메뉴 건너뛰기




Volumn 1758, Issue 4, 2006, Pages 499-508

Preferable stimulation of PON1 arylesterase activity by phosphatidylcholines with unsaturated acyl chains or oxidized acyl chains at sn-2 position

Author keywords

Acyl chain; Arylesterase; Oxidized; Paraoxonase; Phospholipid; PON1; Preferable stimulation; Unsaturation

Indexed keywords

ARYLDIALKYLPHOSPHATASE; ARYLDIALKYLPHOSPHATASE 1; ARYLESTERASE; PHOSPHATIDIC ACID; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLGLYCEROL; PHOSPHATIDYLSERINE;

EID: 33646861598     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.03.022     Document Type: Article
Times cited : (17)

References (62)
  • 1
    • 0029905656 scopus 로고    scopus 로고
    • Structural and functional diversity of paraoxonase
    • La Du B.N. Structural and functional diversity of paraoxonase. Nat. Med. 2 (1996) 1186-1187
    • (1996) Nat. Med. , vol.2 , pp. 1186-1187
    • La Du, B.N.1
  • 4
    • 0034635449 scopus 로고    scopus 로고
    • Calcium-dependent human serum homocysteine thiolactone hydrolase. A protective mechanism against protein N-homocysteinylation
    • Jakubowski H. Calcium-dependent human serum homocysteine thiolactone hydrolase. A protective mechanism against protein N-homocysteinylation. J. Biol. Chem. 275 (2000) 3957-3962
    • (2000) J. Biol. Chem. , vol.275 , pp. 3957-3962
    • Jakubowski, H.1
  • 5
    • 0030293198 scopus 로고    scopus 로고
    • The effect of the human serum paraoxonase polymorphism is reversed with diazoxon, soman and sarin
    • Davies H.G., Richter R.J., Keifer M., Broomfield C.A., Sowalla J., and Furlong C.E. The effect of the human serum paraoxonase polymorphism is reversed with diazoxon, soman and sarin. Nat. Genet. 14 (1996) 334-336
    • (1996) Nat. Genet. , vol.14 , pp. 334-336
    • Davies, H.G.1    Richter, R.J.2    Keifer, M.3    Broomfield, C.A.4    Sowalla, J.5    Furlong, C.E.6
  • 6
    • 0026096803 scopus 로고
    • Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities
    • Gan K.N., Smolen A., Eckerson H.W., and La Du B.N. Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities. Drug Metab. Dispos. 19 (1991) 100-106
    • (1991) Drug Metab. Dispos. , vol.19 , pp. 100-106
    • Gan, K.N.1    Smolen, A.2    Eckerson, H.W.3    La Du, B.N.4
  • 9
    • 0037443799 scopus 로고    scopus 로고
    • Paraoxonase (PON1) deficiency is associated with increased macrophage oxidative stress: studies in PON1-knockout mice
    • Rozenberg O., Rosenblat M., Coleman R., Shih D.M., and Aviram M. Paraoxonase (PON1) deficiency is associated with increased macrophage oxidative stress: studies in PON1-knockout mice. Free Radic. Biol. Med. 34 (2003) 774-784
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 774-784
    • Rozenberg, O.1    Rosenblat, M.2    Coleman, R.3    Shih, D.M.4    Aviram, M.5
  • 11
    • 20444419056 scopus 로고    scopus 로고
    • Paraoxonase 1 (PON1) attenuates macrophage oxidative status: studies in PON1 transfected cells and in PON1 transgenic mice
    • Rozenberg O., Shih D.M., and Aviram M. Paraoxonase 1 (PON1) attenuates macrophage oxidative status: studies in PON1 transfected cells and in PON1 transgenic mice. Atherosclerosis 181 (2005) 9-18
    • (2005) Atherosclerosis , vol.181 , pp. 9-18
    • Rozenberg, O.1    Shih, D.M.2    Aviram, M.3
  • 12
    • 0032522985 scopus 로고    scopus 로고
    • Paraoxonase inhibits high-density lipoprotein oxidation and preserves its functions. A possible peroxidative role for paraoxonase
    • Aviram M., Rosenblat M., Bisgaier C.L., Newton R.S., Primo-Parmo S.L., and La Du B.N. Paraoxonase inhibits high-density lipoprotein oxidation and preserves its functions. A possible peroxidative role for paraoxonase. J. Clin. Invest. 101 (1998) 1581-1590
    • (1998) J. Clin. Invest. , vol.101 , pp. 1581-1590
    • Aviram, M.1    Rosenblat, M.2    Bisgaier, C.L.3    Newton, R.S.4    Primo-Parmo, S.L.5    La Du, B.N.6
  • 13
    • 5344238178 scopus 로고    scopus 로고
    • Paraoxonases 1, 2, and 3, oxidative stress, and macrophage foam cell formation during atherosclerosis development
    • Aviram M., and Rosenblat M. Paraoxonases 1, 2, and 3, oxidative stress, and macrophage foam cell formation during atherosclerosis development. Free Radic. Biol. Med. 37 (2004) 1304-1316
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 1304-1316
    • Aviram, M.1    Rosenblat, M.2
  • 15
    • 13844256208 scopus 로고    scopus 로고
    • Paraoxonase 1 (PON1) enhances HDL-mediated macrophage cholesterol efflux via the ABCA1 transporter in association with increased HDL binding to the cells: a possible role for lysophosphatidylcholine
    • Rosenblat M., Vaya J., Shih D., and Aviram M. Paraoxonase 1 (PON1) enhances HDL-mediated macrophage cholesterol efflux via the ABCA1 transporter in association with increased HDL binding to the cells: a possible role for lysophosphatidylcholine. Atherosclerosis 179 (2005) 69-77
    • (2005) Atherosclerosis , vol.179 , pp. 69-77
    • Rosenblat, M.1    Vaya, J.2    Shih, D.3    Aviram, M.4
  • 16
    • 9244247649 scopus 로고    scopus 로고
    • Distribution spectrum of paraoxonase activity in HDL fractions
    • Bergmeier C., Siekmeier R., and Gross W. Distribution spectrum of paraoxonase activity in HDL fractions. Clin. Chem. 50 (2004) 2309-2315
    • (2004) Clin. Chem. , vol.50 , pp. 2309-2315
    • Bergmeier, C.1    Siekmeier, R.2    Gross, W.3
  • 17
    • 33646872590 scopus 로고    scopus 로고
    • M. Rosenblat, R. Karry, M. Aviram, Paraoxonase 1 (PON1) is a more potent antioxidant and stimulant of macrophage cholesterol efflux, when present in HDL than in lipoprotein-deficient serum: relevance to diabetes, Atherosclerosis (in press).
  • 21
    • 0034673981 scopus 로고    scopus 로고
    • Smoking is associated with reduced serum paraoxonase activity and concentration in patients with coronary artery disease
    • James R.W., Leviev I., and Righetti A. Smoking is associated with reduced serum paraoxonase activity and concentration in patients with coronary artery disease. Circulation 101 (2000) 2252-2257
    • (2000) Circulation , vol.101 , pp. 2252-2257
    • James, R.W.1    Leviev, I.2    Righetti, A.3
  • 22
    • 0347948591 scopus 로고    scopus 로고
    • Study of factors influencing the decreased HDL associated PON1 activity with aging
    • Seres I., Paragh G., Deschene E., Fulop Jr. T., and Khalil A. Study of factors influencing the decreased HDL associated PON1 activity with aging. Exp. Gerontol. 39 (2004) 59-66
    • (2004) Exp. Gerontol. , vol.39 , pp. 59-66
    • Seres, I.1    Paragh, G.2    Deschene, E.3    Fulop Jr., T.4    Khalil, A.5
  • 23
    • 10044283247 scopus 로고    scopus 로고
    • Preferential inhibition of paraoxonase activity of human paraoxonase 1 by negatively charged lipids
    • Nguyen S.D., and Sok D.E. Preferential inhibition of paraoxonase activity of human paraoxonase 1 by negatively charged lipids. J. Lipid Res. 45 (2004) 2211-2220
    • (2004) J. Lipid Res. , vol.45 , pp. 2211-2220
    • Nguyen, S.D.1    Sok, D.E.2
  • 24
    • 33646856339 scopus 로고    scopus 로고
    • L. Jaouad, C. de Guise, H. Berrougui, M. Cloutier, M. Isabelle, T. Fulop, H. Payette, A. Khalil, Age-related decrease in high-density lipoproteins antioxidant activity is due to an alteration in the PON1's free sulfhydryl groups, Atherosclerosis (in press).
  • 26
    • 0029165744 scopus 로고
    • Comparison of purified human and rabbit serum paraoxonases
    • Kuo C.L., and La Du B.N. Comparison of purified human and rabbit serum paraoxonases. Drug Metab. Dispos. 23 (1995) 935-944
    • (1995) Drug Metab. Dispos. , vol.23 , pp. 935-944
    • Kuo, C.L.1    La Du, B.N.2
  • 29
    • 0031795752 scopus 로고    scopus 로고
    • Lipid polymorphism and protein-lipid interactions
    • Epand R.M. Lipid polymorphism and protein-lipid interactions. Biochim. Biophys. Acta 1376 (1998) 353-368
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 353-368
    • Epand, R.M.1
  • 30
    • 0142138852 scopus 로고    scopus 로고
    • Beneficial effect of oleoylated lipids on paraoxonase1: protection against oxidative inactivation and stabilization
    • Nguyen S.D., and Sok D.E. Beneficial effect of oleoylated lipids on paraoxonase1: protection against oxidative inactivation and stabilization. Biochem. J. 375 (2003) 275-285
    • (2003) Biochem. J. , vol.375 , pp. 275-285
    • Nguyen, S.D.1    Sok, D.E.2
  • 31
    • 0021070710 scopus 로고
    • The human serum paraoxonase/arylesterase polymorphism
    • Eckerson H.W., Wyle C.M., and La Du B.N. The human serum paraoxonase/arylesterase polymorphism. Am. J. Hum. Genet. 35 (1983) 1126-1138
    • (1983) Am. J. Hum. Genet. , vol.35 , pp. 1126-1138
    • Eckerson, H.W.1    Wyle, C.M.2    La Du, B.N.3
  • 32
    • 0016850021 scopus 로고
    • Separation of plasma lipoproteins by density-gradient ultracentrifugation
    • Redgrave T.G., Roberts D.C., and West C.E. Separation of plasma lipoproteins by density-gradient ultracentrifugation. Anal. Biochem. 65 (1975) 42-49
    • (1975) Anal. Biochem. , vol.65 , pp. 42-49
    • Redgrave, T.G.1    Roberts, D.C.2    West, C.E.3
  • 33
    • 0036043968 scopus 로고    scopus 로고
    • Preparation, isolation, and characterization of liposomes containing natural and synthetic lipids
    • Chatterjee S., and Banerjee D.K. Preparation, isolation, and characterization of liposomes containing natural and synthetic lipids. Methods Mol. Biol. 199 (2002) 3-16
    • (2002) Methods Mol. Biol. , vol.199 , pp. 3-16
    • Chatterjee, S.1    Banerjee, D.K.2
  • 34
    • 0015801350 scopus 로고
    • Lipid model membranes. Characterization of mixed phospholipid vesicles
    • Litman B.J. Lipid model membranes. Characterization of mixed phospholipid vesicles. Biochemistry 12 (1973) 2545-2554
    • (1973) Biochemistry , vol.12 , pp. 2545-2554
    • Litman, B.J.1
  • 35
    • 24044485601 scopus 로고    scopus 로고
    • Oxidized phospholipids induce phase separation in lipid vesicles
    • Megli F.M., Russo L., and Sabatini K. Oxidized phospholipids induce phase separation in lipid vesicles. FEBS Lett. 579 (2005) 4577-4584
    • (2005) FEBS Lett. , vol.579 , pp. 4577-4584
    • Megli, F.M.1    Russo, L.2    Sabatini, K.3
  • 36
    • 0033515056 scopus 로고    scopus 로고
    • Identification of residues essential for human paraoxonase (PON1) arylesterase/organophosphatase activities
    • Josse D., Xie W., Renault F., Rochu D., Schopfer L.M., Masson P., and Lockridge O. Identification of residues essential for human paraoxonase (PON1) arylesterase/organophosphatase activities. Biochemistry 38 (1999) 2816-2825
    • (1999) Biochemistry , vol.38 , pp. 2816-2825
    • Josse, D.1    Xie, W.2    Renault, F.3    Rochu, D.4    Schopfer, L.M.5    Masson, P.6    Lockridge, O.7
  • 37
    • 0002476204 scopus 로고
    • Analysis of variance I: The one-way classification
    • McGraw-Hill, New York
    • Steel R.G.D., and Torrie J.H. Analysis of variance I: The one-way classification. Principles and Procedures of Statistics (1960), McGraw-Hill, New York 99-132
    • (1960) Principles and Procedures of Statistics , pp. 99-132
    • Steel, R.G.D.1    Torrie, J.H.2
  • 38
    • 0142124855 scopus 로고    scopus 로고
    • Oxidized phospholipids as modulators of inflammation in atherosclerosis
    • Leitinger N. Oxidized phospholipids as modulators of inflammation in atherosclerosis. Curr. Opin. Lipidol. 14 (2003) 421-430
    • (2003) Curr. Opin. Lipidol. , vol.14 , pp. 421-430
    • Leitinger, N.1
  • 39
    • 0023920459 scopus 로고
    • Activation of protein kinase C by short chain phosphatidylcholines
    • Walker J.M., and Sando J.J. Activation of protein kinase C by short chain phosphatidylcholines. J. Biol. Chem. 263 (1988) 4537-4540
    • (1988) J. Biol. Chem. , vol.263 , pp. 4537-4540
    • Walker, J.M.1    Sando, J.J.2
  • 40
    • 0345492016 scopus 로고    scopus 로고
    • Lipid-protein interactions studied by introduction of a tryptophan residue: the mechanosensitive channel MscL
    • Powl A.M., East J.M., and Lee A.G. Lipid-protein interactions studied by introduction of a tryptophan residue: the mechanosensitive channel MscL. Biochemistry 42 (2003) 14306-14317
    • (2003) Biochemistry , vol.42 , pp. 14306-14317
    • Powl, A.M.1    East, J.M.2    Lee, A.G.3
  • 41
    • 0028075333 scopus 로고
    • The modulation of protein kinase C activity by membrane lipid bilayer structure
    • Slater S.J., Kelly M.B., Taddeo F.J., Ho C., Rubin E., and Stubbs C.D. The modulation of protein kinase C activity by membrane lipid bilayer structure. J. Biol. Chem. 269 (1994) 4866-4871
    • (1994) J. Biol. Chem. , vol.269 , pp. 4866-4871
    • Slater, S.J.1    Kelly, M.B.2    Taddeo, F.J.3    Ho, C.4    Rubin, E.5    Stubbs, C.D.6
  • 42
    • 0035830646 scopus 로고    scopus 로고
    • Organotin compounds alter the physical organization of phosphatidylcholine membranes
    • Chicano J.J., Ortiz A., Teruel J.A., and Aranda F.J. Organotin compounds alter the physical organization of phosphatidylcholine membranes. Biochim. Biophys. Acta 1510 (2001) 330-341
    • (2001) Biochim. Biophys. Acta , vol.1510 , pp. 330-341
    • Chicano, J.J.1    Ortiz, A.2    Teruel, J.A.3    Aranda, F.J.4
  • 43
    • 0026018961 scopus 로고
    • Packing characteristics of highly unsaturated bilayer lipids: raman spectroscopic studies of multilamellar phosphatidylcholine dispersions
    • Litman B.J., Lewis E.N., and Levin I.W. Packing characteristics of highly unsaturated bilayer lipids: raman spectroscopic studies of multilamellar phosphatidylcholine dispersions. Biochemistry 30 (1991) 313-319
    • (1991) Biochemistry , vol.30 , pp. 313-319
    • Litman, B.J.1    Lewis, E.N.2    Levin, I.W.3
  • 44
    • 0028117570 scopus 로고
    • A calorimetric investigation of a series of mixed-chain polyunsaturated phosphatidylcholines: effect of sn-2 chain length and degree of unsaturation
    • Niebylski C.D., and Salem Jr. N. A calorimetric investigation of a series of mixed-chain polyunsaturated phosphatidylcholines: effect of sn-2 chain length and degree of unsaturation. Biophys. J. 67 (1994) 2387-2393
    • (1994) Biophys. J. , vol.67 , pp. 2387-2393
    • Niebylski, C.D.1    Salem Jr., N.2
  • 45
    • 0033598833 scopus 로고    scopus 로고
    • CTP: phosphocholine cytidylyltransferase activation by oxidized phosphatidylcholines correlates with a decrease in lipid order: a 2H NMR analysis
    • Drobnies A.E., van Der Ende B., Thewalt J.L., and Cornell R.B. CTP: phosphocholine cytidylyltransferase activation by oxidized phosphatidylcholines correlates with a decrease in lipid order: a 2H NMR analysis. Biochemistry 38 (1999) 15606-15614
    • (1999) Biochemistry , vol.38 , pp. 15606-15614
    • Drobnies, A.E.1    van Der Ende, B.2    Thewalt, J.L.3    Cornell, R.B.4
  • 46
    • 1642359646 scopus 로고    scopus 로고
    • Roles of curvature and hydrophobic interstice energy in fusion: studies of lipid perturbant effects
    • Haque M.E., and Lentz B.R. Roles of curvature and hydrophobic interstice energy in fusion: studies of lipid perturbant effects. Biochemistry 43 (2004) 3507-3517
    • (2004) Biochemistry , vol.43 , pp. 3507-3517
    • Haque, M.E.1    Lentz, B.R.2
  • 47
    • 0035138344 scopus 로고    scopus 로고
    • The enthalpy of acyl chain packing and the apparent water-accessible apolar surface area of phospholipids
    • Heerklotz H., and Epand R.M. The enthalpy of acyl chain packing and the apparent water-accessible apolar surface area of phospholipids. Biophys. J. 80 (2001) 271-279
    • (2001) Biophys. J. , vol.80 , pp. 271-279
    • Heerklotz, H.1    Epand, R.M.2
  • 48
    • 0022626736 scopus 로고
    • Polymorphic phase behavior of platelet-activating factor
    • Huang C., Mason J.T., Stephenson F.A., and Levin I.W. Polymorphic phase behavior of platelet-activating factor. Biophys. J. 49 (1986) 587-595
    • (1986) Biophys. J. , vol.49 , pp. 587-595
    • Huang, C.1    Mason, J.T.2    Stephenson, F.A.3    Levin, I.W.4
  • 51
    • 0018180248 scopus 로고
    • Comparative studies on the effects of pH and Ca2+ on bilayers of various negatively charged phospholipids and their mixtures with phosphatidylcholine
    • van Dijck P.W., de Kruijff B., Verkleij A.J., van Deenen L.L., and de Gier J. Comparative studies on the effects of pH and Ca2+ on bilayers of various negatively charged phospholipids and their mixtures with phosphatidylcholine. Biochim. Biophys. Acta 512 (1978) 84-96
    • (1978) Biochim. Biophys. Acta , vol.512 , pp. 84-96
    • van Dijck, P.W.1    de Kruijff, B.2    Verkleij, A.J.3    van Deenen, L.L.4    de Gier, J.5
  • 52
    • 0032483123 scopus 로고    scopus 로고
    • Interfacial membrane properties modulate protein kinase C activation: role of the position of acyl chain unsaturation
    • Giorgione J.R., Kraayenhof R., and Ep R.M. Interfacial membrane properties modulate protein kinase C activation: role of the position of acyl chain unsaturation. Biochemistry 37 (1998) 10956-10960
    • (1998) Biochemistry , vol.37 , pp. 10956-10960
    • Giorgione, J.R.1    Kraayenhof, R.2    Ep, R.M.3
  • 53
    • 0035807063 scopus 로고    scopus 로고
    • Regulation of CTP: phosphocholine cytidylyltransferase activity by the physical properties of lipid membranes: an important role for stored curvature strain energy
    • Davies S.M., Epand R.M., Kraayenhof R., and Cornell R.B. Regulation of CTP: phosphocholine cytidylyltransferase activity by the physical properties of lipid membranes: an important role for stored curvature strain energy. Biochemistry 40 (2001) 10522-10531
    • (2001) Biochemistry , vol.40 , pp. 10522-10531
    • Davies, S.M.1    Epand, R.M.2    Kraayenhof, R.3    Cornell, R.B.4
  • 54
    • 0042823534 scopus 로고    scopus 로고
    • Curvature and bending constants for phosphatidylserine-containing membranes
    • Fuller N., Benatti C.R., and Rand R.P. Curvature and bending constants for phosphatidylserine-containing membranes. Biophys. J. 85 (2003) 1667-1674
    • (2003) Biophys. J. , vol.85 , pp. 1667-1674
    • Fuller, N.1    Benatti, C.R.2    Rand, R.P.3
  • 55
    • 0027179178 scopus 로고
    • Role of membrane defects in the regulation of the activity of protein kinase C
    • Senisterra G., and Epand R.M. Role of membrane defects in the regulation of the activity of protein kinase C. Arch. Biochem. Biophys. 300 (1993) 378-383
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 378-383
    • Senisterra, G.1    Epand, R.M.2
  • 56
    • 0022815250 scopus 로고
    • Morphological responses to calcium-induced interaction of phosphatidylserine-containing vesicles
    • Kachar B., Fuller N., and Rand R.P. Morphological responses to calcium-induced interaction of phosphatidylserine-containing vesicles. Biophys. J. 50 (1986) 779-788
    • (1986) Biophys. J. , vol.50 , pp. 779-788
    • Kachar, B.1    Fuller, N.2    Rand, R.P.3
  • 57
    • 17044372764 scopus 로고    scopus 로고
    • Paraoxonase 1 (PON1) is present in postprandial chylomicrons
    • Fuhrman B., Volkova N., and Aviram M. Paraoxonase 1 (PON1) is present in postprandial chylomicrons. Atherosclerosis 180 (2005) 55-61
    • (2005) Atherosclerosis , vol.180 , pp. 55-61
    • Fuhrman, B.1    Volkova, N.2    Aviram, M.3
  • 58
    • 24344460308 scopus 로고    scopus 로고
    • High affinity, stability, and lactonase activity of serum paraoxonase PON1 anchored on HDL with ApoA-I
    • Gaidukov L., and Tawfik D.S. High affinity, stability, and lactonase activity of serum paraoxonase PON1 anchored on HDL with ApoA-I. Biochemistry 44 (2005) 11843-11854
    • (2005) Biochemistry , vol.44 , pp. 11843-11854
    • Gaidukov, L.1    Tawfik, D.S.2
  • 60
    • 12244252280 scopus 로고    scopus 로고
    • Paraoxonase-1 reduces monocyte chemotaxis and adhesion to endothelial cells due to oxidation of palmitoyl, linoleoyl glycerophosphorylcholine
    • Ahmed Z., Babaei S., Maguire G.F., Draganov D., Kuksis A., La Du B.N., and Connelly P.W. Paraoxonase-1 reduces monocyte chemotaxis and adhesion to endothelial cells due to oxidation of palmitoyl, linoleoyl glycerophosphorylcholine. Cardiovasc. Res. 57 (2003) 225-231
    • (2003) Cardiovasc. Res. , vol.57 , pp. 225-231
    • Ahmed, Z.1    Babaei, S.2    Maguire, G.F.3    Draganov, D.4    Kuksis, A.5    La Du, B.N.6    Connelly, P.W.7
  • 62
    • 0142200309 scopus 로고    scopus 로고
    • Group V and X secretory phospholipase A(2)s-induced modification of high-density lipoprotein linked to the reduction of its antiatherogenic functions
    • Ishimoto Y., Yamada K., Yamamoto S., Ono T., Notoya M., and Hanasaki K. Group V and X secretory phospholipase A(2)s-induced modification of high-density lipoprotein linked to the reduction of its antiatherogenic functions. Biochim. Biophys. Acta 1642 (2003) 129-138
    • (2003) Biochim. Biophys. Acta , vol.1642 , pp. 129-138
    • Ishimoto, Y.1    Yamada, K.2    Yamamoto, S.3    Ono, T.4    Notoya, M.5    Hanasaki, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.