메뉴 건너뛰기




Volumn 41, Issue 4, 2000, Pages 546-553

Phosphatidylcholine fluidity and structure affect lecithin:cholesterol acyltransferase activity

Author keywords

Cholesteryl ester; High density lipoproteins; n 3 fatty acids; Trans fatty acids

Indexed keywords

APOLIPOPROTEIN A1; CHOLESTEROL ESTER; HIGH DENSITY LIPOPROTEIN; OMEGA 3 FATTY ACID; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLCHOLINE STEROL ACYLTRANSFERASE; TRITIUM;

EID: 0033993972     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (40)

References (27)
  • 1
    • 0014264541 scopus 로고
    • The plasma lecithin:cholesterol acyltransferase reaction
    • Glomset, J. A. 1968. The plasma lecithin:cholesterol acyltransferase reaction. J. Lipid Res. 9: 155-167.
    • (1968) J. Lipid Res. , vol.9 , pp. 155-167
    • Glomset, J.A.1
  • 2
    • 0022626984 scopus 로고
    • Selectivity and contribution of lecithin:cholesterol acyltransferase to plasma cholesterol ester formation
    • Ueno, K., N. Sakuma, M. Kawaguchi, T. Fujinami, and H. Okuyama. 1986. Selectivity and contribution of lecithin:cholesterol acyltransferase to plasma cholesterol ester formation. J. Biochem. 99: 541-547.
    • (1986) J. Biochem. , vol.99 , pp. 541-547
    • Ueno, K.1    Sakuma, N.2    Kawaguchi, M.3    Fujinami, T.4    Okuyama, H.5
  • 3
    • 0018120222 scopus 로고
    • Human plasma lecithin-cholesterol acyltransferase. Characterization of cofactor-dependent phospholipase activity
    • Aron, L., S. Jones, and C. J. Fielding. 1978. Human plasma lecithin-cholesterol acyltransferase. Characterization of cofactor-dependent phospholipase activity. J. Biol. Chem. 253: 7220-7226.
    • (1978) J. Biol. Chem. , vol.253 , pp. 7220-7226
    • Aron, L.1    Jones, S.2    Fielding, C.J.3
  • 4
    • 0015502979 scopus 로고
    • Lecithin: Cholesterol acyltransferase: effects of substrate composition upon enzyme activity
    • Fielding, C. J., V. G. Shore, and P. E. Fielding. 1972. Lecithin: cholesterol acyltransferase: effects of substrate composition upon enzyme activity. Biochim. Biophys. Acta. 270: 513-518.
    • (1972) Biochim. Biophys. Acta , vol.270 , pp. 513-518
    • Fielding, C.J.1    Shore, V.G.2    Fielding, P.E.3
  • 5
    • 0028887870 scopus 로고
    • Molecular physiology of reverse cholesterol transport
    • Fielding, C. J., and P. E. Fielding. 1995. Molecular physiology of reverse cholesterol transport. J. Lipid Res. 36: 211-228.
    • (1995) J. Lipid Res. , vol.36 , pp. 211-228
    • Fielding, C.J.1    Fielding, P.E.2
  • 6
    • 0014866663 scopus 로고
    • Plasma lipoproteins in familial lecithin:cholesterol acyltransferase deficiency: Lipid composition and reactivity in vitro
    • Glomset, J. A., K. R. Norum, and W. King. 1970. Plasma lipoproteins in familial lecithin:cholesterol acyltransferase deficiency: lipid composition and reactivity in vitro. J. Clin. Invest. 49: 1827-1867.
    • (1970) J. Clin. Invest. , vol.49 , pp. 1827-1867
    • Glomset, J.A.1    Norum, K.R.2    King, W.3
  • 7
    • 0030991224 scopus 로고    scopus 로고
    • Disruption of the murine lecithin:cholesterol acyltransferase gene causes impairment of adrenal lipid delivery and up-regulation of scavenger receptor class B type I
    • Ng, D. S., O. L. Francone, T. M. Forte, J. L. Zhang, M. Haghpassand, and E. M. Rubin. 1997. Disruption of the murine lecithin:cholesterol acyltransferase gene causes impairment of adrenal lipid delivery and up-regulation of scavenger receptor class B type I. J. Biol. Chem. 272: 15777-15781.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15777-15781
    • Ng, D.S.1    Francone, O.L.2    Forte, T.M.3    Zhang, J.L.4    Haghpassand, M.5    Rubin, E.M.6
  • 8
    • 0030897994 scopus 로고    scopus 로고
    • Targeted disruption of the mouse lecithin:cholesterol acyltransferase (LCAT) gene - Generation of a new animal model for human LCAT deficiency
    • Sakai, N., B. L. Vaisman, C. A. Koch, R. F. Hoyt, Jr., S. M. Meyn, G. D. Talley, J. A. Paiz, H. B. Brewer, Jr., and S. Santamarina-Fojo. 1997. Targeted disruption of the mouse lecithin:cholesterol acyltransferase (LCAT) gene - Generation of a new animal model for human LCAT deficiency. J. Biol. Chem. 272: 7506-7510.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7506-7510
    • Sakai, N.1    Vaisman, B.L.2    Koch, C.A.3    Hoyt R.F., Jr.4    Meyn, S.M.5    Talley, G.D.6    Paiz, J.A.7    Brewer H.B., Jr.8    Santamarina-Fojo, S.9
  • 9
    • 0029070484 scopus 로고
    • Tissue-specific expression of the human gene for lecithin:cholesterol acyltransferase in transgenic mice alters blood lipids, lipoproteins and lipases towards a less atherogenic profile
    • Mehlum, A., B. Staels, N. Duverger, A. Tailleux, G. Castro, C. Fievet, G. Lue, J-C. Fruchart, G. Olivecrona, G. Skretting, J. Auwerx, and H. Prydz. 1995. Tissue-specific expression of the human gene for lecithin:cholesterol acyltransferase in transgenic mice alters blood lipids, lipoproteins and lipases towards a less atherogenic profile. Eur. J. Biochem. 230: 567-575.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 567-575
    • Mehlum, A.1    Staels, B.2    Duverger, N.3    Tailleux, A.4    Castro, G.5    Fievet, C.6    Lue, G.7    Fruchart, J.-C.8    Olivecrona, G.9    Skretting, G.10    Auwerx, J.11    Prydz, H.12
  • 10
    • 0029845121 scopus 로고    scopus 로고
    • Potential gene therapy for lecithin-cholesterol acyltransferase (LCAT)-deficient and hypoalphalipoproteinemic patients with adenovirus-mediated transfer of human LCAT gene
    • Séguret-Macé, S., M. Latta-Mahiett, G. Castro, G. Luc, J. C. Fruchart, E. Rubin, P. Denèfle, and N. Duverger. 1996. Potential gene therapy for lecithin-cholesterol acyltransferase (LCAT)-deficient and hypoalphalipoproteinemic patients with adenovirus-mediated transfer of human LCAT gene. Circulation 94: 2177-2184.
    • (1996) Circulation , vol.94 , pp. 2177-2184
    • Séguret-Macé, S.1    Latta-Mahiett, M.2    Castro, G.3    Luc, G.4    Fruchart, J.C.5    Rubin, E.6    Denèfle, P.7    Duverger, N.8
  • 12
    • 0023664182 scopus 로고
    • Reaction of discoidal complexes of apolipoprotein A-I and various phosphatidylcholines with lecithin:cholesterol acyltransferase. Interfacial effects
    • Jonas, A., N. L. Zorich, K. E. Kezdy, and W. E. Trick. 1987. Reaction of discoidal complexes of apolipoprotein A-I and various phosphatidylcholines with lecithin:cholesterol acyltransferase. Interfacial effects. J. Biol. Chem. 262: 3969-3974.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3969-3974
    • Jonas, A.1    Zorich, N.L.2    Kezdy, K.E.3    Trick, W.E.4
  • 13
    • 0021923801 scopus 로고
    • Acyl chain and head-group specificity of human plasma lecithin:cholesterol acyltransferase. Separation of matrix and molecular specificities
    • Pownall, H. J., Q. Pao, and J. B. Massey. 1985. Acyl chain and head-group specificity of human plasma lecithin:cholesterol acyltransferase. Separation of matrix and molecular specificities. J. Biol. Chem. 260: 2146-2152.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2146-2152
    • Pownall, H.J.1    Pao, Q.2    Massey, J.B.3
  • 14
    • 0021963754 scopus 로고
    • Isolation and specificity of rat lecithin:cholesterol acyltransferase: Comparison with the human enzyme using reassembled high-density lipoproteins containing ether analogs of phosphatidylcholine
    • Pownall, H. J., Q. Pao, and J. B. Massey. 1985. Isolation and specificity of rat lecithin:cholesterol acyltransferase: comparison with the human enzyme using reassembled high-density lipoproteins containing ether analogs of phosphatidylcholine. Biochim. Biophys. Acta. 833: 456-462.
    • (1985) Biochim. Biophys. Acta , vol.833 , pp. 456-462
    • Pownall, H.J.1    Pao, Q.2    Massey, J.B.3
  • 15
    • 0020488558 scopus 로고
    • Reaction of human lecithin:cholesterol acyltransferase with micellar substrates is independent of the phase state of the lipid
    • Jonas, A., and C. E. Matz. 1982. Reaction of human lecithin:cholesterol acyltransferase with micellar substrates is independent of the phase state of the lipid. Biochemistry. 21: 6867-6872.
    • (1982) Biochemistry , vol.21 , pp. 6867-6872
    • Jonas, A.1    Matz, C.E.2
  • 16
    • 0030894376 scopus 로고    scopus 로고
    • Long chain polyunsaturated fatty acids in the sn-2 position of phosphatidylcholine decrease the stability of recombinant high density lipoprotein apoA-I and the activation energy of lecithin:cholesterol acyltransferase reaction
    • Parks, J. S., and A. K. Gebre. 1997. Long chain polyunsaturated fatty acids in the sn-2 position of phosphatidylcholine decrease the stability of recombinant high density lipoprotein apoA-I and the activation energy of lecithin:cholesterol acyltransferase reaction. J. Lipid Res. 38: 266-275.
    • (1997) J. Lipid Res. , vol.38 , pp. 266-275
    • Parks, J.S.1    Gebre, A.K.2
  • 17
    • 0018727330 scopus 로고
    • Isolation and characterization of high density lipoprotein apoproteins in the non-human primate (vervet)
    • Parks, J. S., and L. L. Rudel. 1979. Isolation and characterization of high density lipoprotein apoproteins in the non-human primate (vervet). J. Biol. Chem. 254: 6716-6723.
    • (1979) J. Biol. Chem. , vol.254 , pp. 6716-6723
    • Parks, J.S.1    Rudel, L.L.2
  • 18
    • 0026769840 scopus 로고
    • Inhibition of lecithin:cholesterol acyltransferase activity by synthetic phosphatidylcholine species containing eicosapentaenoic acid or docosahexaenoic acid in the sn-2 position
    • Parks, J. S., T. Y. Thuren, and J. D. Schmitt. 1992. Inhibition of lecithin:cholesterol acyltransferase activity by synthetic phosphatidylcholine species containing eicosapentaenoic acid or docosahexaenoic acid in the sn-2 position. J. Lipid Res. 33: 879-887.
    • (1992) J. Lipid Res. , vol.33 , pp. 879-887
    • Parks, J.S.1    Thuren, T.Y.2    Schmitt, J.D.3
  • 20
    • 0032444552 scopus 로고    scopus 로고
    • Effect of long chain polyunsaturated fatty acids in the sn-2 position of phosphatidycholine on the interaction with recombinant high density lipoprotein apolipoprotein A-I
    • Huggins, K. W., L. K. Curtiss, A. K. Gebre, and J. S. Parks. 1998. Effect of long chain polyunsaturated fatty acids in the sn-2 position of phosphatidycholine on the interaction with recombinant high density lipoprotein apolipoprotein A-I. J. Lipid Res. 39: 2423-2431.
    • (1998) J. Lipid Res. , vol.39 , pp. 2423-2431
    • Huggins, K.W.1    Curtiss, L.K.2    Gebre, A.K.3    Parks, J.S.4
  • 21
    • 0029976437 scopus 로고    scopus 로고
    • Glycosylation structure and enzyme activity of lecithin:cholesterol acyltransferase from human plasma, Hep G2 cells, and baculoviral and Chinese hamster ovary cell expression systems
    • Miller, K. R., J. Wang, M. Sorci-Thomas, R. A. Anderson, and J. S. Parks. 1996. Glycosylation structure and enzyme activity of lecithin:cholesterol acyltransferase from human plasma, Hep G2 cells, and baculoviral and Chinese hamster ovary cell expression systems. J. Lipid Res. 37: 551-561.
    • (1996) J. Lipid Res. , vol.37 , pp. 551-561
    • Miller, K.R.1    Wang, J.2    Sorci-Thomas, M.3    Anderson, R.A.4    Parks, J.S.5
  • 23
    • 0030857975 scopus 로고    scopus 로고
    • Influence of the positions of cis double bonds in the sn-2-acyl chain of phosphatidylethanolamine on the bilayer's melting behavior
    • Huang, C. H., H. N. Lin, S. S. Li, and G. Q. Wang. 1997. Influence of the positions of cis double bonds in the sn-2-acyl chain of phosphatidylethanolamine on the bilayer's melting behavior. J. Biol. Chem. 272: 21917-21926.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21917-21926
    • Huang, C.H.1    Lin, H.N.2    Li, S.S.3    Wang, G.Q.4
  • 24
    • 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 N. Salem, Jr. 1991. A calorimetric investigation of a series of mixed-chain polyunsaturated phosphatidylcholines: effect of sn-2 chain length and degree of unsaturation. Biochem. J. 67: 2387-2393.
    • (1991) Biochem. J. , vol.67 , pp. 2387-2393
    • Niebylski, C.D.1    Salem N., Jr.2
  • 25
    • 0026034974 scopus 로고
    • A comparison of alpha-linolenic and gamma-linolenic acid in phosphatidylcholine bilayers
    • Ehringer, W. D., D. Belcher, S. R. Wassall, and W. Stillwell. 1991. A comparison of alpha-linolenic and gamma-linolenic acid in phosphatidylcholine bilayers. Chem. Phys. Lipid. 57: 87-96.
    • (1991) Chem. Phys. Lipid , vol.57 , pp. 87-96
    • Ehringer, W.D.1    Belcher, D.2    Wassall, S.R.3    Stillwell, W.4
  • 26
    • 0028308561 scopus 로고
    • Binding of lecithin:cholesterol acyltransferase to reconstituted high density lipoproteins is affected by their lipid but not apolipoprotein composition
    • Bolin, D. J., and A. Jonas. 1994. Binding of lecithin:cholesterol acyltransferase to reconstituted high density lipoproteins is affected by their lipid but not apolipoprotein composition. J. Biol. Chem. 269: 7429-7434.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7429-7434
    • Bolin, D.J.1    Jonas, A.2
  • 27
    • 0029017707 scopus 로고
    • Effect of interfacial pressure on the binding and phospholipase A2 activity of recombinant human lecithin-cholesterol acyltransferase
    • Weinberg, R. B., J. B. Jones, P. H. Pritchard, and A. G. Lacko. 1995. Effect of interfacial pressure on the binding and phospholipase A2 activity of recombinant human lecithin-cholesterol acyltransferase. Biochem. Biophys. Res. Commun. 211: 840-846.
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , pp. 840-846
    • Weinberg, R.B.1    Jones, J.B.2    Pritchard, P.H.3    Lacko, A.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.