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Volumn 249, Issue 3, 1997, Pages 708-715

Structural and functional properties of the 154-171 wild-type and variant peptides of human lecithin-cholesterol acyltransferase

Author keywords

Amphipathic helix; High density lipoprotein; Lecithin cholesterol acyltransferase; Lipid protein interaction; Phospholipid

Indexed keywords

PHOSPHATIDYLCHOLINE STEROL ACYLTRANSFERASE;

EID: 0030661982     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-2-00708.x     Document Type: Article
Times cited : (23)

References (52)
  • 1
    • 0025734840 scopus 로고
    • Lecithin-cholesterol acyltransferase deficiency and fish-eye disease
    • Assmann, G., von Eckardstein, A. & Funke, H. (1991) Lecithin-cholesterol acyltransferase deficiency and fish-eye disease, Curr. Opin. Lipidol. 2, 110-117.
    • (1991) Curr. Opin. Lipidol. , vol.2 , pp. 110-117
    • Assmann, G.1    Von Eckardstein, A.2    Funke, H.3
  • 2
    • 0026331991 scopus 로고
    • Localization of an apolipoprotein A-I epitope critical for activation of lecithin-cholesterol acyltransferase
    • Banka, C. L., Bonnet, A. S., Smith, R. S. & Curtiss, L. K. (1991) Localization of an apolipoprotein A-I epitope critical for activation of lecithin-cholesterol acyltransferase, J. Biol. Chem. 266, 23 886-23 892.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23886-23892
    • Banka, C.L.1    Bonnet, A.S.2    Smith, R.S.3    Curtiss, L.K.4
  • 3
    • 0024431290 scopus 로고
    • Reaction of lecithin cholesterol acyltransferase with water-soluble substrates
    • Bonelli, F. S. & Jonas, A. (1989) Reaction of lecithin cholesterol acyltransferase with water-soluble substrates. J. Biol. Chem. 264, 14723-14728.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14723-14728
    • Bonelli, F.S.1    Jonas, A.2
  • 4
    • 0023050209 scopus 로고
    • Conformation and mode of organization of amphiphilic membrane components: A conformational analysis
    • Brasseur, R. & Ruysschaert, J. M. (1986) Conformation and mode of organization of amphiphilic membrane components: a conformational analysis, Biochem. J. 238, 1-11.
    • (1986) Biochem. J. , vol.238 , pp. 1-11
    • Brasseur, R.1    Ruysschaert, J.M.2
  • 6
    • 0025936242 scopus 로고
    • Differentiation of lipid-associating helices by use of three-dimensional molecular hydrophobicity potential calculations
    • Brasseur, R. (1991) Differentiation of lipid-associating helices by use of three-dimensional molecular hydrophobicity potential calculations, J. Biol. Chem. 266, 16 120-16 127.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16120-16127
    • Brasseur, R.1
  • 9
    • 0020526487 scopus 로고
    • Characterization of lecithin:cholesterol acyltransferase from human plasma. II. Physical properties of the enzyme
    • Chong, K. S., Hara, S., Thompson, R. K. & Lacko, A. G. (1983) Characterization of lecithin:cholesterol acyltransferase from human plasma. II. Physical properties of the enzyme, Arch. Biochem. Biophys. 222, 553-560.
    • (1983) Arch. Biochem. Biophys. , vol.222 , pp. 553-560
    • Chong, K.S.1    Hara, S.2    Thompson, R.K.3    Lacko, A.G.4
  • 10
    • 0022474744 scopus 로고
    • Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
    • Compton, L. A. & Johnson, W. C. Jr (1986) Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication, Anal. Biochem. 155, 155-167.
    • (1986) Anal. Biochem. , vol.155 , pp. 155-167
    • Compton, L.A.1    Johnson Jr., W.C.2
  • 11
    • 0020649886 scopus 로고
    • Establishing homologies in protein sequences
    • Dayhoff, M. O., Barker, W. C. & Hunt, L. T. (1983) Establishing homologies in protein sequences. Methods Enzymol. 91, 524-544.
    • (1983) Methods Enzymol. , vol.91 , pp. 524-544
    • Dayhoff, M.O.1    Barker, W.C.2    Hunt, L.T.3
  • 12
    • 0022550987 scopus 로고
    • Hydrophobicity profiles for detection of receptor binding domains on apolipoprotein E and the low density lipoprotein apolipoprotein(B-E) receptor
    • De Loof, H., Rosseneu, M., Brasseur, R. & Ruysschaert, J. M. (1986) Hydrophobicity profiles for detection of receptor binding domains on apolipoprotein E and the low density lipoprotein apolipoprotein(B-E) receptor, Proc. Natl Acad. Sci. USA 83, 2295-2299.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 2295-2299
    • De Loof, H.1    Rosseneu, M.2    Brasseur, R.3    Ruysschaert, J.M.4
  • 13
    • 0029101725 scopus 로고
    • Lipid binding and lecithin cholesterol acyl transferase activation by the IO and 22 kDa fragments of apo E3 and its Thr57-Cys variant
    • De Pauw, M., Vanloo, B., Weisgraber, K. & Rosseneu, M. (1995) Lipid binding and lecithin cholesterol acyl transferase activation by the IO and 22 kDa fragments of apo E3 and its Thr57-Cys variant, Biochemistry 34, 10953-10960.
    • (1995) Biochemistry , vol.34 , pp. 10953-10960
    • De Pauw, M.1    Vanloo, B.2    Weisgraber, K.3    Rosseneu, M.4
  • 14
    • 0020519746 scopus 로고
    • Microheterogeneity and physical properties of human lecithin:cholesterol acyltransferase
    • Doi, Y. & Nishida, T. (1983) Microheterogeneity and physical properties of human lecithin:cholesterol acyltransferase, J. Biol. Chem. 258, 5840-5846.
    • (1983) J. Biol. Chem. , vol.258 , pp. 5840-5846
    • Doi, Y.1    Nishida, T.2
  • 15
    • 0002473020 scopus 로고
    • Lipolytic enzymes and the role of apolipoproteins in the regulation of their activity
    • Rosseneu, M., ed. CRC, Boca-Raton
    • Dolphin, P. J. (1992) Lipolytic enzymes and the role of apolipoproteins in the regulation of their activity, in Structure and function of plasma apolipoproteins (Rosseneu, M., ed.) pp. 295-362, CRC, Boca-Raton.
    • (1992) Structure and Function of Plasma Apolipoproteins , pp. 295-362
    • Dolphin, P.J.1
  • 16
    • 9844265362 scopus 로고
    • Identification of a novel mutation in the LCAT gene resulting in fish-eye disease with alpha-LCAT activity
    • Abstr.
    • Duverger, N., Klein, H. G., Luc, G., Fruchart, J. C., Albers, J. J. & Brewer, H. B. Jr (1993) Identification of a novel mutation in the LCAT gene resulting in fish-eye disease with alpha-LCAT activity, Circulation 88, I-423 no. 2274 (Abstr.).
    • (1993) Circulation , vol.88 , Issue.2274
    • Duverger, N.1    Klein, H.G.2    Luc, G.3    Fruchart, J.C.4    Albers, J.J.5    Brewer Jr., H.B.6
  • 17
    • 0019934717 scopus 로고
    • The helical hydrophobic moment: A measure of the amphiphilicity of a helix
    • Eisenberg, D., Weiss, R. M. & Terwilliger, T. C. (1982) The helical hydrophobic moment: a measure of the amphiphilicity of a helix, Nature 299, 371-374.
    • (1982) Nature , vol.299 , pp. 371-374
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 20
    • 0001965939 scopus 로고
    • Lecithin cholesterol acyltransferase
    • Esfahani, M. & Swaney, J. B., eds Telford Press, Caldwell NY
    • Fielding, C. J. (1990) Lecithin cholesterol acyltransferase in Advances in cholesterol research (Esfahani, M. & Swaney, J. B., eds) pp. 271-314, Telford Press, Caldwell NY.
    • (1990) Advances in Cholesterol Research , pp. 271-314
    • Fielding, C.J.1
  • 21
    • 0028887870 scopus 로고
    • Molecular physiology of reverse cholesterol transport
    • Fielding, C. J. & Fielding, P. E. (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
  • 22
    • 0025836742 scopus 로고
    • Structure-function relationships in human lecithin cholesterol acyltransferase. Site-directed mutagenesis at serine residues 181 and 216
    • Francone, O. L. & Fielding, C. J. (1991) Structure-function relationships in human lecithin cholesterol acyltransferase. Site-directed mutagenesis at serine residues 181 and 216, Biochemistry 30, 10074-10077.
    • (1991) Biochemistry , vol.30 , pp. 10074-10077
    • Francone, O.L.1    Fielding, C.J.2
  • 23
    • 0018787059 scopus 로고
    • Stability and properties of lecithin-cholesterol acyltransferase
    • Furukawa, Y. & Nishida, T. (1979) Stability and properties of lecithin-cholesterol acyltransferase. J. Biol. Chem. 254, 7213-7219.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7213-7219
    • Furukawa, Y.1    Nishida, T.2
  • 24
    • 0014264541 scopus 로고
    • The plasma LCAT reaction
    • Glomset, J. A. (1968) The plasma LCAT reaction, J. Lipid Res. 9, 155-167.
    • (1968) J. Lipid Res. , vol.9 , pp. 155-167
    • Glomset, J.A.1
  • 25
    • 0024234855 scopus 로고
    • CLUSTAL: A package for performing mutiple sequence alignment on a microcomputer
    • Amst.
    • Higgins, D. G. & Sharp, P. M. (1988) CLUSTAL: a package for performing mutiple sequence alignment on a microcomputer, Gene (Amst.) 73, 237-244.
    • (1988) Gene , vol.73 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 27
    • 0029048822 scopus 로고
    • Properties of an N-terminal proteolytic fragment of apolipoprotein A-I in solution and in reconstituted high density lipoproteins
    • Ji, Y. & Jonas, A. (1995) Properties of an N-terminal proteolytic fragment of apolipoprotein A-I in solution and in reconstituted high density lipoproteins. J. Biol. Chem. 270, 11 290-11 297.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11290-11297
    • Ji, Y.1    Jonas, A.2
  • 28
    • 0025900794 scopus 로고
    • Lecithin-cholesterol acyltransferase in the metabolism of high-density lipoproteins
    • Jonas, A. (1991) Lecithin-cholesterol acyltransferase in the metabolism of high-density lipoproteins, Biochim. Biophys. Acta 1084, 205-219.
    • (1991) Biochim. Biophys. Acta , vol.1084 , pp. 205-219
    • Jonas, A.1
  • 30
    • 0030933460 scopus 로고    scopus 로고
    • The molecular pathology of lecithin:cholesterol acyltransferase (LCAT) deficiency syndromes
    • Kuivenhoven, J. A., Pritchard, H., Frohlich, J., Assmann, G. & Kastelein, J. (1997) The molecular pathology of lecithin:cholesterol acyltransferase (LCAT) deficiency syndromes, J. Lipid Res. 38, 191-205.
    • (1997) J. Lipid Res. , vol.38 , pp. 191-205
    • Kuivenhoven, J.A.1    Pritchard, H.2    Frohlich, J.3    Assmann, G.4    Kastelein, J.5
  • 31
    • 0010983249 scopus 로고    scopus 로고
    • The C-terminal helix of human apolipoprotein A-II promotes the fusion of unilamellar liposomes and displaces apolipoprotein A-I from high density lipoproteins
    • in the press
    • Lambert, G., Decout, A., Vanloo, B., Rouy, D., Duverger, N., Kalopissis, A., Vandekerckhove, J., Chambaz, J., Brasseur, R. & Rosseneu, M. (1997) The C-terminal helix of human apolipoprotein A-II promotes the fusion of unilamellar liposomes and displaces apolipoprotein A-I from high density lipoproteins. Biochemistry, in the press.
    • (1997) Biochemistry
    • Lambert, G.1    Decout, A.2    Vanloo, B.3    Rouy, D.4    Duverger, N.5    Kalopissis, A.6    Vandekerckhove, J.7    Chambaz, J.8    Brasseur, R.9    Rosseneu, M.10
  • 33
    • 0022556093 scopus 로고
    • Thermodynamics of apolipoprotein-phospholipid association
    • Massey, J. B. & Pownall, H. J. (1986) Thermodynamics of apolipoprotein-phospholipid association, Methods Enzymol. 128, 403-413.
    • (1986) Methods Enzymol. , vol.128 , pp. 403-413
    • Massey, J.B.1    Pownall, H.J.2
  • 34
    • 0020490523 scopus 로고
    • Micellar complexes of human apo A-I with phosphatidylcholines and cholesterol prepared from cholatelipid dispersions
    • Matz, C. E. & Jonas, A. (1982) Micellar complexes of human apo A-I with phosphatidylcholines and cholesterol prepared from cholatelipid dispersions, J. Biol. Chem. 257, 4535-4540.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4535-4540
    • Matz, C.E.1    Jonas, A.2
  • 35
    • 0027519147 scopus 로고
    • Apolipoprotein A-I domains involved in the activation of lecithin-cholesterol acyltransferase activation
    • Meng, Q. H., Calabresi, L., Fruchart, J. C. & Marcel, Y. L. (1993) Apolipoprotein A-I domains involved in the activation of lecithin-cholesterol acyltransferase activation, J. Biol. Chem. 268, 1596-1602.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1596-1602
    • Meng, Q.H.1    Calabresi, L.2    Fruchart, J.C.3    Marcel, Y.L.4
  • 36
    • 0026712240 scopus 로고
    • Site-directed mutagenesis and structure-function analysis of human apolipoprotein A-I: Relation between LCAT activation and lipid binding
    • Minnich, A., Collet, X., Roghani, A., Cladaras, C., Hamilton, R. L., Fielding, C. J. & Zannis, V. I. (1992) Site-directed mutagenesis and structure-function analysis of human apolipoprotein A-I: relation between LCAT activation and lipid binding, J. Biol. Chem. 267, 25 830-25 838.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25830-25838
    • Minnich, A.1    Collet, X.2    Roghani, A.3    Cladaras, C.4    Hamilton, R.L.5    Fielding, C.J.6    Zannis, V.I.7
  • 37
    • 0015937178 scopus 로고
    • Interaction of an apolipoprotein (ApoLP-Alanine) with phosphatidylcholine
    • Morrisett, J. D., David, J. S. K., Pownall, H. J. & Gotto, A. M. Jr (1973) Interaction of an apolipoprotein (ApoLP-Alanine) with phosphatidylcholine, Biochemistry 12, 1290-1299.
    • (1973) Biochemistry , vol.12 , pp. 1290-1299
    • Morrisett, J.D.1    David, J.S.K.2    Pownall, H.J.3    Gotto Jr., A.M.4
  • 38
    • 0002380717 scopus 로고
    • Familial lecithin:cholesterol acyltransferase deficiency, including fish eye disease
    • Scriver, C. R., Beaudet, A. L., Sly, W. S. & Valle, D., eds McGraw-Hill Inc., New York
    • Norum, K. R., Gjone, E. & Glomset, J. A. (1989) Familial lecithin:cholesterol acyltransferase deficiency, including fish eye disease, in The metabolic basis of inherited disease (Scriver, C. R., Beaudet, A. L., Sly, W. S. & Valle, D., eds) pp. 1181-1194, McGraw-Hill Inc., New York.
    • (1989) The Metabolic Basis of Inherited Disease , pp. 1181-1194
    • Norum, K.R.1    Gjone, E.2    Glomset, J.A.3
  • 39
    • 0030047675 scopus 로고    scopus 로고
    • Only the two end helixes of eight tandem amphipathic helical domains of human apo A-I have significant lipid affinity. Implications for HDL assembly
    • Palgunachari, M. N., Mishra, V. K., Lund-Katz, S., Phillips, M. C., Adeyeye, S. O., Alluri, S., Anantharamaiah, G. M. & Segrest, J. P. (1996) Only the two end helixes of eight tandem amphipathic helical domains of human apo A-I have significant lipid affinity. Implications for HDL assembly, Arteriosclerosis 16, 328-338.
    • (1996) Arteriosclerosis , vol.16 , pp. 328-338
    • Palgunachari, M.N.1    Mishra, V.K.2    Lund-Katz, S.3    Phillips, M.C.4    Adeyeye, S.O.5    Alluri, S.6    Anantharamaiah, G.M.7    Segrest, J.P.8
  • 40
    • 0029047044 scopus 로고
    • In vitro expression of natural variants of human lecithin cholesterol acyltransferase
    • Qu, S. J., Fan, H. Z., Blanco-Vaca, F. & Pownall, H. (1995) In vitro expression of natural variants of human lecithin cholesterol acyltransferase, J. Lipid Res. 36, 967-973.
    • (1995) J. Lipid Res. , vol.36 , pp. 967-973
    • Qu, S.J.1    Fan, H.Z.2    Blanco-Vaca, F.3    Pownall, H.4
  • 41
    • 0017446960 scopus 로고
    • Amphipathic helices and plasma lipoproteins: Thermodynamic and geometric considerations
    • Segrest, J. P. (1977) Amphipathic helices and plasma lipoproteins: thermodynamic and geometric considerations, Chem. Phys. Lipids 18, 7-22.
    • (1977) Chem. Phys. Lipids , vol.18 , pp. 7-22
    • Segrest, J.P.1
  • 42
    • 0027384540 scopus 로고
    • Apolipoprotein A-I domains involved in lecithin-cholesterol acyltransferase activation
    • Sorci-Thomas, M., Kearns, M. W. & Lee, J. P. (1993) Apolipoprotein A-I domains involved in lecithin-cholesterol acyltransferase activation, J. Biol. Chem. 268, 21403-21409.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21403-21409
    • Sorci-Thomas, M.1    Kearns, M.W.2    Lee, J.P.3
  • 43
    • 0016814761 scopus 로고
    • Effect of the human plasma apolipoproteins and phosphatidylcholine acyl donor on the activity of lecithin:cholesterol acyltransferase
    • Soutar, A. K., Garner, C. W., Baker, H. N., Sparrow, J. T., Jackson, R. L., Gotto, A. M. & Smith, L. C. (1975) Effect of the human plasma apolipoproteins and phosphatidylcholine acyl donor on the activity of lecithin:cholesterol acyltransferase, Biochemistry 14, 3057-3064.
    • (1975) Biochemistry , vol.14 , pp. 3057-3064
    • Soutar, A.K.1    Garner, C.W.2    Baker, H.N.3    Sparrow, J.T.4    Jackson, R.L.5    Gotto, A.M.6    Smith, L.C.7
  • 45
    • 0027065504 scopus 로고
    • G-To F-actin modulation by single amino acid substitution in the actin binding site of actobindin and thymosine β 4
    • Vancompernolle, K., Goethals, M., Huet, C., Louvard, D. & Vandekerckhove, J. (1992) G-To F-actin modulation by single amino acid substitution in the actin binding site of actobindin and thymosine β 4, EMBO J. 11, 4739-4746.
    • (1992) EMBO J. , vol.11 , pp. 4739-4746
    • Vancompernolle, K.1    Goethals, M.2    Huet, C.3    Louvard, D.4    Vandekerckhove, J.5
  • 48
    • 0031024677 scopus 로고    scopus 로고
    • Ammo acid residue 149 of lecithin cholesterol acyltansferase determines phospholipase A2 and transacylase fatty acyl specificity
    • Wang, J. C., Gebre, A. K., Anderson, R. A. & Parks, J. S. (1997) Ammo acid residue 149 of lecithin cholesterol acyltansferase determines phospholipase A2 and transacylase fatty acyl specificity, J. Biol. Chem. 272, 280-286.
    • (1997) J. Biol. Chem. , vol.272 , pp. 280-286
    • Wang, J.C.1    Gebre, A.K.2    Anderson, R.A.3    Parks, J.S.4
  • 49
    • 0029017707 scopus 로고
    • Effect of interfacial pressure on the binding and phospholipase A2 activity of recombinant human lecithin-cholesterol acyltransferase
    • Weinberg, R. B., Jones, J. B., Pritchard, P. H. & Lacko, A. G. (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
  • 50
    • 0027186135 scopus 로고
    • Discrete carboxy-terminal segments of apolipoprotein E mediate lipoprotein association and protein oligomerization
    • Westerlund, J. A. & Weisgraber, K. H. (1993) Discrete carboxy-terminal segments of apolipoprotein E mediate lipoprotein association and protein oligomerization, J. Biol. Chem. 268, 15 745-15 750.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15745-15750
    • Westerlund, J.A.1    Weisgraber, K.H.2
  • 51
    • 0023900109 scopus 로고
    • Human apolipoprotein E3 in aqueous solution. I. Evidence for two structural domains
    • Wetterau, J. R., Aggerbeck, L. P., Rall, S. C. Jr & Weisgraber, K. H. (1988) Human apolipoprotein E3 in aqueous solution. I. Evidence for two structural domains, J. Biol. Chem. 263, 6240-6248.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6240-6248
    • Wetterau, J.R.1    Aggerbeck, L.P.2    Rall Jr., S.C.3    Weisgraber, K.H.4
  • 52
    • 0020632431 scopus 로고
    • Interaction of lecithin-cholesterol acyltransferase with human plasma lipoproteins and with lecithin-cholesterol vesicles
    • Yamazaki, S., Mitsunaga, T., Furukawa, Y. & Nishida, T. (1983) Interaction of lecithin-cholesterol acyltransferase with human plasma lipoproteins and with lecithin-cholesterol vesicles, J. Biol. Chem. 258, 5847-5853.
    • (1983) J. Biol. Chem. , vol.258 , pp. 5847-5853
    • Yamazaki, S.1    Mitsunaga, T.2    Furukawa, Y.3    Nishida, T.4


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