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Volumn 2, Issue C, 1997, Pages 287-322

The CDP-ethanolamine pathway in mammalian cells

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EID: 0000109851     PISSN: 18745245     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-5245(97)80013-4     Document Type: Article
Times cited : (7)

References (191)
  • 1
    • 0017613194 scopus 로고
    • Factors controlling the biosynthesis of individual phosphoglycerides in liver
    • kesson B., and Sundler R. Factors controlling the biosynthesis of individual phosphoglycerides in liver. Biochem. Soc. Trans. 5 (1977) 43-48
    • (1977) Biochem. Soc. Trans. , vol.5 , pp. 43-48
    • kesson, B.1    Sundler, R.2
  • 2
    • 0027377058 scopus 로고
    • Involvement of mitochondrial contact sites in the subcellular compartmentalization of phosholipid biosynthetic enzymes
    • Ardail D., Gasnier F., Lermé F., Simonot C., Louisot P., and Gateau-Roesch O. Involvement of mitochondrial contact sites in the subcellular compartmentalization of phosholipid biosynthetic enzymes. J. Biol. Chem. 268 (1993) 25985-25992
    • (1993) J. Biol. Chem. , vol.268 , pp. 25985-25992
    • Ardail, D.1    Gasnier, F.2    Lermé, F.3    Simonot, C.4    Louisot, P.5    Gateau-Roesch, O.6
  • 3
    • 0025957105 scopus 로고
    • Synthesis of phosphatidylethanolamine and ethanolamine plasmalogen by the CDP-ethanolamine and decarboxylase pathways in rat heart, kidney and liver
    • Arthur G., and Page L. Synthesis of phosphatidylethanolamine and ethanolamine plasmalogen by the CDP-ethanolamine and decarboxylase pathways in rat heart, kidney and liver. Biochem. J. 273 (1991) 121-125
    • (1991) Biochem. J. , vol.273 , pp. 121-125
    • Arthur, G.1    Page, L.2
  • 4
    • 0027282811 scopus 로고
    • The ethanolamine requirement of keratinocytes for growth is not due to defective synthesis of ethanolamine phosphoacylglycerols by the decarboxylation pathway
    • Arthur G., and Lu X. The ethanolamine requirement of keratinocytes for growth is not due to defective synthesis of ethanolamine phosphoacylglycerols by the decarboxylation pathway. Biochem. J. 293 (1993) 125-130
    • (1993) Biochem. J. , vol.293 , pp. 125-130
    • Arthur, G.1    Lu, X.2
  • 5
    • 0021364174 scopus 로고
    • High-performance liquid Chromatographie determination of serum aliphatic amine in chronic renal failure
    • Baba S., Watanabe Y., Gajyo F., and Arakawa M. High-performance liquid Chromatographie determination of serum aliphatic amine in chronic renal failure. Clin. Chi m. Acta 136 (1984) 49-56
    • (1984) Clin. Chi m. Acta , vol.136 , pp. 49-56
    • Baba, S.1    Watanabe, Y.2    Gajyo, F.3    Arakawa, M.4
  • 6
    • 0019156821 scopus 로고
    • Topography of phosphatidylcholine, phosphatidylethanolamine and triacylglycerol biosynthetic enzymes in rat liver microsomes
    • Ballas L.M., and Bell R.M. Topography of phosphatidylcholine, phosphatidylethanolamine and triacylglycerol biosynthetic enzymes in rat liver microsomes. Biochim. Biophys. Acta 602 (1980) 578-590
    • (1980) Biochim. Biophys. Acta , vol.602 , pp. 578-590
    • Ballas, L.M.1    Bell, R.M.2
  • 7
    • 0018846846 scopus 로고
    • Enzymes of glycerolipid synthesis in eukaryotes
    • Bell R.M., and Coleman R.A. Enzymes of glycerolipid synthesis in eukaryotes. Annu. Rev. Biochem. 49 (1980) 459-487
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 459-487
    • Bell, R.M.1    Coleman, R.A.2
  • 8
    • 0025356574 scopus 로고
    • The regulation and cellular functions of phosphatidylcholine hydrolysis
    • Billah M.M., and Anthes J.C. The regulation and cellular functions of phosphatidylcholine hydrolysis. Biochem. J. 269 (1991) 281-291
    • (1991) Biochem. J. , vol.269 , pp. 281-291
    • Billah, M.M.1    Anthes, J.C.2
  • 9
    • 0024150892 scopus 로고
    • Assembly of phospholipids into cellular membranes. Biosynthesis, transmembrane movement and intracellular translocation
    • Bishop W.P., and Bell R.M. Assembly of phospholipids into cellular membranes. Biosynthesis, transmembrane movement and intracellular translocation. Ann. Rev. Cell Biol. 4 (1988) 579-610
    • (1988) Ann. Rev. Cell Biol. , vol.4 , pp. 579-610
    • Bishop, W.P.1    Bell, R.M.2
  • 10
    • 0015932054 scopus 로고
    • 2+-stimulated incorporation of nitrogen bases into microsomal phospholipids
    • 2+-stimulated incorporation of nitrogen bases into microsomal phospholipids. Biochim. Biophys. Acta 306 (1973) 396-402
    • (1973) Biochim. Biophys. Acta , vol.306 , pp. 396-402
    • Bjerve, K.S.1
  • 11
    • 0021970180 scopus 로고
    • The biosynthesis of phosphatidylserine and phosphatidylethanolamine from L-[3-14C]serine in isolated rat hepatocytes
    • Bjerve K.S. The biosynthesis of phosphatidylserine and phosphatidylethanolamine from L-[3-14C]serine in isolated rat hepatocytes. Biochim. Biophys. Acta 833 (1985) 396-405
    • (1985) Biochim. Biophys. Acta , vol.833 , pp. 396-405
    • Bjerve, K.S.1
  • 12
    • 0013874131 scopus 로고
    • In vivo studies on pathways for the biosynthesis of lecithin in the rat
    • Björnstad P., and Bremer J. In vivo studies on pathways for the biosynthesis of lecithin in the rat. J. Lipid Res. 7 (1966) 38-45
    • (1966) J. Lipid Res. , vol.7 , pp. 38-45
    • Björnstad, P.1    Bremer, J.2
  • 13
    • 0002360622 scopus 로고
    • Enzymatic formation and decarboxylation of phosphatidylserine
    • Borkenhagen L.F., Kennedy E.P., and Fielding L. Enzymatic formation and decarboxylation of phosphatidylserine. J. Biol. Chem. 236 (1961) 28-29
    • (1961) J. Biol. Chem. , vol.236 , pp. 28-29
    • Borkenhagen, L.F.1    Kennedy, E.P.2    Fielding, L.3
  • 14
    • 0000226495 scopus 로고
    • The biosynthesis of choline and its relation to phospholipid metabolism
    • Bremer J., Figard P.H., and Greenberg D.M. The biosynthesis of choline and its relation to phospholipid metabolism. Biochim. Biophys. Acta 43 (1960) 477-488
    • (1960) Biochim. Biophys. Acta , vol.43 , pp. 477-488
    • Bremer, J.1    Figard, P.H.2    Greenberg, D.M.3
  • 15
    • 0017692143 scopus 로고
    • Choline kinase and ethanolamine kinase are separate, soluble enzymes in rat liver
    • Brophy P.J., Choy P.C., Toone J.R., and Vance D.E. Choline kinase and ethanolamine kinase are separate, soluble enzymes in rat liver. Eur. J. Biochem. 78 (1977) 491-495
    • (1977) Eur. J. Biochem. , vol.78 , pp. 491-495
    • Brophy, P.J.1    Choy, P.C.2    Toone, J.R.3    Vance, D.E.4
  • 16
    • 0023896759 scopus 로고
    • l-Ether-linked phosphoglycerides. Major endogenous sources of arachidonate in the human neutrophil
    • Chilton F.H., and Connell T.R. l-Ether-linked phosphoglycerides. Major endogenous sources of arachidonate in the human neutrophil. J. Biol. Chem. 263 (1988) 5260-5265
    • (1988) J. Biol. Chem. , vol.263 , pp. 5260-5265
    • Chilton, F.H.1    Connell, T.R.2
  • 17
    • 0018187973 scopus 로고
    • Lipid requirements for activation of CTP:phosphocholine cytidylyltransferase from rat liver
    • Choy P.C., and Vance D.E. Lipid requirements for activation of CTP:phosphocholine cytidylyltransferase from rat liver. J. Biol. Chem. 253 (1978) 5163-5167
    • (1978) J. Biol. Chem. , vol.253 , pp. 5163-5167
    • Choy, P.C.1    Vance, D.E.2
  • 18
    • 0017848044 scopus 로고
    • Evidence that biosynthesis of phosphatidylethanolamine, phosphatidylcholine, and triacylglycerol occurs on the cytoplasmic side of microsomal versicles
    • Coleman R., and Bell R.M. Evidence that biosynthesis of phosphatidylethanolamine, phosphatidylcholine, and triacylglycerol occurs on the cytoplasmic side of microsomal versicles. J. Cell Biol. 76 (1978) 245-253
    • (1978) J. Cell Biol. , vol.76 , pp. 245-253
    • Coleman, R.1    Bell, R.M.2
  • 19
    • 0011024356 scopus 로고
    • Cholinephosphotransferase
    • Vance D.E. (Ed), CRC Press Inc., Boca Raton, FL
    • Cornell R. Cholinephosphotransferase. In: Vance D.E. (Ed). Phosphatidylcholine Metabolism (1989), CRC Press Inc., Boca Raton, FL 47-64
    • (1989) Phosphatidylcholine Metabolism , pp. 47-64
    • Cornell, R.1
  • 20
    • 0024364943 scopus 로고
    • Chemical cross-linking reveals a dimeric structure for CTP:phosphocholine cytidylyltransferase
    • Cornell R. Chemical cross-linking reveals a dimeric structure for CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 264 (1989) 9077-9082
    • (1989) J. Biol. Chem. , vol.264 , pp. 9077-9082
    • Cornell, R.1
  • 21
    • 0025886751 scopus 로고
    • Regulation of CTP phosphocholine cytidylyltransferase by lipids. 1. Negative surface charge dependence for activation
    • Cornell R.B. Regulation of CTP phosphocholine cytidylyltransferase by lipids. 1. Negative surface charge dependence for activation. Biochemistry 30 (1991) 5873-5880
    • (1991) Biochemistry , vol.30 , pp. 5873-5880
    • Cornell, R.B.1
  • 22
    • 0025778806 scopus 로고
    • Regulation of CTP:phosphocholine cytidylyltransferase by lipids. 2. Surface curvature, acyl chain length, and lipid-phase dependence for activation
    • Cornell R.B. Regulation of CTP:phosphocholine cytidylyltransferase by lipids. 2. Surface curvature, acyl chain length, and lipid-phase dependence for activation. Biochemistry 30 (1991) 5881-5888
    • (1991) Biochemistry , vol.30 , pp. 5881-5888
    • Cornell, R.B.1
  • 23
    • 0022351161 scopus 로고
    • Solubilization and reconstitution of cholinephosphotransferase from sarcoplasmic reticulum: Stabilization of solubilized enzyme by diacylglycerol and glycerol
    • Cornell R., and MacLennan D.H. Solubilization and reconstitution of cholinephosphotransferase from sarcoplasmic reticulum: Stabilization of solubilized enzyme by diacylglycerol and glycerol. Biochim. Biophys. Acta 821 (1985) 97-105
    • (1985) Biochim. Biophys. Acta , vol.821 , pp. 97-105
    • Cornell, R.1    MacLennan, D.H.2
  • 24
    • 0021340291 scopus 로고
    • Isolation of plasma membrane, Golgi apparatus and endoplasmic reticulum fractions from single homogenates of mouse liver
    • Croze E.M., and Morré D.J. Isolation of plasma membrane, Golgi apparatus and endoplasmic reticulum fractions from single homogenates of mouse liver. J. Cell. Physiol. 119 (1984) 46-57
    • (1984) J. Cell. Physiol. , vol.119 , pp. 46-57
    • Croze, E.M.1    Morré, D.J.2
  • 25
    • 0027182769 scopus 로고
    • Cloning and expression of a novel phosphatidylethanolamine /V-methyltransferase A specific biochemical and cytological marker for a unique membrane fraction in rat liver
    • Cui Z., Vance J.E., Chen M.H., Voelker D.R., and Vance D.E. Cloning and expression of a novel phosphatidylethanolamine /V-methyltransferase A specific biochemical and cytological marker for a unique membrane fraction in rat liver. J. Biol. Chem. 268 (1993) 16655-16663
    • (1993) J. Biol. Chem. , vol.268 , pp. 16655-16663
    • Cui, Z.1    Vance, J.E.2    Chen, M.H.3    Voelker, D.R.4    Vance, D.E.5
  • 26
    • 0019833703 scopus 로고
    • Source of arachidonic acid for prostaglandin synthesis in Madin-Darby canine kidney cells
    • Daniel L.W., King L., and Waite M. Source of arachidonic acid for prostaglandin synthesis in Madin-Darby canine kidney cells. J. Biol. Chem. 24 (1981) 12830-12835
    • (1981) J. Biol. Chem. , vol.24 , pp. 12830-12835
    • Daniel, L.W.1    King, L.2    Waite, M.3
  • 27
    • 0015470777 scopus 로고
    • Intracellular sites of lipid synthesis and the biogenesis of mitochodria
    • Dennis E.A., and Kennedy E.P. Intracellular sites of lipid synthesis and the biogenesis of mitochodria. J. Lipid Res. 13 (1972) 263-267
    • (1972) J. Lipid Res. , vol.13 , pp. 263-267
    • Dennis, E.A.1    Kennedy, E.P.2
  • 29
    • 0025081948 scopus 로고
    • Isolation and characterization of the human liver ethanolamine kinase
    • Draus E., Niefind J., Victor K., and Havsteen B. Isolation and characterization of the human liver ethanolamine kinase. Biochim. Biophys. Acta 1045 (1990) 195-204
    • (1990) Biochim. Biophys. Acta , vol.1045 , pp. 195-204
    • Draus, E.1    Niefind, J.2    Victor, K.3    Havsteen, B.4
  • 30
    • 0019888255 scopus 로고
    • Thermolabile CDP-choline synthetase in an animal cell mutant defective in lecithin formation
    • Esko J.D., Wermuth M.M., and Raetz C.R.M. Thermolabile CDP-choline synthetase in an animal cell mutant defective in lecithin formation. J. Biol. Chem. 256 (1981) 7388-7393
    • (1981) J. Biol. Chem. , vol.256 , pp. 7388-7393
    • Esko, J.D.1    Wermuth, M.M.2    Raetz, C.R.M.3
  • 31
    • 0018101532 scopus 로고
    • The role of phosphatidylglycerol in the activation of CTPiphosphocholine cytidylyltransferase from rat lung
    • Feldman DA., Kova C.C.R., Dranginis PL., and Weinhold P.A. The role of phosphatidylglycerol in the activation of CTPiphosphocholine cytidylyltransferase from rat lung. J. Biol. Chem. 253 (1978) 4980-4986
    • (1978) J. Biol. Chem. , vol.253 , pp. 4980-4986
    • Feldman, DA.1    Kova, C.C.R.2    Dranginis, PL.3    Weinhold, P.A.4
  • 32
    • 0023645095 scopus 로고
    • CTP:phosphorylcholine cytidylyltransferase from rat liver. Isolation and characterization of the catalytic subunit
    • Feldman D.A., and Weinhold P.A. CTP:phosphorylcholine cytidylyltransferase from rat liver. Isolation and characterization of the catalytic subunit. J. Biol. Chem. 262 (1987) 9075-9081
    • (1987) J. Biol. Chem. , vol.262 , pp. 9075-9081
    • Feldman, D.A.1    Weinhold, P.A.2
  • 33
    • 0027513762 scopus 로고
    • Identification of a protein complex between choline-phosphate cytidylyltransferase and a 112-kDa protein in rat liver
    • Feldman D.A., and Weinhold P.A. Identification of a protein complex between choline-phosphate cytidylyltransferase and a 112-kDa protein in rat liver. J. Biol. Chem. 268 (1993) 3127-3135
    • (1993) J. Biol. Chem. , vol.268 , pp. 3127-3135
    • Feldman, D.A.1    Weinhold, P.A.2
  • 34
    • 0016378181 scopus 로고
    • Subcellular fractionation of rat liver
    • Fleischer S., and Kervina M. Subcellular fractionation of rat liver. Methods Enzymol. 31 (1974) 6-41
    • (1974) Methods Enzymol. , vol.31 , pp. 6-41
    • Fleischer, S.1    Kervina, M.2
  • 35
    • 0024672061 scopus 로고
    • Plasmenylethanolamine is the major storage depot for arachidonic acid in rabbit vascular smooth muscle and is rapidly hydrolyzed after angiotesin II stimulation
    • Ford D.A., and Gross R.W. Plasmenylethanolamine is the major storage depot for arachidonic acid in rabbit vascular smooth muscle and is rapidly hydrolyzed after angiotesin II stimulation. Proc. Natl. Acad. Sci. USA 86 (1989) 3479-3483
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3479-3483
    • Ford, D.A.1    Gross, R.W.2
  • 36
    • 0026643973 scopus 로고
    • The primary determinant of rabbit myocardial ethanolamine phosphotransferase substrate selectivity is the covalent nature of the sn-1 aliphatic group of diradyl glycerol acceptors
    • Ford D.A., Rosenbloom K.B., and Gross R.W. The primary determinant of rabbit myocardial ethanolamine phosphotransferase substrate selectivity is the covalent nature of the sn-1 aliphatic group of diradyl glycerol acceptors. J. Biol. Chem. 267 (1992) 11222-11228
    • (1992) J. Biol. Chem. , vol.267 , pp. 11222-11228
    • Ford, D.A.1    Rosenbloom, K.B.2    Gross, R.W.3
  • 37
    • 0020024570 scopus 로고
    • Topographic distribution of enzymes synthesizing phosphatidylcholine and phosphatidylethanolamine in chicken brain microsomes
    • Freysz L., Harth S., and Dreyfus H. Topographic distribution of enzymes synthesizing phosphatidylcholine and phosphatidylethanolamine in chicken brain microsomes. J. Neurochem. 38 (1982) 582-587
    • (1982) J. Neurochem. , vol.38 , pp. 582-587
    • Freysz, L.1    Harth, S.2    Dreyfus, H.3
  • 41
    • 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 Porcellati 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    Porcellati, G.4
  • 42
    • 0023054506 scopus 로고
    • A comparison of the reversibility of phosphoethanolamine transferase and phosphocholine transferee in rat brain microsomes
    • Goracci G., Francescangeli E., Horrocks L., and Porcellati G. A comparison of the reversibility of phosphoethanolamine transferase and phosphocholine transferee 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.3    Porcellati, G.4
  • 43
    • 0018611980 scopus 로고
    • The effect of fasting and refeeding on the composition and synthesis of triacylglycerols, phosphatidylcholines, and phosphatidylethanolamines in rat liver
    • Groener J.E.M., Klein W., and van Golde L.M.G. The effect of fasting and refeeding on the composition and synthesis of triacylglycerols, phosphatidylcholines, and phosphatidylethanolamines in rat liver. Arch. Biochem. Biophys. 198 (1979) 287-295
    • (1979) Arch. Biochem. Biophys. , vol.198 , pp. 287-295
    • Groener, J.E.M.1    Klein, W.2    van Golde, L.M.G.3
  • 44
    • 0021740333 scopus 로고
    • Phosphorylethanolamine - the major constituent of the phosphomonoester peak observed by 3IP-NMR in developing dog brain
    • Gyulai L., Bolinger L., Leigh Jr. J.S., Barlow C., and Chance B. Phosphorylethanolamine - the major constituent of the phosphomonoester peak observed by 3IP-NMR in developing dog brain. FEBSLett. 178 (1984) 137-142
    • (1984) FEBSLett. , vol.178 , pp. 137-142
    • Gyulai, L.1    Bolinger, L.2    Leigh Jr., J.S.3    Barlow, C.4    Chance, B.5
  • 45
    • 0021130324 scopus 로고
    • Synthesis of phosphatidylcholines in rat hepatocytes. Possible regulation by norepinephrine via an a-adrenergic mechanism
    • Haagsman H.P., van den Heuvel J.M., van Golde L.M.G., and Geelen M.J.H. Synthesis of phosphatidylcholines in rat hepatocytes. Possible regulation by norepinephrine via an a-adrenergic mechanism. J. Biol. Chem. 259 (1984) 11273-11278
    • (1984) J. Biol. Chem. , vol.259 , pp. 11273-11278
    • Haagsman, H.P.1    van den Heuvel, J.M.2    van Golde, L.M.G.3    Geelen, M.J.H.4
  • 46
    • 0025789988 scopus 로고
    • Phorbol ester-stimulated hydrolysis of phosphatidylcholine and phosphatidylethanolamine by phospholipase D in HeLa cells: Evidence that the basal turnover of phosphoglycerides does not involve phospholipase D
    • Hii C.S.T., Edwards Y.S., and Murray AW. Phorbol ester-stimulated hydrolysis of phosphatidylcholine and phosphatidylethanolamine by phospholipase D in HeLa cells: Evidence that the basal turnover of phosphoglycerides does not involve phospholipase D. J. Biol. Chem. 266 (1991) 20238-20243
    • (1991) J. Biol. Chem. , vol.266 , pp. 20238-20243
    • Hii, C.S.T.1    Edwards, Y.S.2    Murray, AW.3
  • 47
    • 0023654278 scopus 로고
    • Mutants of Saccharomyces cerevisiae defective in sn-l,2-diacylglycerol cholinephosphotransferase Isolation, characterization, and cloning of the CPT1 gene
    • Hjelmstad R.H., and Bell R.M. Mutants of Saccharomyces cerevisiae defective in sn-l,2-diacylglycerol cholinephosphotransferase Isolation, characterization, and cloning of the CPT1 gene. J. Biol. Chem. 262 (1987) 3909-3917
    • (1987) J. Biol. Chem. , vol.262 , pp. 3909-3917
    • Hjelmstad, R.H.1    Bell, R.M.2
  • 48
    • 0024297462 scopus 로고
    • The sn-l,2-diacylglycerol ethanolaminephosphotransferase activity of Saccharomyces cerevisiae. Isolation of mutants and cloning of the EPT1 gene
    • Hjelmstad R.H., and Bell R.M. The sn-l,2-diacylglycerol ethanolaminephosphotransferase activity of Saccharomyces cerevisiae. Isolation of mutants and cloning of the EPT1 gene. J. Biol. Chem. 263 (1988) 19748-19757
    • (1988) J. Biol. Chem. , vol.263 , pp. 19748-19757
    • Hjelmstad, R.H.1    Bell, R.M.2
  • 49
    • 0025181843 scopus 로고
    • The sn-l,2-diacylglycerol cholinephosphotransferase of Saccharomyces cerevisiae. Nucleotide sequence, transcriptional mapping, and gene product analysis of the CPTJ gene
    • Hjelmstad R.H., and Bell R.M. The sn-l,2-diacylglycerol cholinephosphotransferase of Saccharomyces cerevisiae. Nucleotide sequence, transcriptional mapping, and gene product analysis of the CPTJ gene. J. Biol. Chem. 265 (1990) 1755-1764
    • (1990) J. Biol. Chem. , vol.265 , pp. 1755-1764
    • Hjelmstad, R.H.1    Bell, R.M.2
  • 50
    • 0025805689 scopus 로고
    • jn-l,2-Diacylglycerol choline-and ethanolaminephosphotransferases in Saccharomyces cerevisiae. Nucleotide sequence of the EPT1 gene and comparison of the CPTJ and EPT1 gene products
    • Hjelmstad R.H., and Bell R.M. jn-l,2-Diacylglycerol choline-and ethanolaminephosphotransferases in Saccharomyces cerevisiae. Nucleotide sequence of the EPT1 gene and comparison of the CPTJ and EPT1 gene products. J. Biol. Chem. 266 (1991) 5094-5103
    • (1991) J. Biol. Chem. , vol.266 , pp. 5094-5103
    • Hjelmstad, R.H.1    Bell, R.M.2
  • 51
    • 0025806498 scopus 로고
    • sn-1,2-Diacylglycerol choline-and ethanolaminephosphotransferases in Saccharomyces cerevisiae. Mixed micellar analysis of the CPT1 and EPT1 gene products
    • Hjelmstad R.H., and Bell R.M. sn-1,2-Diacylglycerol choline-and ethanolaminephosphotransferases in Saccharomyces cerevisiae. Mixed micellar analysis of the CPT1 and EPT1 gene products. J. Biol. Chem. 266 (1991) 4357-4365
    • (1991) J. Biol. Chem. , vol.266 , pp. 4357-4365
    • Hjelmstad, R.H.1    Bell, R.M.2
  • 52
    • 0017842211 scopus 로고
    • Differential utilization of 1-palmitoyl and 1-stearoyl homologues of various unsaturated 1,2-diacyl-M-glycerols for phosphatidylcholine and phosphatidylethanolamine synthesis in rat liver microsomes
    • Holub B.J. Differential utilization of 1-palmitoyl and 1-stearoyl homologues of various unsaturated 1,2-diacyl-M-glycerols for phosphatidylcholine and phosphatidylethanolamine synthesis in rat liver microsomes. J. Biol. Chem. 253 (1978) 691-696
    • (1978) J. Biol. Chem. , vol.253 , pp. 691-696
    • Holub, B.J.1
  • 53
    • 0026751161 scopus 로고
    • Cloning of a human choline kinase cDNA by complementation of the yeast cki mutation
    • Hosaka K., Tanaka S., Nikawa J., and Yamashita S. Cloning of a human choline kinase cDNA by complementation of the yeast cki mutation. FEBS Lett. 304 (1992) 229-232
    • (1992) FEBS Lett. , vol.304 , pp. 229-232
    • Hosaka, K.1    Tanaka, S.2    Nikawa, J.3    Yamashita, S.4
  • 54
    • 0025816080 scopus 로고
    • Phosphatidylcholine metabolism in rat liver after partial hepatectomy. Evidence for increased activity and amount of CTP:phosphocholine cytidylyltransferase
    • Houweling M., Tijburg L.B.M., Jamil H., Vance D.E., Nyathi C.B., Vaartjes W.J., and van Golde L.M.G. Phosphatidylcholine metabolism in rat liver after partial hepatectomy. Evidence for increased activity and amount of CTP:phosphocholine cytidylyltransferase. Biochem. J. 278 (1991) 347-351
    • (1991) Biochem. J. , vol.278 , pp. 347-351
    • Houweling, M.1    Tijburg, L.B.M.2    Jamil, H.3    Vance, D.E.4    Nyathi, C.B.5    Vaartjes, W.J.6    van Golde, L.M.G.7
  • 55
    • 0026545179 scopus 로고
    • Phosphatidylethanolamine metabolism in rat liver after partial hepatectomy. Control of biosynthesis of phosphatidylethanolamine by the availability of ethanolamine
    • Houweling M., Tijburg L.B.M., Vaartjes W.J., and Van Golde L.M.G. Phosphatidylethanolamine metabolism in rat liver after partial hepatectomy. Control of biosynthesis of phosphatidylethanolamine by the availability of ethanolamine. Biochem. J. 283 (1992) 55-61
    • (1992) Biochem. J. , vol.283 , pp. 55-61
    • Houweling, M.1    Tijburg, L.B.M.2    Vaartjes, W.J.3    Van Golde, L.M.G.4
  • 56
    • 0027300046 scopus 로고
    • Evidence that CTPxholine-phosphate cytidylyltransferase is regulated at a pretanslational level in rat liver after partial hepatectomy
    • Houweling M., Tijburg L.B.M., Vaartjes W.J., Batenburg J.J., Kalmar G.B., Cornell R.B., and van Golde L.M.G. Evidence that CTPxholine-phosphate cytidylyltransferase is regulated at a pretanslational level in rat liver after partial hepatectomy. Eur. J. Biochem. 214 (1993) 927-933
    • (1993) Eur. J. Biochem. , vol.214 , pp. 927-933
    • Houweling, M.1    Tijburg, L.B.M.2    Vaartjes, W.J.3    Batenburg, J.J.4    Kalmar, G.B.5    Cornell, R.B.6    van Golde, L.M.G.7
  • 57
    • 0025091897 scopus 로고
    • Improved methods to isolate and subfractionate rat liver mitochondria. Lipid composition of the inner and outer membrane
    • Hovius R., Lambrechts H., Nicolay K., and De Kruijff B. Improved methods to isolate and subfractionate rat liver mitochondria. Lipid composition of the inner and outer membrane. Biochim. Biophys. Acta 1021 (1990) 217-226
    • (1990) Biochim. Biophys. Acta , vol.1021 , pp. 217-226
    • Hovius, R.1    Lambrechts, H.2    Nicolay, K.3    De Kruijff, B.4
  • 58
    • 0026785368 scopus 로고
    • On the mechanism of the mitochrondrial decarboxylation of phosphatidylserine
    • Hovius R., Faber B., Brigot B., Nicolay K., and De Kruijff B. On the mechanism of the mitochrondrial decarboxylation of phosphatidylserine. J. Biol. Chem. 267 (1992) 16790-16795
    • (1992) J. Biol. Chem. , vol.267 , pp. 16790-16795
    • Hovius, R.1    Faber, B.2    Brigot, B.3    Nicolay, K.4    De Kruijff, B.5
  • 59
    • 0023665131 scopus 로고
    • Absorption and transport of base moieties of phosphatidylcholine and phosphatidylethanolamine in rats
    • Ikeda I., Imaizumi K., and Sugano M. Absorption and transport of base moieties of phosphatidylcholine and phosphatidylethanolamine in rats. Biochim. Biophys. Acta 921 (1987) 245-253
    • (1987) Biochim. Biophys. Acta , vol.921 , pp. 245-253
    • Ikeda, I.1    Imaizumi, K.2    Sugano, M.3
  • 60
    • 0024447421 scopus 로고
    • Effect of phosphatidylethanolamine and its constituent base on the metabolism of linoleic acid in rat liver
    • Imaizumi K., Sakono M., Mawatari K., Murata M., and Sugano M. Effect of phosphatidylethanolamine and its constituent base on the metabolism of linoleic acid in rat liver. Biochim. Biophys. Acta 1005 (1989) 253-259
    • (1989) Biochim. Biophys. Acta , vol.1005 , pp. 253-259
    • Imaizumi, K.1    Sakono, M.2    Mawatari, K.3    Murata, M.4    Sugano, M.5
  • 61
    • 0017109815 scopus 로고
    • Phospholipid synthesis in mammary tissue. Choline and ethanolamine kinases: Kinetic evidence for two discrete active sites
    • Infante J.P., and Kinsella J.E. Phospholipid synthesis in mammary tissue. Choline and ethanolamine kinases: Kinetic evidence for two discrete active sites. Lipids 11 (1976) 727-735
    • (1976) Lipids , vol.11 , pp. 727-735
    • Infante, J.P.1    Kinsella, J.E.2
  • 62
    • 0017717033 scopus 로고
    • Rate-limiting steps in the cytidine pathway for the synthesis of phosphatidylcholine and phosphatidylethanolamine
    • Infante J.P. Rate-limiting steps in the cytidine pathway for the synthesis of phosphatidylcholine and phosphatidylethanolamine. Biochem. J. 167 (1977) 847-849
    • (1977) Biochem. J. , vol.167 , pp. 847-849
    • Infante, J.P.1
  • 63
    • 0001991171 scopus 로고
    • Choline transport and choline kinase
    • Vance D.E. (Ed), CRC Press Inc., Boca Raton, FL
    • Ishidate K. Choline transport and choline kinase. In: Vance D.E. (Ed). Phosphatidylcholine Metabolism (1989), CRC Press Inc., Boca Raton, FL 9-32
    • (1989) Phosphatidylcholine Metabolism , pp. 9-32
    • Ishidate, K.1
  • 64
    • 0021678131 scopus 로고
    • Complete purification of choline kinase from rat kidney and preparation of rabbit antibody against rat kidney choline kinase
    • Ishidate K., Nakagomi K., and Nakazawa Y. Complete purification of choline kinase from rat kidney and preparation of rabbit antibody against rat kidney choline kinase. J. Biol. Chem. 259 (1984) 14706-14710
    • (1984) J. Biol. Chem. , vol.259 , pp. 14706-14710
    • Ishidate, K.1    Nakagomi, K.2    Nakazawa, Y.3
  • 65
    • 0022363386 scopus 로고
    • Complete co-purification of choline kinase and ethanolamine kinase from rat kidney and immunological evidence for both activities residing on the same enzyme protein (s) in rat tissue
    • Ishidate K., Furusawa K., and Nakazawa Y. Complete co-purification of choline kinase and ethanolamine kinase from rat kidney and immunological evidence for both activities residing on the same enzyme protein (s) in rat tissue. Biochim. Biophys. Acta 836 (1985) 119-124
    • (1985) Biochim. Biophys. Acta , vol.836 , pp. 119-124
    • Ishidate, K.1    Furusawa, K.2    Nakazawa, Y.3
  • 66
    • 0021954028 scopus 로고
    • Evidence for the existence of multiple forms of choline (ethanolamine) kinase in rat tissues
    • Ishidate K., lida K., Tadokoro K., and Nakazawa Y. Evidence for the existence of multiple forms of choline (ethanolamine) kinase in rat tissues. Biochim. Biophys. Acta 833 (1985) 1-8
    • (1985) Biochim. Biophys. Acta , vol.833 , pp. 1-8
    • Ishidate, K.1    lida, K.2    Tadokoro, K.3    Nakazawa, Y.4
  • 67
    • 0026538888 scopus 로고
    • Choline/ethanolamine kinase from rat kidney
    • Ishidate K., and Nakazawa Y. Choline/ethanolamine kinase from rat kidney. Meth. Enzymol. 209 (1992) 121-134
    • (1992) Meth. Enzymol. , vol.209 , pp. 121-134
    • Ishidate, K.1    Nakazawa, Y.2
  • 68
    • 0026543232 scopus 로고
    • CDPcholine:l,2-diacylglycerol cholinephosphotransferase from rat liver microsomes. II Photoaffinity labeling by radioactive CDP-choline analogs
    • Ishidate K., Matsuo R., and Nakazawa Y. CDPcholine:l,2-diacylglycerol cholinephosphotransferase from rat liver microsomes. II Photoaffinity labeling by radioactive CDP-choline analogs. Biochim. Biophys. Acta 1124 (1992) 36-44
    • (1992) Biochim. Biophys. Acta , vol.1124 , pp. 36-44
    • Ishidate, K.1    Matsuo, R.2    Nakazawa, Y.3
  • 69
    • 0027450135 scopus 로고
    • CDPcholine:l,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. CDPcholine:l,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
  • 70
    • 0025930606 scopus 로고
    • Substrate specificity of CTP:phosphocholine cytidylyltransferase
    • Jamil H., and Vance D.E. Substrate specificity of CTP:phosphocholine cytidylyltransferase. Biochim. Biophys. Acta 1086 (1991) 335-339
    • (1991) Biochim. Biophys. Acta , vol.1086 , pp. 335-339
    • Jamil, H.1    Vance, D.E.2
  • 71
    • 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
  • 72
    • 0027314174 scopus 로고
    • Evidence that binding of CTP:phosphocholine cytidylyltransferase to membranes in rat hepatocytes is modulated by the ratio of bilayer-to non-bilayer-forming lipids
    • Jamil H., Hatch G.M., and Vance D.E. Evidence that binding of CTP:phosphocholine cytidylyltransferase to membranes in rat hepatocytes is modulated by the ratio of bilayer-to non-bilayer-forming lipids. Biochem. J. 291 (1993) 419-427
    • (1993) Biochem. J. , vol.291 , pp. 419-427
    • Jamil, H.1    Hatch, G.M.2    Vance, D.E.3
  • 73
    • 0018265533 scopus 로고
    • Distribution of phospholipid biosynthetic enzymes among cell components of rat liver
    • Jelsema C.J., and Morré D.J. Distribution of phospholipid biosynthetic enzymes among cell components of rat liver. J. Biol. Chem. 253 (1978) 7960-7971
    • (1978) J. Biol. Chem. , vol.253 , pp. 7960-7971
    • Jelsema, C.J.1    Morré, D.J.2
  • 74
    • 0026737180 scopus 로고
    • Comparison of the lipid regulation of yeast and rat CTP:phosphocholine cytidylyltransferase expressed in COS cells
    • Johnson J.E., Kalmar G.B., Sohal P.S., Walkey C.J., Yamashita S., and Cornell R.B. Comparison of the lipid regulation of yeast and rat CTP:phosphocholine cytidylyltransferase expressed in COS cells. Biochem. J. 285 (1992) 815-820
    • (1992) Biochem. J. , vol.285 , pp. 815-820
    • Johnson, J.E.1    Kalmar, G.B.2    Sohal, P.S.3    Walkey, C.J.4    Yamashita, S.5    Cornell, R.B.6
  • 76
    • 0025030678 scopus 로고
    • Cloning and expression of rat liver CTP:phosphocholine cytidylyltransferase: An amphipatic protein that controls phosphatidylcholine synthesis ss
    • Kalmar G.B., Kay R.J., Lachance A., Aebersold R., and Cornell R.B. Cloning and expression of rat liver CTP:phosphocholine cytidylyltransferase: An amphipatic protein that controls phosphatidylcholine synthesis ss. Proc. Natl. Acad. Sci. USA 876 (1990) 6029-6033
    • (1990) Proc. Natl. Acad. Sci. USA , vol.876 , pp. 6029-6033
    • Kalmar, G.B.1    Kay, R.J.2    Lachance, A.3    Aebersold, R.4    Cornell, R.B.5
  • 77
    • 0019270948 scopus 로고
    • The base exchange enzymes and phospholipase D of mammalian tissues
    • Kanfer J.N. The base exchange enzymes and phospholipase D of mammalian tissues. Can. J. Biochem. 58 (1980) 1370-1380
    • (1980) Can. J. Biochem. , vol.58 , pp. 1370-1380
    • Kanfer, J.N.1
  • 78
    • 0002749379 scopus 로고
    • Phospholipase D and the base exchange enzyme
    • CRC Press Inc., Boca Raton, FL
    • Kanfer J.N. Phospholipase D and the base exchange enzyme. Phosphatidylcholine Metabolism (1989), CRC Press Inc., Boca Raton, FL 65-86
    • (1989) Phosphatidylcholine Metabolism , pp. 65-86
    • Kanfer, J.N.1
  • 79
    • 0019803398 scopus 로고
    • Effects of phosphoethanolamine on growth of mammary carcinoma cells in culture
    • Kano-Sueoka T., and Errick J.E. Effects of phosphoethanolamine on growth of mammary carcinoma cells in culture. Exp. Cell Res. 136 (1981) 137-145
    • (1981) Exp. Cell Res. , vol.136 , pp. 137-145
    • Kano-Sueoka, T.1    Errick, J.E.2
  • 80
    • 0023644750 scopus 로고
    • Phosphatidylethanolamine biosynthesis in rat mammary carcinoma cells that require and do not require ethanolamine for proliferation
    • Kano-Sueoka T., and King D.M. Phosphatidylethanolamine biosynthesis in rat mammary carcinoma cells that require and do not require ethanolamine for proliferation. J. Biol. Chem. 262 (1987) 6074-6081
    • (1987) J. Biol. Chem. , vol.262 , pp. 6074-6081
    • Kano-Sueoka, T.1    King, D.M.2
  • 81
    • 0015934663 scopus 로고
    • Utilization of endogenous phospholipids by the back-reaction of CDPcholine (-ethanolamine) : 1,2-diglyceride choline (ethanolamine)-phosphotransferase in rat liver microsomes
    • Kanon H., and Ohno K. Utilization of endogenous phospholipids by the back-reaction of CDPcholine (-ethanolamine) : 1,2-diglyceride choline (ethanolamine)-phosphotransferase in rat liver microsomes. Biochim. Biophys. Acta 306 (1973) 203-217
    • (1973) Biochim. Biophys. Acta , vol.306 , pp. 203-217
    • Kanon, H.1    Ohno, K.2
  • 82
    • 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
  • 83
    • 0016666155 scopus 로고
    • Substrate-selectivity of rat liver microsomal 1,2-diacylglycerol. CDPcholine (ethanolamine) choline (ethanolamine) phosphotransferase in utilizing endogenous substrates
    • Kanoh H., and Ohno K. Substrate-selectivity of rat liver microsomal 1,2-diacylglycerol. CDPcholine (ethanolamine) choline (ethanolamine) phosphotransferase in utilizing endogenous substrates. Biochim. Biophys. Acta 380 (1975) 199-207
    • (1975) Biochim. Biophys. Acta , vol.380 , pp. 199-207
    • Kanoh, H.1    Ohno, K.2
  • 84
    • 0017062311 scopus 로고
    • Solubilization and purification of rat liver microsomal 1,2-diacylglycerol: CDPcholine cholinephosphotransferase and 1,2-diacylglycerol: CDP-ethanolamine ethanolaminephosphotransferase
    • Kanoh H., and Ohno K. Solubilization and purification of rat liver microsomal 1,2-diacylglycerol: CDPcholine 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
  • 85
    • 0023960318 scopus 로고
    • Dynamic spatial distribution of proteins in the cell
    • Kaprelyants A.S. Dynamic spatial distribution of proteins in the cell. Trends Biochem. Sci. 13 (1988) 43-46
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 43-46
    • Kaprelyants, A.S.1
  • 86
    • 0000749205 scopus 로고
    • The function of cytidine coenzyme in the biosynthesis of phospholipids
    • Kennedy E.P., and Weiss S.B. The function of cytidine coenzyme in the biosynthesis of phospholipids. J. Biol. Chem. 22 (1956) 193-214
    • (1956) J. Biol. Chem. , vol.22 , pp. 193-214
    • Kennedy, E.P.1    Weiss, S.B.2
  • 87
    • 0001697496 scopus 로고
    • Possible metabolic functions of deoxycytidine diphosphate choline and deoxycytidine diphosphate ethanolamine
    • Kennedy E.P., Borkenhagen L.F., and Smith S.W. Possible metabolic functions of deoxycytidine diphosphate choline and deoxycytidine diphosphate ethanolamine. J. Biol. Chem. 234 (1959) 1998-2000
    • (1959) J. Biol. Chem. , vol.234 , pp. 1998-2000
    • Kennedy, E.P.1    Borkenhagen, L.F.2    Smith, S.W.3
  • 88
    • 0002644373 scopus 로고
    • The biosynthesis of phospholipids
    • Opden Kamp J., Roelofcen B., and Wirtz K.W.A. (Eds), Elsevier, Amsterdam
    • Kennedy E.P. The biosynthesis of phospholipids. In: Opden Kamp J., Roelofcen B., and Wirtz K.W.A. (Eds). Lipids and Membranes. Past, Present and Future (1986), Elsevier, Amsterdam 171-206
    • (1986) Lipids and Membranes. Past, Present and Future , pp. 171-206
    • Kennedy, E.P.1
  • 89
    • 0025610139 scopus 로고
    • Regulation of phosphatidylcholine biosynthesis
    • Kent C. Regulation of phosphatidylcholine biosynthesis. Prog. Lipid Res. 29 (1990) 87-105
    • (1990) Prog. Lipid Res. , vol.29 , pp. 87-105
    • Kent, C.1
  • 90
    • 0025811395 scopus 로고
    • Regulation of eukaryotic phospholipid metabolism
    • Kent C., man G.M., Spence M.W., and Dowhan W. Regulation of eukaryotic phospholipid metabolism. FASEB J. 5 (1991) 2258-2266
    • (1991) FASEB J. , vol.5 , pp. 2258-2266
    • Kent, C.1    man, G.M.2    Spence, M.W.3    Dowhan, W.4
  • 91
    • 0027456261 scopus 로고
    • Metabolic channeling and control of the flux
    • Kholodenko B.N., and Westerhoff H.V. Metabolic channeling and control of the flux. FEBS Lett. 320 (1993) 71-74
    • (1993) FEBS Lett. , vol.320 , pp. 71-74
    • Kholodenko, B.N.1    Westerhoff, H.V.2
  • 92
    • 0024595408 scopus 로고
    • Phorbol ester stimulates the hydrolysis of phosphatidylethanolamine in leukemic HL-60, NIH 3T3, and baby hamster kidney cells
    • Kiss Z., and Anderson W.B. Phorbol ester stimulates the hydrolysis of phosphatidylethanolamine in leukemic HL-60, NIH 3T3, and baby hamster kidney cells. J. Biol. Chem. 264 (1989) 1483-1487
    • (1989) J. Biol. Chem. , vol.264 , pp. 1483-1487
    • Kiss, Z.1    Anderson, W.B.2
  • 93
    • 0025879706 scopus 로고
    • Determination of phospholipase D-mediated hydrolysis of phosphatidylethanolamine
    • Kiss Z. Determination of phospholipase D-mediated hydrolysis of phosphatidylethanolamine. Lipids 26 (1991) 321-323
    • (1991) Lipids , vol.26 , pp. 321-323
    • Kiss, Z.1
  • 94
    • 0026734615 scopus 로고
    • Differential effects of platelet-derived growth factor, serum and bombesin on phospholipase D-mediated hydrolysis of phosphatidylethanolamine in NIH 3T3 fibroblasts
    • Kiss Z. Differential effects of platelet-derived growth factor, serum and bombesin on phospholipase D-mediated hydrolysis of phosphatidylethanolamine in NIH 3T3 fibroblasts. Biochem. J. 285 (1992) 229-233
    • (1992) Biochem. J. , vol.285 , pp. 229-233
    • Kiss, Z.1
  • 95
    • 0021812768 scopus 로고
    • Amino acid transport across the human blood-CSF barrier
    • Kruse T., Reiber H., and Neuhoff V. Amino acid transport across the human blood-CSF barrier. J.Neurol. Sci. 70 (1985) 129-138
    • (1985) J.Neurol. Sci. , vol.70 , pp. 129-138
    • Kruse, T.1    Reiber, H.2    Neuhoff, V.3
  • 96
    • 0021846710 scopus 로고
    • Isolation of a somatic-cell mutant defective in phosphatidylserine biosynthesis
    • Kuge O., Nishijima M., and Akamatsu Y. Isolation of a somatic-cell mutant defective in phosphatidylserine biosynthesis. Proc. Natl. Acad. Sci. USA 82 (1985) 1926-1930
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1926-1930
    • Kuge, O.1    Nishijima, M.2    Akamatsu, Y.3
  • 97
    • 0023010680 scopus 로고
    • Phosphatidylserine biosynthesis in cultured Chinese hamster ovary cells. II. Isolation and characterization of phosphatidylserine auxotrophs
    • Kuge O., Nishijima M., and Akamatsu Y. Phosphatidylserine biosynthesis in cultured Chinese hamster ovary cells. II. Isolation and characterization of phosphatidylserine auxotrophs. J. Biol. Chem. 261 (1986) 5790-5794
    • (1986) J. Biol. Chem. , vol.261 , pp. 5790-5794
    • Kuge, O.1    Nishijima, M.2    Akamatsu, Y.3
  • 98
    • 0023038241 scopus 로고
    • Phosphatidylserine biosynthesis in cultured Chinese hamster ovary cells. III. Genetic evidence for utilization of phosphatidylcholine and phosphatidylethanolamine as precursors
    • Kuge O., Nishijima M., and Adamatsu Y. Phosphatidylserine biosynthesis in cultured Chinese hamster ovary cells. III. Genetic evidence for utilization of phosphatidylcholine and phosphatidylethanolamine as precursors. J. Biol. Chem. 261 (1986) 5795-5798
    • (1986) J. Biol. Chem. , vol.261 , pp. 5795-5798
    • Kuge, O.1    Nishijima, M.2    Adamatsu, Y.3
  • 99
    • 0026337977 scopus 로고
    • A Chinese hamster cDNA encoding a protein essential for phosphatidylserine synthase I activity
    • Kuge O., Nishijima M., and Akamatsu Y. A Chinese hamster cDNA encoding a protein essential for phosphatidylserine synthase I activity. J. Biol. Chem. 266 (1991) 24184-24189
    • (1991) J. Biol. Chem. , vol.266 , pp. 24184-24189
    • Kuge, O.1    Nishijima, M.2    Akamatsu, Y.3
  • 100
    • 0024206294 scopus 로고
    • Ethanolamine and choline transport in cultured bovine aortic endothelial cells
    • Lipton B.A., Yorek M.A., and Ginsberg B.H. Ethanolamine and choline transport in cultured bovine aortic endothelial cells. J. Cell Physiol. 137 (1988) 571-576
    • (1988) J. Cell Physiol. , vol.137 , pp. 571-576
    • Lipton, B.A.1    Yorek, M.A.2    Ginsberg, B.H.3
  • 101
    • 0025306052 scopus 로고
    • Ethanolamine metabolism in cultured bovine aortic endothelial cells
    • Lipton B.A., Davidson E.P., Ginsberg B.H., and Yorek M.A. Ethanolamine metabolism in cultured bovine aortic endothelial cells. J. Biol. Chem. 265 (1990) 7195-7201
    • (1990) J. Biol. Chem. , vol.265 , pp. 7195-7201
    • Lipton, B.A.1    Davidson, E.P.2    Ginsberg, B.H.3    Yorek, M.A.4
  • 102
    • 0027239515 scopus 로고
    • Expression of rat CTPiphosphocholine cytidylyltransferase in insect cells using a Baculovinis vector
    • Luche M.M., Rock CO., and Jackowski S. Expression of rat CTPiphosphocholine cytidylyltransferase in insect cells using a Baculovinis vector. Arch. Biochem. Biophys. 301 (1993) 114-118
    • (1993) Arch. Biochem. Biophys. , vol.301 , pp. 114-118
    • Luche, M.M.1    Rock, CO.2    Jackowski, S.3
  • 103
    • 0025809623 scopus 로고
    • Phospholipid fatty acid remodeling in mammalian cells
    • MacDonald J.I.S., and Sprecher H. Phospholipid fatty acid remodeling in mammalian cells. Biochim. Biophys. Acta 1084 (1991) 105-121
    • (1991) Biochim. Biophys. Acta , vol.1084 , pp. 105-121
    • MacDonald, J.I.S.1    Sprecher, H.2
  • 104
    • 0027473820 scopus 로고
    • Kinetic selectivity of cholinephosphotransferase in mouse liver: the Km for CDP-choline depends on diacylglycerol structure
    • Mantel C.R., Schulz 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    Schulz, A.R.2    Miyazawa, K.3    Broxmeyer, H.E.4
  • 105
    • 0026505351 scopus 로고
    • Newly imported ethanolamine is preferentially utilized for phosphatidylethanolamine biosynthesis in the hamster heart
    • McMaster C.R., and Choy P.C. Newly imported ethanolamine is preferentially utilized for phosphatidylethanolamine biosynthesis in the hamster heart. Biochim. Biophys. Acta 1124 (1992) 13-16
    • (1992) Biochim. Biophys. Acta , vol.1124 , pp. 13-16
    • McMaster, C.R.1    Choy, P.C.2
  • 106
    • 0026735997 scopus 로고
    • Serine regulates phosphatidylethanolamine biosynthesis in the hamster heart
    • McMaster C.R., and Choy P.C. Serine regulates phosphatidylethanolamine biosynthesis in the hamster heart. J. Biol. Chem. 267 (1992) 14586-14591
    • (1992) J. Biol. Chem. , vol.267 , pp. 14586-14591
    • McMaster, C.R.1    Choy, P.C.2
  • 107
    • 0026664217 scopus 로고
    • Phosphatidylethanolamine is the donor of the ethanolamine residue linking a glycosylphosphatidylinositol anchor to protein
    • Menon A.K., and Stevens V.L. Phosphatidylethanolamine is the donor of the ethanolamine residue linking a glycosylphosphatidylinositol anchor to protein. J. Biol. Chem. 267 (1992) 15277-15280
    • (1992) J. Biol. Chem. , vol.267 , pp. 15277-15280
    • Menon, A.K.1    Stevens, V.L.2
  • 108
    • 0021924986 scopus 로고
    • Rat plasma levels of amino acids and related compounds during stress
    • Milakolfsky L., Hare T.A., Miller J.M., and Vogel W.H. Rat plasma levels of amino acids and related compounds during stress. Life Sci. 36 (1985) 753-761
    • (1985) Life Sci. , vol.36 , pp. 753-761
    • Milakolfsky, L.1    Hare, T.A.2    Miller, J.M.3    Vogel, W.H.4
  • 109
    • 0023025855 scopus 로고
    • Characterization of the pathways for phosphatidylethanolamine biosynthesis in Chinese hamsters ovary mutant and parental cell lines
    • Miller M.A., and Kent C. Characterization of the pathways for phosphatidylethanolamine biosynthesis in Chinese hamsters ovary mutant and parental cell lines. J. Biol. Chem. 261 (1986) 9753-9761
    • (1986) J. Biol. Chem. , vol.261 , pp. 9753-9761
    • Miller, M.A.1    Kent, C.2
  • 110
    • 0024308391 scopus 로고
    • Localization of the membrane-associated CTP:phosphocholine cytidylyltransferase in Chinese hamster ovary cells with an altered membrane composition
    • Morand J.N., and Kent C. Localization of the membrane-associated CTP:phosphocholine cytidylyltransferase in Chinese hamster ovary cells with an altered membrane composition. J. Biol. Chem. 264 (1989) 13785-13792
    • (1989) J. Biol. Chem. , vol.264 , pp. 13785-13792
    • Morand, J.N.1    Kent, C.2
  • 111
    • 0023126563 scopus 로고
    • Preferential synthesis of diacyl and alkenylacyl ethanolamine and choline glycerophospholipids in rabbit platelet membranes
    • Morikawa S., Taniguchi S., Fujii K., Mori H., Kumada K., Fujiwara M., and Fujiwara M. Preferential synthesis of diacyl and alkenylacyl ethanolamine and choline glycerophospholipids in rabbit platelet membranes. J. Biol. Chem. 262 (1987) 1213-1217
    • (1987) J. Biol. Chem. , vol.262 , pp. 1213-1217
    • Morikawa, S.1    Taniguchi, S.2    Fujii, K.3    Mori, H.4    Kumada, K.5    Fujiwara, M.6    Fujiwara, M.7
  • 112
    • 0018144296 scopus 로고
    • Acyl chain length dependency of diacylglycerol cholinephosphotransferase and diacylglycerol ethanolaminephosphotransferase. Effect of different saturated fatty acids at the C-1 or C-2 position of diacylglycerol on solubilized rat liver microsomal enzymes
    • Morimoto K., and Kanon H. Acyl chain length dependency of diacylglycerol cholinephosphotransferase and diacylglycerol ethanolaminephosphotransferase. Effect of different saturated fatty acids at the C-1 or C-2 position of diacylglycerol on solubilized rat liver microsomal enzymes. J. Biol. Chem. 253 (1978) 5056-5060
    • (1978) J. Biol. Chem. , vol.253 , pp. 5056-5060
    • Morimoto, K.1    Kanon, H.2
  • 114
    • 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
    • O, K.-M.1    Choy, P.C.2
  • 115
    • 0027394019 scopus 로고
    • Effects of fasting on phosphatidylcholine biosynthesis in hamster liver: regulation of cholinephosphotransferase activity by endogenous argininosuccinate
    • O K.-M., and Choy P.C. Effects of fasting on phosphatidylcholine biosynthesis in hamster liver: regulation of cholinephosphotransferase activity by endogenous argininosuccinate. Biochem. J. 289 (1993) 727-733
    • (1993) Biochem. J. , vol.289 , pp. 727-733
    • O, K.-M.1    Choy, P.C.2
  • 116
    • 0021279747 scopus 로고
    • Regulation of phosphatidylcholine biosynthesis
    • Pelech S.L., and Vance D.E. Regulation of phosphatidylcholine biosynthesis. Biochim. Biophys. Acta 799 (1984) 217-251
    • (1984) Biochim. Biophys. Acta , vol.799 , pp. 217-251
    • Pelech, S.L.1    Vance, D.E.2
  • 117
    • 0019865571 scopus 로고
    • ) Isolation of somatic cell mutants defective in the biosynthesis of phosphatidylethanolamine
    • Polokoff M.A., Wing D.C., and Raetz C.H.R. ) Isolation of somatic cell mutants defective in the biosynthesis of phosphatidylethanolamine. J. Biol. Chem. 256 (1981) 7687-7690
    • (1981) J. Biol. Chem. , vol.256 , pp. 7687-7690
    • Polokoff, M.A.1    Wing, D.C.2    Raetz, C.H.R.3
  • 118
    • 0025176739 scopus 로고
    • Purification and characterization of choline/ethanolamine kinase from rat liver
    • Porter T.J., and Kent C. Purification and characterization of choline/ethanolamine kinase from rat liver. J. Biol. Chem. 265 (1990) 414-422
    • (1990) J. Biol. Chem. , vol.265 , pp. 414-422
    • Porter, T.J.1    Kent, C.2
  • 119
    • 0026562832 scopus 로고
    • Choline/ethanolamine kinase from rat liver
    • Porter T.J., and Kent C. Choline/ethanolamine kinase from rat liver. Meth. Enzymol. 209 (1992) 134-146
    • (1992) Meth. Enzymol. , vol.209 , pp. 134-146
    • Porter, T.J.1    Kent, C.2
  • 120
    • 0021365702 scopus 로고
    • Ethanolamine accumulation by photoreceptor cells of the rabbit retina
    • Pu G.A.-W., and Anderson RE. Ethanolamine accumulation by photoreceptor cells of the rabbit retina. J. Neurochem. 42 (1984) 182-191
    • (1984) J. Neurochem. , vol.42 , pp. 182-191
    • Pu, G.A.-W.1    Anderson, RE.2
  • 121
    • 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
  • 122
    • 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
  • 123
    • 85012703084 scopus 로고
    • Metabolic regulation
    • Horecker B.L., and Stadman E.R. (Eds), Academic Press, NY
    • Rolleston F.S. Metabolic regulation. In: Horecker B.L., and Stadman E.R. (Eds). Current Topics in Cellular Regulation Vol. 5 (1972), Academic Press, NY 47-75
    • (1972) Current Topics in Cellular Regulation , vol.5 , pp. 47-75
    • Rolleston, F.S.1
  • 124
    • 0025950881 scopus 로고
    • Lipid metabolism in T47D human breast cancer cells: 31P and 13C-NMR studies of choline and ethanolamine uptake
    • Ronen S.M., Rushkin E., and Degani H. Lipid metabolism in T47D human breast cancer cells: 31P and 13C-NMR studies of choline and ethanolamine uptake. Biochim. Biophys. Acta 1095 (1991) 5-16
    • (1991) Biochim. Biophys. Acta , vol.1095 , pp. 5-16
    • Ronen, S.M.1    Rushkin, E.2    Degani, H.3
  • 125
    • 0025028993 scopus 로고
    • Evidence that only newly made phosphatidylethanolamine is methylated to phosphatidylcholine and that phosphatidylethanolamine is not significantly deacylated-reacylated in rat hepatocytes
    • Samborski R.W., Ridgway N.D., and Vance D.E. Evidence that only newly made phosphatidylethanolamine is methylated to phosphatidylcholine and that phosphatidylethanolamine is not significantly deacylated-reacylated in rat hepatocytes. J. Biol. Chem. 265 (1990) 18322-18329
    • (1990) J. Biol. Chem. , vol.265 , pp. 18322-18329
    • Samborski, R.W.1    Ridgway, N.D.2    Vance, D.E.3
  • 126
    • 0024541383 scopus 로고
    • CTPphosphocholine cytidylyltransferase is a substrate for cAMP-dependent protein kinase in vitro
    • Sanghera J.S., and Vance D.E. CTPphosphocholine cytidylyltransferase is a substrate for cAMP-dependent protein kinase in vitro. J. Biol. Chem. 264 (1989) 1215-1223
    • (1989) J. Biol. Chem. , vol.264 , pp. 1215-1223
    • Sanghera, J.S.1    Vance, D.E.2
  • 127
    • 0017189668 scopus 로고
    • Selective utilization of endogenous unsaturated phosphatidylcholines and diacylglycerols by choline-phosphotransferase of mouse lung microsomes
    • Sarzala M.G., and van Golde L.M.G. Selective utilization of endogenous unsaturated phosphatidylcholines and diacylglycerols by choline-phosphotransferase of mouse lung microsomes. Biochim. Biophys. Acta 441 (1976) 423-432
    • (1976) Biochim. Biophys. Acta , vol.441 , pp. 423-432
    • Sarzala, M.G.1    van Golde, L.M.G.2
  • 128
    • 0025770064 scopus 로고
    • Remodeling of rat hepatocyte phospholipids by selective acyl turnover
    • Schmid P.C., Johnson S.B., and Schmid H.H.O. Remodeling of rat hepatocyte phospholipids by selective acyl turnover. J. Biol. Chem. 266 (1991) 13690-13697
    • (1991) J. Biol. Chem. , vol.266 , pp. 13690-13697
    • Schmid, P.C.1    Johnson, S.B.2    Schmid, H.H.O.3
  • 130
    • 0003580753 scopus 로고
    • Metabolism, regulation and function of ether-linked glycerolipids
    • Vance D.E., and Vance J.E. (Eds), Benjamin Cummings Publishing Company, Menlo Park, CA
    • Snyder F. Metabolism, regulation and function of ether-linked glycerolipids. In: Vance D.E., and Vance J.E. (Eds). Biochemistry of Lipids and Membranes (1985), Benjamin Cummings Publishing Company, Menlo Park, CA 273-295
    • (1985) Biochemistry of Lipids and Membranes , pp. 273-295
    • Snyder, F.1
  • 131
    • 0023061429 scopus 로고
    • Complexes of sequential metabolic enzymes
    • Srere P.A. Complexes of sequential metabolic enzymes. Ann. Rev. Biochem. 56 (1987) 89-124
    • (1987) Ann. Rev. Biochem. , vol.56 , pp. 89-124
    • Srere, P.A.1
  • 132
    • 0004251413 scopus 로고
    • The chemistry of phospholipids
    • Ansell G.B., Hawthorne J.N., and Dawson R.M.C. (Eds), Elsevier Scientific Publishing Company, Amsterdam
    • Strickland K.P. The chemistry of phospholipids. In: Ansell G.B., Hawthorne J.N., and Dawson R.M.C. (Eds). Form and function of Phospholipids (1973), Elsevier Scientific Publishing Company, Amsterdam 9-42
    • (1973) Form and function of Phospholipids , pp. 9-42
    • Strickland, K.P.1
  • 133
    • 0026569385 scopus 로고
    • Conversion of 1-O-alkyl^-acyl-j/i-glycero-S-phosphocholine to l-O-alk-r-enyl-2-acyl-j/i-glycero-3-phosphoethanolamine. A novel pathway for the metabolism of ether-linked phosphoglycerides
    • Strum J.C., Emilsson A., Wykle R.L., and Daniel L.W. Conversion of 1-O-alkyl^-acyl-j/i-glycero-S-phosphocholine to l-O-alk-r-enyl-2-acyl-j/i-glycero-3-phosphoethanolamine. A novel pathway for the metabolism of ether-linked phosphoglycerides. J. Biol. Chem. 267 (1992) 1576-1583
    • (1992) J. Biol. Chem. , vol.267 , pp. 1576-1583
    • Strum, J.C.1    Emilsson, A.2    Wykle, R.L.3    Daniel, L.W.4
  • 134
    • 0015934641 scopus 로고
    • Biosynthesis of rat liver phosphatidylethanolamines from intraportally injected ethanolamine
    • Sundler R. Biosynthesis of rat liver phosphatidylethanolamines from intraportally injected ethanolamine. Biochim. Biophys. Acta 306 (1973) 218-226
    • (1973) Biochim. Biophys. Acta , vol.306 , pp. 218-226
    • Sundler, R.1
  • 135
    • 0016188231 scopus 로고
    • Quantitative role of base exchange in phosphatidylethanolamine synthesis in isolated rat hepatocytes
    • Sundler R., Akesson B., and Nilsson A. Quantitative role of base exchange in phosphatidylethanolamine synthesis in isolated rat hepatocytes. FEBS Lett. 43 (1974) 303-307
    • (1974) FEBS Lett. , vol.43 , pp. 303-307
    • Sundler, R.1    Akesson, B.2    Nilsson, A.3
  • 136
    • 0015968108 scopus 로고
    • Sources of diacylglycerols for phospholipid synthesis in rat liver
    • Sundler R., Akesson B., and Nilsson A. Sources of diacylglycerols for phospholipid synthesis in rat liver. Biochim. Biophys. Acta 337 (1974) 248-254
    • (1974) Biochim. Biophys. Acta , vol.337 , pp. 248-254
    • Sundler, R.1    Akesson, B.2    Nilsson, A.3
  • 137
    • 0016753096 scopus 로고
    • Ethanolaminephosphate cytidylyltransferase. Purification and characterization of the enzyme from rat liver
    • Sundler R. Ethanolaminephosphate cytidylyltransferase. Purification and characterization of the enzyme from rat liver. J. Biol. Chem. 250 (1975) 8585-8590
    • (1975) J. Biol. Chem. , vol.250 , pp. 8585-8590
    • Sundler, R.1
  • 138
    • 0016609166 scopus 로고
    • Biosynthesis of phosphatidylethanolamines and phosphatidylcholines from ethanolamine and choline in rat liver
    • Sundler R., and Akesson B. Biosynthesis of phosphatidylethanolamines and phosphatidylcholines from ethanolamine and choline in rat liver. Biochem. J. 146 (1975) 309-315
    • (1975) Biochem. J. , vol.146 , pp. 309-315
    • Sundler, R.1    Akesson, B.2
  • 139
    • 0016761879 scopus 로고
    • Regulation of phospholipid biosynthesis in isolated rat hepatocytes. Effect of different substrates
    • Sundler R., and Akesson B. Regulation of phospholipid biosynthesis in isolated rat hepatocytes. Effect of different substrates. J. Biol. Chem. 250 (1975) 3359-3367
    • (1975) J. Biol. Chem. , vol.250 , pp. 3359-3367
    • Sundler, R.1    Akesson, B.2
  • 140
    • 0021962054 scopus 로고
    • Purification and properties of an ethanolamine-serine base exchange enzyme of rat brain membranes
    • Suzuki T.T., and Kanfer J.N. Purification and properties of an ethanolamine-serine base exchange enzyme of rat brain membranes. J. Biol. Chem. 260 (1985) 1394-1399
    • (1985) J. Biol. Chem. , vol.260 , pp. 1394-1399
    • Suzuki, T.T.1    Kanfer, J.N.2
  • 141
    • 0021829480 scopus 로고
    • Evidence for the existence of isoenzymes of choline kinase and their selective induction in 3-methylcholanthrene-or carbon tetrachloride-treated rat liver
    • Tadokoro K., Ishidate K., and Nakazawa Y. Evidence for the existence of isoenzymes of choline kinase and their selective induction in 3-methylcholanthrene-or carbon tetrachloride-treated rat liver. Biochim. Biophys. Acta 835 (1985) 501-513
    • (1985) Biochim. Biophys. Acta , vol.835 , pp. 501-513
    • Tadokoro, K.1    Ishidate, K.2    Nakazawa, Y.3
  • 142
    • 0025772016 scopus 로고
    • Cytidylyltransferase translocation onto endoplasmic reticulum and increased de novo synthesis without phosphatidylcholine accumulation in Krebs-II ascite cells
    • Tercé F., Record M., Tronchère H., Ribbes G., and Chap H. Cytidylyltransferase translocation onto endoplasmic reticulum and increased de novo synthesis without phosphatidylcholine accumulation in Krebs-II ascite cells. Biochim. Biophys. Acta 1084 (1991) 69-77
    • (1991) Biochim. Biophys. Acta , vol.1084 , pp. 69-77
    • Tercé, F.1    Record, M.2    Tronchère, H.3    Ribbes, G.4    Chap, H.5
  • 143
    • 0023510852 scopus 로고
    • Stimulation of phosphatidylethanolamine synthesis in isolated rat hepatocytes by phorbol 12-myristate 13-acetate
    • Tijburg L.B.M., Houweling M., Geelen M.J.H., and Van Golde L.M.G. Stimulation of phosphatidylethanolamine synthesis in isolated rat hepatocytes by phorbol 12-myristate 13-acetate. Biochim. Biophys. Acta 922 (1987) 184-190
    • (1987) Biochim. Biophys. Acta , vol.922 , pp. 184-190
    • Tijburg, L.B.M.1    Houweling, M.2    Geelen, M.J.H.3    Van Golde, L.M.G.4
  • 144
    • 0023177248 scopus 로고
    • Effects of vasopressin on the synthesis of phosphatidylethanolamines and phosphatidylcholines by isolated rat hepatocytes
    • Tijburg L.B.M., Schuurmans E.A.J.M., Geelen M.J.H., and van Golde L.M.G. Effects of vasopressin on the synthesis of phosphatidylethanolamines and phosphatidylcholines by isolated rat hepatocytes. Biochim. Biophys. Acta 919 (1987) 49-57
    • (1987) Biochim. Biophys. Acta , vol.919 , pp. 49-57
    • Tijburg, L.B.M.1    Schuurmans, E.A.J.M.2    Geelen, M.J.H.3    van Golde, L.M.G.4
  • 145
    • 0023865179 scopus 로고
    • Effects of dietary conditions on the pool sizes of precursors of phosphatidylcholine and phosphatidylethanolamine synthesis in rat liver
    • Tijburg L.B.M., Houweling M., Geelen M.J.H., and van Golde L.M.G. Effects of dietary conditions on the pool sizes of precursors of phosphatidylcholine and phosphatidylethanolamine synthesis in rat liver. Biochim. Biophys. Acta 959 (1988) 1-8
    • (1988) Biochim. Biophys. Acta , vol.959 , pp. 1-8
    • Tijburg, L.B.M.1    Houweling, M.2    Geelen, M.J.H.3    van Golde, L.M.G.4
  • 146
    • 0024312193 scopus 로고
    • Regulation of the biosynthesis of triacylglycerol, phosphatidylcholine and phosphatidylethanolamine in the liver
    • Tijburg L.B.M., Geelen M.J.H., and Van Golde L.M.G. Regulation of the biosynthesis of triacylglycerol, phosphatidylcholine and phosphatidylethanolamine in the liver. Biochim. Biophys. Acta 1004 (1989) 1-19
    • (1989) Biochim. Biophys. Acta , vol.1004 , pp. 1-19
    • Tijburg, L.B.M.1    Geelen, M.J.H.2    Van Golde, L.M.G.3
  • 147
    • 0024401051 scopus 로고
    • Biosynthesis of phosphatidylethanolamine via the CDP-ethanolamine route is an important pathway in isolated rat hepatocytes
    • Tijburg L.B.M., Geelen M.J.H., and Van Golde L.M.G. Biosynthesis of phosphatidylethanolamine via the CDP-ethanolamine route is an important pathway in isolated rat hepatocytes. Biochem. Res. Commun. 160 (1989) 1275-1280
    • (1989) Biochem. Res. Commun. , vol.160 , pp. 1275-1280
    • Tijburg, L.B.M.1    Geelen, M.J.H.2    Van Golde, L.M.G.3
  • 148
    • 0024546179 scopus 로고
    • Inhibition of phosphatidylethanolamine synthesis by glucagon in isolated rat hepatocytes
    • Tijburg L.B.M., Houweling M., Geelen M.J.H., and van Golde L.M.G. Inhibition of phosphatidylethanolamine synthesis by glucagon in isolated rat hepatocytes. Biochem. J. 257 (1989) 645-650
    • (1989) Biochem. J. , vol.257 , pp. 645-650
    • Tijburg, L.B.M.1    Houweling, M.2    Geelen, M.J.H.3    van Golde, L.M.G.4
  • 150
    • 0025374005 scopus 로고
    • Purification and properties of choline kinase from rat brain
    • Uchida T., and Yamashita S. Purification and properties of choline kinase from rat brain. Biochim. Biophys. Acta 1043 (1990) 281-288
    • (1990) Biochim. Biophys. Acta , vol.1043 , pp. 281-288
    • Uchida, T.1    Yamashita, S.2
  • 151
    • 0026519854 scopus 로고
    • Choline/ethanolamine kinase from rat brain
    • Uchida T., and Yamashita S. Choline/ethanolamine kinase from rat brain. Meth. Enzymol. 209 (1992) 147-153
    • (1992) Meth. Enzymol. , vol.209 , pp. 147-153
    • Uchida, T.1    Yamashita, S.2
  • 152
    • 0026699655 scopus 로고
    • Molecular cloning, characterization, and expression in Escherichia coli of a cDNA encoding mammalian choline kinase
    • Uchida T., and Yamashita S. Molecular cloning, characterization, and expression in Escherichia coli of a cDNA encoding mammalian choline kinase. J. Biol. Chem. 267 (1992) 10156-10162
    • (1992) J. Biol. Chem. , vol.267 , pp. 10156-10162
    • Uchida, T.1    Yamashita, S.2
  • 153
    • 0018216639 scopus 로고
    • Evidence for the existence of a single enzyme catalyzing the phosphorylation of choline and ethanolamine in primate lung
    • Ulane R.E., Stephenson L.L., and Farrell P.M. Evidence for the existence of a single enzyme catalyzing the phosphorylation of choline and ethanolamine in primate lung. Biochim. Biophys. Acta 531 (1978) 295-300
    • (1978) Biochim. Biophys. Acta , vol.531 , pp. 295-300
    • Ulane, R.E.1    Stephenson, L.L.2    Farrell, P.M.3
  • 154
    • 77957063003 scopus 로고
    • The copcholine pathway: choline kinase
    • Lung Development. Farrell P.M. (Ed), Academic Press, NY
    • Ulane R.E. The copcholine pathway: choline kinase. In: Farrell P.M. (Ed). Lung Development. Biological and Clinical Perspectives Vol. 1 (1982), Academic Press, NY 295-316
    • (1982) Biological and Clinical Perspectives , vol.1 , pp. 295-316
    • Ulane, R.E.1
  • 156
    • 0000754782 scopus 로고
    • Regulatory and functional aspects of phosphatidylcholine metabolism
    • Vance D.E. (Ed), CRC Press Inc., Boca Raton, FL
    • Vance D.E. Regulatory and functional aspects of phosphatidylcholine metabolism. In: Vance D.E. (Ed). Phosphatidylcholine Metabolism (1989), CRC Press Inc., Boca Raton, FL 225-239
    • (1989) Phosphatidylcholine Metabolism , pp. 225-239
    • Vance, D.E.1
  • 157
    • 0010585602 scopus 로고
    • CTP: cholinephosphate cytidylyltransferase
    • Vance D.E. (Ed), CRC Press Inc., Boca Raton, FL
    • Vance D.E. CTP: cholinephosphate cytidylyltransferase. In: Vance D.E. (Ed). Phosphatidylcholine Metabolism (1989), CRC Press Inc., Boca Raton, FL 33-45
    • (1989) Phosphatidylcholine Metabolism , pp. 33-45
    • Vance, D.E.1
  • 158
    • 0023002227 scopus 로고
    • Specific pools of phospholipids are used for lipoprotein secretion by cultured rat hepatocytes
    • Vance J.E., and Vance D.E. Specific pools of phospholipids are used for lipoprotein secretion by cultured rat hepatocytes. J. Biol. Chem. 261 (1986) 486-4491
    • (1986) J. Biol. Chem. , vol.261 , pp. 486-4491
    • Vance, J.E.1    Vance, D.E.2
  • 159
    • 0023760638 scopus 로고
    • Compartmentalization of phospholipids for lipoprotein assembly on the basis of molecular species and biosynthetic origin
    • Vance J.E. Compartmentalization of phospholipids for lipoprotein assembly on the basis of molecular species and biosynthetic origin. Biochim. Biophys. Acta 963 (1988) 70-81
    • (1988) Biochim. Biophys. Acta , vol.963 , pp. 70-81
    • Vance, J.E.1
  • 160
    • 0023903699 scopus 로고
    • Does rat liver Golgi have the capacity to synthesize phospholipids for lipoprotein secretion?
    • Vance J.E., and Vance D.E. Does rat liver Golgi have the capacity to synthesize phospholipids for lipoprotein secretion?. J. Biol. Chem. 263 (1988) 5898-5909
    • (1988) J. Biol. Chem. , vol.263 , pp. 5898-5909
    • Vance, J.E.1    Vance, D.E.2
  • 161
    • 0025273937 scopus 로고
    • Phospholipid synthesis in a membrane fraction associated with mitochondria
    • Vance J.E. Phospholipid synthesis in a membrane fraction associated with mitochondria. J. Biol. Chem. 265 (1990) 7248-7256
    • (1990) J. Biol. Chem. , vol.265 , pp. 7248-7256
    • Vance, J.E.1
  • 162
    • 0026088027 scopus 로고
    • Newly made phosphatidylserine and phosphatidylethanolmaine are preferentially translocated between rat liver and endoplasmic reticulum
    • Vance J.E. Newly made phosphatidylserine and phosphatidylethanolmaine are preferentially translocated between rat liver and endoplasmic reticulum. J. Biol. Chem. 266 (1991) 89-97
    • (1991) J. Biol. Chem. , vol.266 , pp. 89-97
    • Vance, J.E.1
  • 163
    • 0016016381 scopus 로고
    • Phosphoglyceride metabolism
    • Van den Bosch H. Phosphoglyceride metabolism. Ann. Rev. Biochem. 43 (1974) 243-277
    • (1974) Ann. Rev. Biochem. , vol.43 , pp. 243-277
    • Van den Bosch, H.1
  • 164
    • 0015221229 scopus 로고
    • Some studies on the metabolism of phospholipids in Golgi complex from bovine and rat liver in comparison to other subcellular fractions
    • Van Golde L.M.G., Fleischer B., and Fleischer S. Some studies on the metabolism of phospholipids in Golgi complex from bovine and rat liver in comparison to other subcellular fractions. Biochim. Biophys. Acta 249 (1971) 318-330
    • (1971) Biochim. Biophys. Acta , vol.249 , pp. 318-330
    • Van Golde, L.M.G.1    Fleischer, B.2    Fleischer, S.3
  • 167
    • 0027468258 scopus 로고
    • Immunological characterization, lipid dependence, and subcellular localization of CTP:phosphoethanolamine cytidylyltransferase purified from rat liver. Comparison with CTP:phoshocholine cytidylyltransferase
    • Vermeulen P.S., Tijburg L.B.M., Geelen M.J.H., and Van Golde L.M.G. Immunological characterization, lipid dependence, and subcellular localization of CTP:phosphoethanolamine cytidylyltransferase purified from rat liver. Comparison with CTP:phoshocholine cytidylyltransferase. J. Biol. Chem. 268 (1993) 7458-7464
    • (1993) J. Biol. Chem. , vol.268 , pp. 7458-7464
    • Vermeulen, P.S.1    Tijburg, L.B.M.2    Geelen, M.J.H.3    Van Golde, L.M.G.4
  • 168
    • 0028293429 scopus 로고
    • Substrate specificity of CTP: phosphoethanolamine cytidylyltransferase purified from rat liver
    • Vermeulen P.S., Geelen M.J.H., and Van Golde L.M.G. Substrate specificity of CTP: phosphoethanolamine cytidylyltransferase purified from rat liver. Biochim. Biophys. Acta 1211 (1994) 343-349
    • (1994) Biochim. Biophys. Acta , vol.1211 , pp. 343-349
    • Vermeulen, P.S.1    Geelen, M.J.H.2    Van Golde, L.M.G.3
  • 169
    • 0002845059 scopus 로고
    • Phosphatidylserine functions as the major precursor of phosphatidylethanolamine in cultured BHK-21 cells
    • Voelker D.R. Phosphatidylserine functions as the major precursor of phosphatidylethanolamine in cultured BHK-21 cells. Proc. Natl. Acad. Sci. USA 81 (1984) 2669-2673
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 2669-2673
    • Voelker, D.R.1
  • 170
    • 0022346103 scopus 로고
    • Disruption of phosphatidylserine translocation to the mitochondria in baby hamster kindey cells
    • Voelker D.R. Disruption of phosphatidylserine translocation to the mitochondria in baby hamster kindey cells. J. Biol. Chem. 260 (1985) 14671-14676
    • (1985) J. Biol. Chem. , vol.260 , pp. 14671-14676
    • Voelker, D.R.1
  • 171
    • 0022636810 scopus 로고
    • Isolation and characterization of a Chinese hamster ovary cell line requiring ethanolamine or phosphatidylserine for growth and exhibiting defective phosphatidylserine synthase activity
    • Voelker D.R., and Frazier J.L. Isolation and characterization of a Chinese hamster ovary cell line requiring ethanolamine or phosphatidylserine for growth and exhibiting defective phosphatidylserine synthase activity. J. Biol. Chem. 261 (1986) 1002-1008
    • (1986) J. Biol. Chem. , vol.261 , pp. 1002-1008
    • Voelker, D.R.1    Frazier, J.L.2
  • 172
    • 0024321167 scopus 로고
    • Reconstitution of phosphatidylserine import into rat liver mitochondria
    • Voelker D.R. Reconstitution of phosphatidylserine import into rat liver mitochondria. J. Biol. Chem. 264 (1989) 8019-8025
    • (1989) J. Biol. Chem. , vol.264 , pp. 8019-8025
    • Voelker, D.R.1
  • 173
    • 0025746264 scopus 로고
    • Organelle biogenesis and intracellular lipid transport in eukaryotes
    • Voelker D.R. Organelle biogenesis and intracellular lipid transport in eukaryotes. Microbiol. Revs. 55 (1991) 543-560
    • (1991) Microbiol. Revs. , vol.55 , pp. 543-560
    • Voelker, D.R.1
  • 174
    • 0027405015 scopus 로고
    • The ATP-dependent translocation of phosphatidylserine to the mitochondria is a process that is restricted tot the autologous organelle
    • Voelker D.R. The ATP-dependent translocation of phosphatidylserine to the mitochondria is a process that is restricted tot the autologous organelle. J. Biol. Chem. 268 (1993) 7069-7074
    • (1993) J. Biol. Chem. , vol.268 , pp. 7069-7074
    • Voelker, D.R.1
  • 175
    • 0027415175 scopus 로고
    • Nuclear localization of soluble CTP:phosphocholine cytidylyltransferase
    • Wang Y., Sweitzer T.D., Weinhold P.A., and Kent C. Nuclear localization of soluble CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 268 (1993) 5899-5904
    • (1993) J. Biol. Chem. , vol.268 , pp. 5899-5904
    • Wang, Y.1    Sweitzer, T.D.2    Weinhold, P.A.3    Kent, C.4
  • 176
    • 0025088522 scopus 로고
    • Phosphorylation of CTP:phosphocholine cytidylyltransferase in vivo. Lack of effect of phorbol ester treatment in HeLa cells
    • Watkins J.D., and Kent C. Phosphorylation of CTP:phosphocholine cytidylyltransferase in vivo. Lack of effect of phorbol ester treatment in HeLa cells. J. Biol. Chem. 265 (1990) 2190-2197
    • (1990) J. Biol. Chem. , vol.265 , pp. 2190-2197
    • Watkins, J.D.1    Kent, C.2
  • 177
    • 0026713830 scopus 로고
    • Immunolocalization of membrane-associated CTP:phosphocholine cytidylyltransferase in phosphatidylcholine-deficient Chinese Hamster Ovary cells
    • Watkins J.D., and Kent C. Immunolocalization of membrane-associated CTP:phosphocholine cytidylyltransferase in phosphatidylcholine-deficient Chinese Hamster Ovary cells. J. Biol. Chem. 267 (1992) 5886-5892
    • (1992) J. Biol. Chem. , vol.267 , pp. 5886-5892
    • Watkins, J.D.1    Kent, C.2
  • 178
    • 0016261353 scopus 로고
    • Separation, purification, and characterization of ethanolamine kinase and choline kinase from rat liver
    • Weinhold P.A., and Rethy V.B. Separation, purification, and characterization of ethanolamine kinase and choline kinase from rat liver. Biochemistry 13 (1974) 5135-5141
    • (1974) Biochemistry , vol.13 , pp. 5135-5141
    • Weinhold, P.A.1    Rethy, V.B.2
  • 179
    • 0022972322 scopus 로고
    • The purification and characterization of CTP:phosphorylcholine cytidylyltransferase from rat liver
    • Weinhold P.A., Rounsifer M.E., and Feldman D.A. The purification and characterization of CTP:phosphorylcholine cytidylyltransferase from rat liver. J. Biol. Chem. 261 (1986) 5104-5110
    • (1986) J. Biol. Chem. , vol.261 , pp. 5104-5110
    • Weinhold, P.A.1    Rounsifer, M.E.2    Feldman, D.A.3
  • 180
    • 0024792275 scopus 로고
    • Characterization of cytosolic forms of CTP:choline-phosphate cytidylyltransferase in lung, isolated alveolar type II cells, A549 cell and Hep G2 cells
    • Weinhold P.A., Rounsifer M.E., Charles L., and Feldman D.A. Characterization of cytosolic forms of CTP:choline-phosphate cytidylyltransferase in lung, isolated alveolar type II cells, A549 cell and Hep G2 cells. Biochim. Biophys. Acta 1006 (1989) 299-310
    • (1989) Biochim. Biophys. Acta , vol.1006 , pp. 299-310
    • Weinhold, P.A.1    Rounsifer, M.E.2    Charles, L.3    Feldman, D.A.4
  • 181
    • 0026590767 scopus 로고
    • Choline-phosphate cytidylyltransferase
    • Weinhold P.A., and Feldman D.A. Choline-phosphate cytidylyltransferase. Meth. Enzymol. 209 (1992) 248-258
    • (1992) Meth. Enzymol. , vol.209 , pp. 248-258
    • Weinhold, P.A.1    Feldman, D.A.2
  • 182
    • 0001363220 scopus 로고
    • The phospholipid composition of mammalian tissues
    • Ansell G.B., Hawthorne J.N., and Dawson R.M.C. (Eds), Elsevier Scientific Publishing Company, Amsterdam
    • White D.A. The phospholipid composition of mammalian tissues. In: Ansell G.B., Hawthorne J.N., and Dawson R.M.C. (Eds). Form and Function of Phospholipids (1973), Elsevier Scientific Publishing Company, Amsterdam 441-482
    • (1973) Form and Function of Phospholipids , pp. 441-482
    • White, D.A.1
  • 183
    • 0025815183 scopus 로고
    • Serine utilization as a precursor of phosphatidylserine and alkenyl-(plasmenyl) -, alkyl-, and acylethanolamine phosphoglycerides in cultured glioma cells
    • Xu Z., Byers D.M., Palmer F.B.St.C., Spence M.W., and Cook H.W. Serine utilization as a precursor of phosphatidylserine and alkenyl-(plasmenyl) -, alkyl-, and acylethanolamine phosphoglycerides in cultured glioma cells. J. Biol. Chem. 266 (1991) 2143-2150
    • (1991) J. Biol. Chem. , vol.266 , pp. 2143-2150
    • Xu, Z.1    Byers, D.M.2    Palmer, F.B.St.C.3    Spence, M.W.4    Cook, H.W.5
  • 184
    • 0027243530 scopus 로고
    • Limited metabolic interaction of serine with ethanolamine and choline in the turnover of phosphatidylserine, phosphatidylethanolamine and plasmalogens in cultured glioma cells
    • Xu Z., Byers D.M., Palmer F.B.St.C., Spence M.W., and Cook H.W. Limited metabolic interaction of serine with ethanolamine and choline in the turnover of phosphatidylserine, phosphatidylethanolamine and plasmalogens in cultured glioma cells. Biochim. Biophys. Acta 1168 (1993) 167-174
    • (1993) Biochim. Biophys. Acta , vol.1168 , pp. 167-174
    • Xu, Z.1    Byers, D.M.2    Palmer, F.B.St.C.3    Spence, M.W.4    Cook, H.W.5
  • 185
    • 0021999402 scopus 로고
    • The utilization of ethanolamine and serine for ethanolamine phosphoglycerine synthesis by human Y79 retinoblastoma cells
    • Yorek M.A., Rosario R.T., Dudley D.T., and Spector A.A. The utilization of ethanolamine and serine for ethanolamine phosphoglycerine synthesis by human Y79 retinoblastoma cells. J. Biol. Chem. 260 (1985) 2930-2936
    • (1985) J. Biol. Chem. , vol.260 , pp. 2930-2936
    • Yorek, M.A.1    Rosario, R.T.2    Dudley, D.T.3    Spector, A.A.4
  • 186
    • 0022916580 scopus 로고
    • Effect of ethanolamine on choline uptake and incorporation into phosphatidylcholine in human Y79 retinoblastoma cells
    • Yorek M.A., Dunlap J.A., Spector A.A., and Ginsberg B.H. Effect of ethanolamine on choline uptake and incorporation into phosphatidylcholine in human Y79 retinoblastoma cells. J. Lipid Res. 27 (1986) 1205-1213
    • (1986) J. Lipid Res. , vol.27 , pp. 1205-1213
    • Yorek, M.A.1    Dunlap, J.A.2    Spector, A.A.3    Ginsberg, B.H.4
  • 187
    • 0027179487 scopus 로고
    • Phospholipids in animal eukaryotic membranes: Transverse asymmetry and movement
    • Zachowski A. Phospholipids in animal eukaryotic membranes: Transverse asymmetry and movement. Biochem. J. 294 (1993) 1-14
    • (1993) Biochem. J. , vol.294 , pp. 1-14
    • Zachowski, A.1
  • 188
    • 0019256772 scopus 로고
    • Phosphatidylcholine biosynthesis in isolated hamster heart
    • Zelinski T.A., Savard J.D., Man R.Y.K., and Choy P.C. Phosphatidylcholine biosynthesis in isolated hamster heart. J. Biol. Chem. 255 (1980) 11423-11428
    • (1980) J. Biol. Chem. , vol.255 , pp. 11423-11428
    • Zelinski, T.A.1    Savard, J.D.2    Man, R.Y.K.3    Choy, P.C.4
  • 189
    • 0020442447 scopus 로고
    • Phosphatidylethanolamine biosynthesis in isolated hamster heart
    • Zelinski T.A., and Choy P.C. Phosphatidylethanolamine biosynthesis in isolated hamster heart. Can. J. Biochem. 60 (1982) 817-823
    • (1982) Can. J. Biochem. , vol.60 , pp. 817-823
    • Zelinski, T.A.1    Choy, P.C.2
  • 190
    • 0020456349 scopus 로고
    • Choline regulates phosphatidylethanolamine biosynthesis in isolated hamster heart
    • Zelinski T.A., and Choy P.C. Choline regulates phosphatidylethanolamine biosynthesis in isolated hamster heart. J. Biol. Chem. 257 (1982) 13201-13204
    • (1982) J. Biol. Chem. , vol.257 , pp. 13201-13204
    • Zelinski, T.A.1    Choy, P.C.2
  • 191
    • 0028140110 scopus 로고
    • Cyclic AMP-dependent protein kinase does not regulate CTP:phosphocholine cytidylyltransferase activity in maturing type II cells
    • Zimmerman L.J., Lee W.-S., Smith B.T., and Post M. Cyclic AMP-dependent protein kinase does not regulate CTP:phosphocholine cytidylyltransferase activity in maturing type II cells. Biochim. Biophys. Acta 1211 (1994) 44-50
    • (1994) Biochim. Biophys. Acta , vol.1211 , pp. 44-50
    • Zimmerman, L.J.1    Lee, W.-S.2    Smith, B.T.3    Post, M.4


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