 1-phosphate and inosine activate uracil salvage in rat brain. Biochim Biophys Acta 1472 (1999) 93-98
    • (1999) Biochim Biophys Acta , vol.1472 , pp. 93-98
    • Mascia, L.1    Cotrufo, T.2    Cappiello, M.3    Ipata, P.L.4
  • 119
    • 0027439285 scopus 로고
    • Movement of fatty acids, fatty acid analogues, and bile acids across phospholipid bilayers
    • Kamp F., Westerhoff H.V., and Hamilton J.A. Movement of fatty acids, fatty acid analogues, and bile acids across phospholipid bilayers. Biochemistry 32 (1993) 11074-11086
    • (1993) Biochemistry , vol.32 , pp. 11074-11086
    • Kamp, F.1    Westerhoff, H.V.2    Hamilton, J.A.3
  • 120
    • 0021196072 scopus 로고
    • Permeation of long-chain fatty acid into adipocytes: kinetics, specificity, and evidence for involvement of a membrane protein
    • Abumrad N.A., Park J.H., and Park C.R. Permeation of long-chain fatty acid into adipocytes: kinetics, specificity, and evidence for involvement of a membrane protein. J Biol Chem 259 (1984) 8945-8953
    • (1984) J Biol Chem , vol.259 , pp. 8945-8953
    • Abumrad, N.A.1    Park, J.H.2    Park, C.R.3
  • 121
    • 32544436435 scopus 로고    scopus 로고
    • The multigene family of fatty acid-binding proteins: function, structure and polymorphism
    • Chmurzynska A. The multigene family of fatty acid-binding proteins: function, structure and polymorphism. J Appl Genet 47 (2006) 39-48
    • (2006) J Appl Genet , vol.47 , pp. 39-48
    • Chmurzynska, A.1
  • 122
    • 0030710151 scopus 로고    scopus 로고
    • Isolation and expression of a cDNA for human brain fatty acid-binding protein (B-FABP)
    • Shimizu F., Watanabe T.K., Shinomiya H., Nakamura Y., and Fujiwara T. Isolation and expression of a cDNA for human brain fatty acid-binding protein (B-FABP). Biochim Biophys Acta 1354 (1997) 24-28
    • (1997) Biochim Biophys Acta , vol.1354 , pp. 24-28
    • Shimizu, F.1    Watanabe, T.K.2    Shinomiya, H.3    Nakamura, Y.4    Fujiwara, T.5
  • 123
    • 0026463926 scopus 로고
    • A quantitative method for measuring regional in vivo fatty-acid incorporation into and turnover within brain phospholipids: review and critical analysis
    • Robinson P.J., Noronha J., DeGeorge J.J., Freed L.M., Nariai T., and Rapoport S.I. A quantitative method for measuring regional in vivo fatty-acid incorporation into and turnover within brain phospholipids: review and critical analysis. Brain Res Brain Res Rev 17 (1992) 187-214
    • (1992) Brain Res Brain Res Rev , vol.17 , pp. 187-214
    • Robinson, P.J.1    Noronha, J.2    DeGeorge, J.J.3    Freed, L.M.4    Nariai, T.5    Rapoport, S.I.6
  • 124
    • 0002630964 scopus 로고
    • Supply of n-3 polyunsaturated fatty acids and their significance in the central nervous system
    • Wurtman R.J., and Wurtman J.J. (Eds), Raven Press, New York
    • Bazan N.G. Supply of n-3 polyunsaturated fatty acids and their significance in the central nervous system. In: Wurtman R.J., and Wurtman J.J. (Eds). Nutrition and the brain. 1st ed. vol 8 (1990), Raven Press, New York 8.1-8.24
    • (1990) Nutrition and the brain. 1st ed. , vol.8
    • Bazan, N.G.1
  • 125
    • 0028139467 scopus 로고
    • Preferential incorporation of sn-2 lysoPC DHA over unesterified DHA in the young rat brain
    • Thies F., Pillon C., Moliere P., Lagarde M., and Lecerf J. Preferential incorporation of sn-2 lysoPC DHA over unesterified DHA in the young rat brain. Am J Physiol 267 (1994) R1273-R1279
    • (1994) Am J Physiol , vol.267
    • Thies, F.1    Pillon, C.2    Moliere, P.3    Lagarde, M.4    Lecerf, J.5
  • 126
    • 15444373653 scopus 로고    scopus 로고
    • Long-chain acyl-CoA synthetase 6 preferentially promotes DHA metabolism
    • Marszalek J.R., Kitidis C., DiRusso C.C., and Lodish H.F. Long-chain acyl-CoA synthetase 6 preferentially promotes DHA metabolism. J Biol Chem 280 (2005) 10817-10826
    • (2005) J Biol Chem , vol.280 , pp. 10817-10826
    • Marszalek, J.R.1    Kitidis, C.2    DiRusso, C.C.3    Lodish, H.F.4
  • 127
    • 0021745135 scopus 로고
    • Long-chain acyl-coenzyme A synthetase from rat brain microsomes: kinetic studies using [1-14C]docosahexaenoic acid substrate
    • Reddy T.S., Sprecher P., and Bazan N.G. Long-chain acyl-coenzyme A synthetase from rat brain microsomes: kinetic studies using [1-14C]docosahexaenoic acid substrate. Eur J Biochem 145 (1984) 21-29
    • (1984) Eur J Biochem , vol.145 , pp. 21-29
    • Reddy, T.S.1    Sprecher, P.2    Bazan, N.G.3
  • 128
    • 0033773192 scopus 로고    scopus 로고
    • Nutritional deprivation of alpha-linolenic acid decreases but does not abolish turnover and availability of unacylated docosahexaenoic acid and docosahexaenoyl-CoA in rat brain
    • Contreras M.A., Greiner R.S., Chang M.C., Myers C.S., Salem Jr. N., and Rapoport S.I. Nutritional deprivation of alpha-linolenic acid decreases but does not abolish turnover and availability of unacylated docosahexaenoic acid and docosahexaenoyl-CoA in rat brain. J Neurochem 75 (2000) 2392-2400
    • (2000) J Neurochem , vol.75 , pp. 2392-2400
    • Contreras, M.A.1    Greiner, R.S.2    Chang, M.C.3    Myers, C.S.4    Salem Jr., N.5    Rapoport, S.I.6
  • 129
    • 0020565862 scopus 로고
    • High affinity esterification of eicosanoid precursor fatty acids by platelets
    • Neufeld E.J., Wilson D.B., Sprecher H., and Majerus P.W. High affinity esterification of eicosanoid precursor fatty acids by platelets. J Clin Invest 72 (1983) 214-220
    • (1983) J Clin Invest , vol.72 , pp. 214-220
    • Neufeld, E.J.1    Wilson, D.B.2    Sprecher, H.3    Majerus, P.W.4
  • 130
    • 0026021804 scopus 로고
    • Astrocytes, not neurons, produce docosahexaenoic acid (22:6w-3) and arachidonic acid (20:4w-6)
    • Moore S.A., Yoder A., Murphy S., Dutton G.R., and Spector A.A. Astrocytes, not neurons, produce docosahexaenoic acid (22:6w-3) and arachidonic acid (20:4w-6). J Neurochem 56 (1991) 518-524
    • (1991) J Neurochem , vol.56 , pp. 518-524
    • Moore, S.A.1    Yoder, A.2    Murphy, S.3    Dutton, G.R.4    Spector, A.A.5
  • 131
    • 0025966067 scopus 로고
    • Arecoline-stimulated brain incorporation of intravenously administered fatty acids in unanesthetized rats
    • DeGeorge J.J., Nariai T., Yamazaki S., Williams W.M., and Rapoport S.I. Arecoline-stimulated brain incorporation of intravenously administered fatty acids in unanesthetized rats. J Neurochem 56 (1991) 352-355
    • (1991) J Neurochem , vol.56 , pp. 352-355
    • DeGeorge, J.J.1    Nariai, T.2    Yamazaki, S.3    Williams, W.M.4    Rapoport, S.I.5
  • 132
    • 0026058098 scopus 로고
    • Docosahexaenoic acid (cervonic acid) incorporation into different brain regions in the awake rat
    • Sarda N., Gharib A., Moliere P., Grange E., Bobillier P., and Lagarde M. Docosahexaenoic acid (cervonic acid) incorporation into different brain regions in the awake rat. Neurosci Lett 123 (1991) 57-60
    • (1991) Neurosci Lett , vol.123 , pp. 57-60
    • Sarda, N.1    Gharib, A.2    Moliere, P.3    Grange, E.4    Bobillier, P.5    Lagarde, M.6
  • 133
    • 0035317548 scopus 로고    scopus 로고
    • Plasmalogens, phospholipase A2, and docosahexaenoic acid turnover in brain tissue
    • Farooqui A.A., and Horrocks L.A. Plasmalogens, phospholipase A2, and docosahexaenoic acid turnover in brain tissue. J Mol Neurosci 16 (2001) 263-272
    • (2001) J Mol Neurosci , vol.16 , pp. 263-272
    • Farooqui, A.A.1    Horrocks, L.A.2
  • 134
    • 0035102918 scopus 로고    scopus 로고
    • Plasmalogens: biosynthesis and functions
    • Nagan N., and Zoeller R.A. Plasmalogens: biosynthesis and functions. Prog Lipid Res 40 (2001) 199-229
    • (2001) Prog Lipid Res , vol.40 , pp. 199-229
    • Nagan, N.1    Zoeller, R.A.2
  • 135
    • 0013804809 scopus 로고
    • Fatty acid and fatty aldehyde composition of the major brain lipids in normal human gray matter, white matter, and myelin
    • O'Brien J.S., and Sampson E.L. Fatty acid and fatty aldehyde composition of the major brain lipids in normal human gray matter, white matter, and myelin. J Lipid Res 6 (1965) 545-551
    • (1965) J Lipid Res , vol.6 , pp. 545-551
    • O'Brien, J.S.1    Sampson, E.L.2
  • 136
    • 0015517310 scopus 로고
    • The lipid composition of adult rat brain synaptosomal plasma membranes
    • Breckenridge W.C., Gombos G., and Morgan I.G. The lipid composition of adult rat brain synaptosomal plasma membranes. Biochim Biophys Acta 266 (1972) 695-707
    • (1972) Biochim Biophys Acta , vol.266 , pp. 695-707
    • Breckenridge, W.C.1    Gombos, G.2    Morgan, I.G.3
  • 137
    • 0014329483 scopus 로고
    • Distribution and fatty acid composition of phosphoglycerides in normal human brain
    • Svennerholm L. Distribution and fatty acid composition of phosphoglycerides in normal human brain. J Lipid Res 9 (1968) 570-579
    • (1968) J Lipid Res , vol.9 , pp. 570-579
    • Svennerholm, L.1
  • 138
    • 33748447921 scopus 로고    scopus 로고
    • Unique molecular signatures of glycerophospholipid species in different rat tissues analyzed by tandem mass spectrometry
    • Hicks A.M., DeLong C.J., Thomas M.J., Samuel M., and Cui Z. Unique molecular signatures of glycerophospholipid species in different rat tissues analyzed by tandem mass spectrometry. Biochim Biophys Acta 1761 (2006) 1022-1029
    • (2006) Biochim Biophys Acta , vol.1761 , pp. 1022-1029
    • Hicks, A.M.1    DeLong, C.J.2    Thomas, M.J.3    Samuel, M.4    Cui, Z.5
  • 139
    • 0026270149 scopus 로고
    • Digestion and absorption of polyunsaturated fatty acids
    • Carlier H., Bernard A., and Caselli C. Digestion and absorption of polyunsaturated fatty acids. Reprod Nutr Dev 31 (1991) 475-500
    • (1991) Reprod Nutr Dev , vol.31 , pp. 475-500
    • Carlier, H.1    Bernard, A.2    Caselli, C.3
  • 140
    • 0028707020 scopus 로고
    • The metabolism and availability of essential fatty acids in animal and human tissues
    • Bezard J., Blond J.P., Bernard A., and Clouet P. The metabolism and availability of essential fatty acids in animal and human tissues. Reprod Nutr Dev 34 (1994) 539-568
    • (1994) Reprod Nutr Dev , vol.34 , pp. 539-568
    • Bezard, J.1    Blond, J.P.2    Bernard, A.3    Clouet, P.4
  • 141
    • 0034988945 scopus 로고    scopus 로고
    • Delivery and turnover of plasma-derived essential PUFAs in mammalian brain
    • Rapoport S.I., Chang M.C.J., and Spector A.A. Delivery and turnover of plasma-derived essential PUFAs in mammalian brain. J Lipid Res 42 (2001) 678-685
    • (2001) J Lipid Res , vol.42 , pp. 678-685
    • Rapoport, S.I.1    Chang, M.C.J.2    Spector, A.A.3
  • 142
    • 0023567276 scopus 로고
    • Ingestion of fish oil or a derived n-3 fatty acid concentrate containing eicosapentaenoic acid (EPA) affects fatty acid compositions of individual phospholipids of rat brain, sciatic nerve and retina
    • Philbrick D.J., Mahadevappa V.G., Ackman R.G., and Holub B.J. Ingestion of fish oil or a derived n-3 fatty acid concentrate containing eicosapentaenoic acid (EPA) affects fatty acid compositions of individual phospholipids of rat brain, sciatic nerve and retina. J Nutr 117 (1987) 1663-1670
    • (1987) J Nutr , vol.117 , pp. 1663-1670
    • Philbrick, D.J.1    Mahadevappa, V.G.2    Ackman, R.G.3    Holub, B.J.4
  • 143
    • 0034884757 scopus 로고    scopus 로고
    • Physiological compartmental analysis of a-linolenic acid metabolism in adult humans
    • Pawlosky R.J., Hibbeln J.R., Novotny J.A., and Salem Jr. N. Physiological compartmental analysis of a-linolenic acid metabolism in adult humans. J Lipid Res 42 (2001) 1257-1265
    • (2001) J Lipid Res , vol.42 , pp. 1257-1265
    • Pawlosky, R.J.1    Hibbeln, J.R.2    Novotny, J.A.3    Salem Jr., N.4
  • 144
    • 0036715129 scopus 로고    scopus 로고
    • Quantitative role of plasma free fatty acids in the supply of arachidonic acid to extrahepatic tissues in rats
    • Zhou L., Vessby B., and Nilsson A. Quantitative role of plasma free fatty acids in the supply of arachidonic acid to extrahepatic tissues in rats. J Nutr 132 (2002) 262631
    • (2002) J Nutr , vol.132 , pp. 262631
    • Zhou, L.1    Vessby, B.2    Nilsson, A.3
  • 145
    • 23644461408 scopus 로고    scopus 로고
    • In vivo approaches and rationale for quantifying kinetics and imaging brain lipid metabolic pathways
    • Rapoport S.I. In vivo approaches and rationale for quantifying kinetics and imaging brain lipid metabolic pathways. Prostaglandins Other Lipid Mediat 77 (2005) 185-196
    • (2005) Prostaglandins Other Lipid Mediat , vol.77 , pp. 185-196
    • Rapoport, S.I.1
  • 148
    • 34548431107 scopus 로고    scopus 로고
    • Differential cerebral cortex transcriptomes of baboon neonates consuming moderate and high docosahexaenoic acid formulas
    • Kothapalli K.S.D., Anthony J.C., Pan B.S., Hsieh A.T., Nathanielsz P.W., and Brenna J.T. Differential cerebral cortex transcriptomes of baboon neonates consuming moderate and high docosahexaenoic acid formulas. PLoS ONE 2 (2007) e370
    • (2007) PLoS ONE , vol.2
    • Kothapalli, K.S.D.1    Anthony, J.C.2    Pan, B.S.3    Hsieh, A.T.4    Nathanielsz, P.W.5    Brenna, J.T.6
  • 149
    • 0020464876 scopus 로고
    • Selective incorporation of polyunsaturated fatty acids into phosphatidylcholine by rat liver microsomes
    • Lands W.E.M., Inoue M., Sugiura Y., and Okuyama H. Selective incorporation of polyunsaturated fatty acids into phosphatidylcholine by rat liver microsomes. J Biol Chem 257 (1982) 14968-14972
    • (1982) J Biol Chem , vol.257 , pp. 14968-14972
    • Lands, W.E.M.1    Inoue, M.2    Sugiura, Y.3    Okuyama, H.4
  • 150
    • 0034721711 scopus 로고    scopus 로고
    • Actin-based plasticity in dendritic spines
    • Matus A. Actin-based plasticity in dendritic spines. Science 290 (2000) 754-758
    • (2000) Science , vol.290 , pp. 754-758
    • Matus, A.1
  • 151
    • 0035654078 scopus 로고    scopus 로고
    • Dendritic spines: structure, dynamics and regulation
    • Hering H., and Sheng M. Dendritic spines: structure, dynamics and regulation. Nat Rev Neurosci 2 (2001) 880-888
    • (2001) Nat Rev Neurosci , vol.2 , pp. 880-888
    • Hering, H.1    Sheng, M.2
  • 155
    • 3042554012 scopus 로고    scopus 로고
    • Structural basis of long-term potentiation in single dendritic spines
    • Matsuzaki M., Honkura N., Ellis-Davies G.C., and Kasai H. Structural basis of long-term potentiation in single dendritic spines. Nature 429 (2004) 761-766
    • (2004) Nature , vol.429 , pp. 761-766
    • Matsuzaki, M.1    Honkura, N.2    Ellis-Davies, G.C.3    Kasai, H.4
  • 156
    • 0027402975 scopus 로고
    • Synaptic vesicle phosphoproteins and regulation of synaptic function
    • Greengard P., Valtorta F., Czernik A.J., and Benfenati F. Synaptic vesicle phosphoproteins and regulation of synaptic function. Science 259 (1993) 780-785
    • (1993) Science , vol.259 , pp. 780-785
    • Greengard, P.1    Valtorta, F.2    Czernik, A.J.3    Benfenati, F.4
  • 157
    • 2342544141 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of presynaptic assembly
    • Ziv N.E., and Garner C.C. Cellular and molecular mechanisms of presynaptic assembly. Nat Rev Neurosci 5 (2004) 385-399
    • (2004) Nat Rev Neurosci , vol.5 , pp. 385-399
    • Ziv, N.E.1    Garner, C.C.2
  • 158
    • 13844250636 scopus 로고    scopus 로고
    • Growth of dendritic spines: a continuing story
    • Matus A. Growth of dendritic spines: a continuing story. Curr Opin Neurobiol 15 (2005) 67-72
    • (2005) Curr Opin Neurobiol , vol.15 , pp. 67-72
    • Matus, A.1
  • 159
    • 36049020643 scopus 로고    scopus 로고
    • Oral supplementation with docosahexaenoic acid and uridine 5'-monophosphate increases dendritic spine density in adult gerbil hippocampus
    • Sakamoto T., Cansev M., and Wurtman R.J. Oral supplementation with docosahexaenoic acid and uridine 5'-monophosphate increases dendritic spine density in adult gerbil hippocampus. Brain Res 1182 (2007) 50-59
    • (2007) Brain Res , vol.1182 , pp. 50-59
    • Sakamoto, T.1    Cansev, M.2    Wurtman, R.J.3
  • 160
    • 0024434701 scopus 로고
    • Arachidonic acid induces a long-term activity-dependent enhancement of synaptic transmission in the hippocampus
    • Williams J.H., Errington M.L., Lynch M.A., and Bliss T.V.P. Arachidonic acid induces a long-term activity-dependent enhancement of synaptic transmission in the hippocampus. Nature 341 (1989) 739-742
    • (1989) Nature , vol.341 , pp. 739-742
    • Williams, J.H.1    Errington, M.L.2    Lynch, M.A.3    Bliss, T.V.P.4
  • 161
    • 0037162476 scopus 로고    scopus 로고
    • Postsynaptic transient K(+) current modulated by arachidonic acid regulates synaptic integration and threshold for LTP induction in hippocampal pyramidal cells
    • Ramakers G.M., and Storm J.F.A. Postsynaptic transient K(+) current modulated by arachidonic acid regulates synaptic integration and threshold for LTP induction in hippocampal pyramidal cells. Proc Natl Acad Sci U S A 99 (2002) 10144-10149
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10144-10149
    • Ramakers, G.M.1    Storm, J.F.A.2
  • 162
    • 0346218111 scopus 로고    scopus 로고
    • 12-lipoxygenase metabolites of arachidonic acid mediate metabotropic glutamate receptor-dependent long-term depression at hippocampal CA3-CA1 synapses
    • Feinmark S.J., Begum R., Tsvetkov E., Goussakov I., Funk C.D., Siegelbaum S.A., et al. 12-lipoxygenase metabolites of arachidonic acid mediate metabotropic glutamate receptor-dependent long-term depression at hippocampal CA3-CA1 synapses. J Neurosci 23 (2003) 11427-11435
    • (2003) J Neurosci , vol.23 , pp. 11427-11435
    • Feinmark, S.J.1    Begum, R.2    Tsvetkov, E.3    Goussakov, I.4    Funk, C.D.5    Siegelbaum, S.A.6
  • 163
    • 0030992565 scopus 로고    scopus 로고
    • Membrane fatty acid modifications of PC12 cells by arachidonate or docosahexaenoate affect neurite outgrowth but not norepinephrine release
    • Ikemoto A., Kobayashi T., Watanabe S., and Okuyama H. Membrane fatty acid modifications of PC12 cells by arachidonate or docosahexaenoate affect neurite outgrowth but not norepinephrine release. Neurochem Res 22 (1997) 671-678
    • (1997) Neurochem Res , vol.22 , pp. 671-678
    • Ikemoto, A.1    Kobayashi, T.2    Watanabe, S.3    Okuyama, H.4
  • 164
    • 4143102415 scopus 로고    scopus 로고
    • Docosahexaenoic acid promotes neurite growth in hippocampal neurons
    • Calderon F., and Kim H.-Y. Docosahexaenoic acid promotes neurite growth in hippocampal neurons. J Neurochem 90 (2004) 979-988
    • (2004) J Neurochem , vol.90 , pp. 979-988
    • Calderon, F.1    Kim, H.-Y.2
  • 165
    • 23444445642 scopus 로고    scopus 로고
    • Dietary uridine-5'-monophosphate supplementation increases potassium-evoked dopamine release and promotes neurite outgrowth in aged rats
    • Wang L., Pooler A.M., Albrecht M.A., and Wurtman R.J. Dietary uridine-5'-monophosphate supplementation increases potassium-evoked dopamine release and promotes neurite outgrowth in aged rats. J Mol Neurosci 27 (2005) 137-145
    • (2005) J Mol Neurosci , vol.27 , pp. 137-145
    • Wang, L.1    Pooler, A.M.2    Albrecht, M.A.3    Wurtman, R.J.4
  • 166
    • 33846304174 scopus 로고    scopus 로고
    • Dietary supplementation with uridine-5'-monophosphate (UMP), a membrane phosphatide precursor, increases acetylcholine level and release in striatum of aged rat
    • Wang L., Albrecht M.A., and Wurtman R.J. Dietary supplementation with uridine-5'-monophosphate (UMP), a membrane phosphatide precursor, increases acetylcholine level and release in striatum of aged rat. Brain Res 1133 (2007) 42-48
    • (2007) Brain Res , vol.1133 , pp. 42-48
    • Wang, L.1    Albrecht, M.A.2    Wurtman, R.J.3
  • 167
    • 33745742679 scopus 로고    scopus 로고
    • International Union of Pharmacology LVIII: update on the P2Y G protein-coupled nucleotide receptors: from molecular mechanisms and pathophysiology to therapy
    • Abbracchio M.P., Burnstock G., Boeynaems J.-M., Barnard E.A., Boyer J.L., Kennedy C., et al. International Union of Pharmacology LVIII: update on the P2Y G protein-coupled nucleotide receptors: from molecular mechanisms and pathophysiology to therapy. Pharmacol Rev 58 (2006) 281-341
    • (2006) Pharmacol Rev , vol.58 , pp. 281-341
    • Abbracchio, M.P.1    Burnstock, G.2    Boeynaems, J.-M.3    Barnard, E.A.4    Boyer, J.L.5    Kennedy, C.6
  • 168
    • 12244289617 scopus 로고    scopus 로고
    • Long-term potentiation of glutamatergic synaptic transmission induced by activation of presynaptic P2Y receptors in the rat medial habenula nucleus
    • Price G.D., Robertson S.J., and Edwards F.A. Long-term potentiation of glutamatergic synaptic transmission induced by activation of presynaptic P2Y receptors in the rat medial habenula nucleus. Eur J Neurosci 17 (2003) 844-850
    • (2003) Eur J Neurosci , vol.17 , pp. 844-850
    • Price, G.D.1    Robertson, S.J.2    Edwards, F.A.3
  • 169
    • 0346024190 scopus 로고    scopus 로고
    • Genesis of dendritic spines: insights from ultrastructural and imaging studies
    • Yuste R., and Bonhoeffer T. Genesis of dendritic spines: insights from ultrastructural and imaging studies. Nat Rev Neurosci 5 (2004) 24-34
    • (2004) Nat Rev Neurosci , vol.5 , pp. 24-34
    • Yuste, R.1    Bonhoeffer, T.2
  • 170
    • 33751118287 scopus 로고    scopus 로고
    • Chronic administration of UMP ameliorates the impairment of hippocampal-dependent memory in impoverished rats
    • Teather L.A., and Wurtman R.J. Chronic administration of UMP ameliorates the impairment of hippocampal-dependent memory in impoverished rats. J Nutr 136 (2006) 2834-2837
    • (2006) J Nutr , vol.136 , pp. 2834-2837
    • Teather, L.A.1    Wurtman, R.J.2


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