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Volumn 1393, Issue 1, 1998, Pages 90-98

Activation of CTP: Phosphocholine cytidylyltransferase by hypochlorite-oxidized phosphatidylcholines

Author keywords

Cytidylyltransferase; Oxidized phospholipid; Phosphatidylcholine metabolism; Response to oxidative stress

Indexed keywords

CHOLINE PHOSPHATE CYTIDYLYLTRANSFERASE; PHOSPHATIDYLCHOLINE;

EID: 0032584548     PISSN: 00052760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2760(98)00060-5     Document Type: Article
Times cited : (12)

References (48)
  • 2
    • 0020065662 scopus 로고
    • Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides
    • Ursini F., Maiorino M., Valente M., Ferri L., Gregolin C. Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides. Biochim. Biophys. Acta. 710:1982;197-211.
    • (1982) Biochim. Biophys. Acta , vol.710 , pp. 197-211
    • Ursini, F.1    Maiorino, M.2    Valente, M.3    Ferri, L.4    Gregolin, C.5
  • 3
    • 0025610139 scopus 로고
    • Regulation of phosphatidylcholine biosynthesis (Review)
    • Kent C. Regulation of phosphatidylcholine biosynthesis (Review). Prog. Lipid Res. 29:1990;87-105.
    • (1990) Prog. Lipid Res. , vol.29 , pp. 87-105
    • Kent, C.1
  • 4
    • 0002310935 scopus 로고    scopus 로고
    • Regulation of mammalian CTP:phosphocholine cytidylyltransferase (Review)
    • Cornell R.B. Regulation of mammalian CTP:phosphocholine cytidylyltransferase (Review). Adv. Lipobiol. 1A:1996;1-38.
    • (1996) Adv. Lipobiol. , vol.1 , pp. 1-38
    • Cornell, R.B.1
  • 5
    • 0028302144 scopus 로고
    • Phosphatidylcholine cycle and regulation of phosphatidylcholine biosynthesis by enzyme translocation (Review)
    • Tronchere H., Record M., Terce F., Chap H. Phosphatidylcholine cycle and regulation of phosphatidylcholine biosynthesis by enzyme translocation (Review). 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
  • 6
    • 0029745175 scopus 로고    scopus 로고
    • Lipid regulation of CTP:phosphocholine cytidylyltransferase: Electrostatic, hydrophobic, and synergistic interactions of anionic phospholipids and diacylglycerol
    • Arnold R.S., Cornell R.B. Lipid regulation of CTP:phosphocholine cytidylyltransferase: electrostatic, hydrophobic, and synergistic interactions of anionic phospholipids and diacylglycerol. Biochemistry. 35:1996;9917-9924.
    • (1996) Biochemistry , vol.35 , pp. 9917-9924
    • Arnold, R.S.1    Cornell, R.B.2
  • 7
    • 0028067154 scopus 로고
    • Identification of the membrane-binding domain of rat liver CTP:phosphocholine cytidylyltransferase using chymotrypsin proteolysis
    • Craig L., Johnson J.E., Cornell R.B. Identification of the membrane-binding domain of rat liver CTP:phosphocholine cytidylyltransferase using chymotrypsin proteolysis. J. Biol. Chem. 269:1994;3311-3317.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3311-3317
    • Craig, L.1    Johnson, J.E.2    Cornell, R.B.3
  • 9
    • 0029833954 scopus 로고    scopus 로고
    • Structure of the membrane binding domain of CTP:phosphocholine cytidylyltransferase
    • Dunne S.J., Cornell R.B., Johnson J.E., Glover N.R., Tracey A.S. Structure of the membrane binding domain of CTP:phosphocholine cytidylyltransferase. Biochemistry. 35:1996;11975-11989.
    • (1996) Biochemistry , vol.35 , pp. 11975-11989
    • Dunne, S.J.1    Cornell, R.B.2    Johnson, J.E.3    Glover, N.R.4    Tracey, A.S.5
  • 10
    • 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
  • 13
    • 0020702109 scopus 로고
    • Assessment of chlorination by human neutrophils
    • Foote C.S., Goyne T.E., Lehrer R.I. Assessment of chlorination by human neutrophils. Nature. 301:1983;715-716.
    • (1983) Nature , vol.301 , pp. 715-716
    • Foote, C.S.1    Goyne, T.E.2    Lehrer, R.I.3
  • 16
    • 8544251150 scopus 로고
    • The acid ionization constant of HOCl from 5 to 35°
    • Morris J.C. The acid ionization constant of HOCl from 5 to 35° J. Phys. Chem. 70:1966;3798-3805.
    • (1966) J. Phys. Chem. , vol.70 , pp. 3798-3805
    • Morris, J.C.1
  • 17
    • 33845261493 scopus 로고
    • A rapid method for total lipid extraction and purification
    • Bligh E.G., Dyer W.J. A rapid method for total lipid extraction and purification. Can. J. Physiol. 57:1959;911-917.
    • (1959) Can. J. Physiol. , vol.57 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 18
    • 0021288839 scopus 로고
    • Spectrophotometric determination of lipid conjugated dienes
    • Recknagel R.O., Glende E.A. Jr. Spectrophotometric determination of lipid conjugated dienes. Methods Enzymol. 105:1984;331-337.
    • (1984) Methods Enzymol. , vol.105 , pp. 331-337
    • Recknagel, R.O.1    Glende E.A., Jr.2
  • 19
    • 0020604097 scopus 로고
    • Bile salt-dependent oxygenation of polyunsaturated phosphocholines by soybean lipoxygenase-1
    • Eskola J., Laakso S. Bile salt-dependent oxygenation of polyunsaturated phosphocholines by soybean lipoxygenase-1. Biochim. Biophys. Acta. 751:1983;305-311.
    • (1983) Biochim. Biophys. Acta , vol.751 , pp. 305-311
    • Eskola, J.1    Laakso, S.2
  • 20
    • 0027550461 scopus 로고
    • Baculovirus-mediated expression of rat liver CTP:phosphocholine cytidylyltransferase
    • MacDonald J.I.S., Kent C. Baculovirus-mediated expression of rat liver CTP:phosphocholine cytidylyltransferase. Protein Expression Purif. 4:1993;1-7.
    • (1993) Protein Expression Purif. , vol.4 , pp. 1-7
    • MacDonald, J.I.S.1    Kent, C.2
  • 21
    • 0029074898 scopus 로고
    • Functions of the C-terminal domain of CTP:phosphocholine cytidylyltransferase. Effects of C-terminal deletions on enzyme activity, intracellular localization and phosphorylation potential
    • Cornell R.B., Kalmar G.B., Kay R.J., Johnson M.A., Sanghera J.S., Pelech S.L. Functions of the C-terminal domain of CTP:phosphocholine cytidylyltransferase. Effects of C-terminal deletions on enzyme activity, intracellular localization and phosphorylation potential. Biochem. J. 310:1995;699-708.
    • (1995) Biochem. J. , vol.310 , pp. 699-708
    • Cornell, R.B.1    Kalmar, G.B.2    Kay, R.J.3    Johnson, M.A.4    Sanghera, J.S.5    Pelech, S.L.6
  • 22
    • 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
  • 23
    • 0025334244 scopus 로고
    • Sphingosine inhibits the activity of rat liver CTP:phosphocholine cytidylyltransferase
    • Sohal P.S., Cornell R.B. Sphingosine inhibits the activity of rat liver CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 265:1990;11746-11750.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11746-11750
    • Sohal, P.S.1    Cornell, R.B.2
  • 24
    • 33947440127 scopus 로고
    • Structure and absorption spectra of α,β-unsaturated ketones
    • Woodward R.B. Structure and absorption spectra of α,β-unsaturated ketones. J. Am. Chem. Soc. 63:1941;1123-1126.
    • (1941) J. Am. Chem. Soc. , vol.63 , pp. 1123-1126
    • Woodward, R.B.1
  • 25
    • 0014027843 scopus 로고
    • The role of phospholipids in stimulating phosphorylcholine cytidylyltransferase activity
    • Fiscus W.G., Schneider W.C. The role of phospholipids in stimulating phosphorylcholine cytidylyltransferase activity. J. Biol. Chem. 241:1966;3324-3330.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3324-3330
    • Fiscus, W.G.1    Schneider, W.C.2
  • 26
    • 0028339581 scopus 로고
    • Susceptibility of rat retina acyl-CoA: 1-acyl-sn-glycero-3-phosphocholine O-acyltransferase and CTP:phosphocholine cytidylyltransferase activity to lipid peroxidation and hydroperoxide treatment
    • Anfuso C.D., Lupo G., Sipione S., Alberghina M. Susceptibility of rat retina acyl-CoA: 1-acyl-sn-glycero-3-phosphocholine O-acyltransferase and CTP:phosphocholine cytidylyltransferase activity to lipid peroxidation and hydroperoxide treatment. FEBS Lett. 347:1994;123-127.
    • (1994) FEBS Lett. , vol.347 , pp. 123-127
    • Anfuso, C.D.1    Lupo, G.2    Sipione, S.3    Alberghina, M.4
  • 27
    • 0029017977 scopus 로고
    • Lipid peroxidation inhibits oleoyl-CoA: 1-acyl-sn-glycero-3-phosphocholine O-acyltransferase but not CTP:phosphocholine cytidylyltransferase in rat brain membranes
    • Alberghina M., Lupo G., Anfuso C.D., el Ghonemy S.H.I. Lipid peroxidation inhibits oleoyl-CoA: 1-acyl-sn-glycero-3-phosphocholine O-acyltransferase but not CTP:phosphocholine cytidylyltransferase in rat brain membranes. Neurochem. Int. 26:1995;477-487.
    • (1995) Neurochem. Int. , vol.26 , pp. 477-487
    • Alberghina, M.1    Lupo, G.2    Anfuso, C.D.3    El Ghonemy, S.H.I.4
  • 28
    • 0025279551 scopus 로고
    • Effect of hypoxia on phosphatidylcholine biosynthesis in the isolated hamster heart
    • Hatch G.M., Choy P.C. Effect of hypoxia on phosphatidylcholine biosynthesis in the isolated hamster heart. Biochem. J. 268:1990;47-54.
    • (1990) Biochem. J. , vol.268 , pp. 47-54
    • Hatch, G.M.1    Choy, P.C.2
  • 29
    • 0021266236 scopus 로고
    • CTP:phosphorylcholine cytidylyltransferase in rat lung: The effect of free fatty acids on the translocation of activity between microsomes and cytosol
    • Weinhold P.A., Rounsifer M.E., Williams S.E., Brubaker P.G., Feldman D.A. CTP:phosphorylcholine cytidylyltransferase in rat lung: the effect of free fatty acids on the translocation of activity between microsomes and cytosol. J. Biol. Chem. 259:1984;10315-10321.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10315-10321
    • Weinhold, P.A.1    Rounsifer, M.E.2    Williams, S.E.3    Brubaker, P.G.4    Feldman, D.A.5
  • 30
    • 0020607490 scopus 로고
    • Fatty acids promote translocation of CTP:phosphocholine cytidylyltransferase to the endoplasmic reticulum and stimulate rat hepatic phosphatidylcholine synthesis
    • Pelech S.L., Pritchard P.H., Brindley D.N., Vance D.E. Fatty acids promote translocation of CTP:phosphocholine cytidylyltransferase to the endoplasmic reticulum and stimulate rat hepatic phosphatidylcholine synthesis. J. Biol. Chem. 258:1983;6782-6788.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6782-6788
    • Pelech, S.L.1    Pritchard, P.H.2    Brindley, D.N.3    Vance, D.E.4
  • 32
    • 0023935408 scopus 로고
    • Brain cell death following ischemia and reperfusion: A proposed biochemical sequence
    • Krause G.S., White B.C., Aust S.D., Nayini N.R., Kumar K. Brain cell death following ischemia and reperfusion: a proposed biochemical sequence. Crit. Care Med. 16:1988;714-726.
    • (1988) Crit. Care Med. , vol.16 , pp. 714-726
    • Krause, G.S.1    White, B.C.2    Aust, S.D.3    Nayini, N.R.4    Kumar, K.5
  • 33
    • 0024520513 scopus 로고
    • Central nervous system trauma and stroke. I. Biochemical considerations for oxygen radical formation and lipid peroxidation
    • Braugler J.M., Hall E.D. Central nervous system trauma and stroke. I. Biochemical considerations for oxygen radical formation and lipid peroxidation. Free Rad. Biol. Med. 6:1989;289-301.
    • (1989) Free Rad. Biol. Med. , vol.6 , pp. 289-301
    • Braugler, J.M.1    Hall, E.D.2
  • 34
    • 0027525526 scopus 로고
    • Brain injury by global ischemia and reperfusion: A theoretical perspective on membrane damage and repair (Review)
    • White B.C., Grossman L.I., Krause G.S. Brain injury by global ischemia and reperfusion: a theoretical perspective on membrane damage and repair (Review). Neurology. 43:1993;1656-1665.
    • (1993) Neurology , vol.43 , pp. 1656-1665
    • White, B.C.1    Grossman, L.I.2    Krause, G.S.3
  • 36
    • 0029895638 scopus 로고    scopus 로고
    • Disparate effects of oxidation on plasma acyltransferase activities: Inhibition of cholesterol esterification but stimulation of transesterification of oxidized phospholipids
    • Subbaiah P.V., Liu M. Disparate effects of oxidation on plasma acyltransferase activities: inhibition of cholesterol esterification but stimulation of transesterification of oxidized phospholipids. Biochim. Biophys. Acta. 1301:1996;115-126.
    • (1996) Biochim. Biophys. Acta , vol.1301 , pp. 115-126
    • Subbaiah, P.V.1    Liu, M.2
  • 37
    • 0025312048 scopus 로고
    • Lipid peroxidation inactivates rat liver microsomal glycerol-3-phosphate acyl transferase
    • Thomas P.D., Poznansky M.J. Lipid peroxidation inactivates rat liver microsomal glycerol-3-phosphate acyl transferase. J. Biol. Chem. 265:1990;2684-2691.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2684-2691
    • Thomas, P.D.1    Poznansky, M.J.2
  • 38
    • 0025214407 scopus 로고
    • Lipid peroxidation as the mechanism of modification of brain 5′-nucleotidase activity in vitro
    • Mishra O.P., Delivoria-Papadopoulos M., Cahillane G., Wagerles L.C. Lipid peroxidation as the mechanism of modification of brain 5′-nucleotidase activity in vitro. Neurochem. Res. 15:1990;237-242.
    • (1990) Neurochem. Res. , vol.15 , pp. 237-242
    • Mishra, O.P.1    Delivoria-Papadopoulos, M.2    Cahillane, G.3    Wagerles, L.C.4
  • 44
    • 0028006744 scopus 로고
    • Activation of the mitogen-activated protein kinase signaling pathway in neutrophils (role of oxidants)
    • Fialkow L., Chan C.K., Rotin D., Grinstein S., Downey G.P. Activation of the mitogen-activated protein kinase signaling pathway in neutrophils (role of oxidants). J. Biol. Chem. 269:1994;31234-31242.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31234-31242
    • Fialkow, L.1    Chan, C.K.2    Rotin, D.3    Grinstein, S.4    Downey, G.P.5
  • 45
    • 0029744885 scopus 로고    scopus 로고
    • Sounding the alarm: Protein kinase cascades activated by stress and inflammation (Minireview)
    • Kyriakis J.M., Avruch J. Sounding the alarm: protein kinase cascades activated by stress and inflammation (Minireview). J. Biol. Chem. 271:1996;24313-24316.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24313-24316
    • Kyriakis, J.M.1    Avruch, J.2
  • 46
    • 0020597565 scopus 로고
    • Leukotrienes: Mediators of immediate hypersensitivity reactions and inflammation
    • Samuelsson B. Leukotrienes: mediators of immediate hypersensitivity reactions and inflammation. Science. 220:1983;568-575.
    • (1983) Science , vol.220 , pp. 568-575
    • Samuelsson, B.1
  • 47
    • 0022313066 scopus 로고
    • Interaction of lipid hydroperoxides with eicosenoid biosynthesis
    • Lands W.E.M. Interaction of lipid hydroperoxides with eicosenoid biosynthesis. J. Free Rad. Biol. Med. 1:1985;97-101.
    • (1985) J. Free Rad. Biol. Med. , vol.1 , pp. 97-101
    • Lands, W.E.M.1
  • 48
    • 0025908558 scopus 로고
    • Human plasma platelet-activating factor acetylhydrolase (oxidative fragmented phospholipids as substrates)
    • Stremler K.E., Stafforini D.M., Prescott S.M., McIntyre T.M. Human plasma platelet-activating factor acetylhydrolase (oxidative fragmented phospholipids as substrates). J. Biol. Chem. 266:1991;11095-11103.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11095-11103
    • Stremler, K.E.1    Stafforini, D.M.2    Prescott, S.M.3    McIntyre, T.M.4


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