메뉴 건너뛰기




Volumn 101, Issue 2, 2011, Pages 353-361

C-terminus of apolipoprotein A-I removes phospholipids from a triolein/phospholipids/water interface, but the N-terminus does not: A possible mechanism for nascent HDL assembly

Author keywords

[No Author keywords available]

Indexed keywords

1-PALMITOYL-2-OLEOYLPHOSPHATIDYLCHOLINE; 2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; APOLIPOPROTEIN A1; PEPTIDE; PHOSPHATIDYLCHOLINE; PHOSPHOLIPID; PRE BETA HIGH DENSITY LIPOPROTEIN; TRIOLEIN; WATER;

EID: 80052469074     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.03.055     Document Type: Article
Times cited : (20)

References (44)
  • 1
    • 42649134146 scopus 로고    scopus 로고
    • HDL, ABC Transporters, and Cholesterol Efflux: Implications for the Treatment of Atherosclerosis
    • DOI 10.1016/j.cmet.2008.03.001, PII S1550413108000727
    • A.R. Tall, and L. Yvan-Charvet N. Wang HDL, ABC transporters, and cholesterol efflux: implications for the treatment of atherosclerosis Cell Metab. 7 2008 365 375 (Pubitemid 351598023)
    • (2008) Cell Metabolism , vol.7 , Issue.5 , pp. 365-375
    • Tall, A.R.1    Yvan-Charvet, L.2    Terasaka, N.3    Pagler, T.4    Wang, N.5
  • 2
    • 57349114776 scopus 로고    scopus 로고
    • HDL: Bridging past and present with a look at the future
    • A.M. Scanu, and C. Edelstein HDL: bridging past and present with a look at the future FASEB J. 22 2008 4044 4054
    • (2008) FASEB J. , vol.22 , pp. 4044-4054
    • Scanu, A.M.1    Edelstein, C.2
  • 4
    • 0026523122 scopus 로고
    • The amphipathic helix in the exchangeable apolipoproteins: A review of secondary structure and function
    • J.P. Segrest, and M.K. Jones G.M. Anantharamaiah The amphipathic helix in the exchangeable apolipoproteins: a review of secondary structure and function J. Lipid Res. 33 1992 141 166
    • (1992) J. Lipid Res. , vol.33 , pp. 141-166
    • Segrest, J.P.1    Jones, M.K.2    Anantharamaiah, G.M.3
  • 5
    • 0030820806 scopus 로고    scopus 로고
    • The carboxyl-terminal hydrophobic residues of apolipoprotein A-I affect its rate of phospholipid binding and its association with high density lipoprotein
    • DOI 10.1074/jbc.272.28.17511
    • M. Laccotripe, and S.C. Makrides V.I. Zannis The carboxyl-terminal hydrophobic residues of apolipoprotein A-I affect its rate of phospholipid binding and its association with high density lipoprotein J. Biol. Chem. 272 1997 17511 17522 (Pubitemid 27311184)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.28 , pp. 17511-17522
    • Laccotripe, M.1    Makrides, S.C.2    Jonas, A.3    Zannis, V.I.4
  • 6
    • 33846988253 scopus 로고    scopus 로고
    • Conformation and lipid binding of a C-terminal (198-243) peptide of human apolipoprotein A-I
    • H.L. Zhu, and D. Atkinson Conformation and lipid binding of a C-terminal (198-243) peptide of human apolipoprotein A-I Biochemistry 46 2007 1624 1634
    • (2007) Biochemistry , vol.46 , pp. 1624-1634
    • Zhu, H.L.1    Atkinson, D.2
  • 7
    • 20544444749 scopus 로고    scopus 로고
    • A mass spectrometric determination of the conformation of dimeric apolipoprotein A-I in discoidal high density lipoproteins
    • DOI 10.1021/bi050421z
    • R.A. Silva, and G.M. Hilliard W.S. Davidson A mass spectrometric determination of the conformation of dimeric apolipoprotein A-I in discoidal high density lipoproteins Biochemistry 44 2005 8600 8607 (Pubitemid 40840425)
    • (2005) Biochemistry , vol.44 , Issue.24 , pp. 8600-8607
    • Silva, R.A.G.D.1    Hilliard, G.M.2    Li, L.3    Segrest, J.P.4    Davidson, W.S.5
  • 9
    • 0037165652 scopus 로고    scopus 로고
    • Heteronuclear NMR studies of human serum apolipoprotein A-I: Part I. Secondary structure in lipid-mimetic solution
    • DOI 10.1016/S0014-5793(02)02600-5, PII S0014579302026005
    • M. Okon, and P.G. Frank R.J. Cushley Heteronuclear NMR studies of human serum apolipoprotein A-I. Part I. Secondary structure in lipid-mimetic solution FEBS Lett. 517 2002 139 143 (Pubitemid 34327646)
    • (2002) FEBS Letters , vol.517 , Issue.1-3 , pp. 139-143
    • Okon, M.1    Frank, P.G.2    Marcel, Y.L.3    Cushley, R.J.4
  • 10
    • 0022510143 scopus 로고
    • Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins
    • D.M. Engelman, T.A. Steitz, and A. Goldman Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins Annu. Rev. Biophys. Biophys. Chem. 15 1986 321 353
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 321-353
    • Engelman, D.M.1    Steitz, T.A.2    Goldman, A.3
  • 11
    • 0030005250 scopus 로고    scopus 로고
    • Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides
    • W.C. Wimley, T.P. Creamer, and S.H. White Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides Biochemistry 35 1996 5109 5124
    • (1996) Biochemistry , vol.35 , pp. 5109-5124
    • Wimley, W.C.1    Creamer, T.P.2    White, S.H.3
  • 12
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • DOI 10.1038/nsb1096-842
    • W.C. Wimley, and S.H. White Experimentally determined hydrophobicity scale for proteins at membrane interfaces Nat. Struct. Biol. 3 1996 842 848 (Pubitemid 26330634)
    • (1996) Nature Structural Biology , vol.3 , Issue.10 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 14
    • 33748645937 scopus 로고    scopus 로고
    • Contributions of the N- and C-terminal helical segments to the lipid-free structure and lipid interaction of apolipoprotein A-I
    • DOI 10.1021/bi060726t
    • M. Tanaka, and P. Dhanasekaran H. Saito Contributions of the N- and C-terminal helical segments to the lipid-free structure and lipid interaction of apolipoprotein A-I Biochemistry 45 2006 10351 10358 (Pubitemid 44384811)
    • (2006) Biochemistry , vol.45 , Issue.34 , pp. 10351-10358
    • Tanaka, M.1    Dhanasekaran, P.2    Nguyen, D.3    Ohta, S.4    Lund-Katz, S.5    Phillips, M.C.6    Saito, H.7
  • 15
    • 14344258702 scopus 로고    scopus 로고
    • A three-dimensional molecular model of lipid-free apolipoprotein A-I determined by cross-linking/mass spectrometry and sequence threading
    • DOI 10.1021/bi047717+
    • R.A.G.D. Silva, and G.M. Hilliard W.S. Davidson A three-dimensional molecular model of lipid-free apolipoprotein A-I determined by cross-linking/mass spectrometry and sequence threading Biochemistry 44 2005 2759 2769 (Pubitemid 40293652)
    • (2005) Biochemistry , vol.44 , Issue.8 , pp. 2759-2769
    • Silva, R.A.G.D.1    Hilliard, G.M.2    Fang, J.3    Macha, S.4    Davidson, W.S.5
  • 17
    • 35649022609 scopus 로고    scopus 로고
    • The N-terminal (1-44) and C-terminal (198-243) peptides of apolipoprotein A-I behave differently at the triolein/water interface
    • DOI 10.1021/bi7010114
    • L. Wang, and N. Hua D.M. Small The N-terminal (1-44) and C-terminal (198-243) peptides of apolipoprotein A-I behave differently at the triolein/water interface Biochemistry 46 2007 12140 12151 (Pubitemid 350022369)
    • (2007) Biochemistry , vol.46 , Issue.43 , pp. 12140-12151
    • Wang, L.1    Hua, N.2    Atkinson, D.3    Small, D.M.4
  • 18
    • 66349133111 scopus 로고    scopus 로고
    • The adsorption of biological peptides and proteins at the oil/water interface. A potentially important but largely unexplored field
    • D.M. Small, L.B. Wang, and M.A. Mitsche The adsorption of biological peptides and proteins at the oil/water interface. A potentially important but largely unexplored field J. Lipid Res. 50 Suppl 2009 S329 S334
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL
    • Small, D.M.1    Wang, L.B.2    Mitsche, M.A.3
  • 19
    • 0026736891 scopus 로고
    • Conformational analysis of apolipoprotein A-I and E-3 based on primary sequence and circular dichroism
    • R.T. Nolte, and D. Atkinson Conformational analysis of apolipoprotein A-I and E-3 based on primary sequence and circular dichroism Biophys. J. 63 1992 1221 1239 (Pubitemid 23004470)
    • (1992) Biophysical Journal , vol.63 , Issue.5 , pp. 1221-1239
    • Nolte, R.T.1    Atkinson, D.2
  • 20
    • 5444226264 scopus 로고    scopus 로고
    • Conformation and lipid binding of the N-terminal (1-44) domain of human apolipoprotein A-I
    • DOI 10.1021/bi0487894
    • H.L. Zhu, and D. Atkinson Conformation and lipid binding of the N-terminal (1-44) domain of human apolipoprotein A-I Biochemistry 43 2004 13156 13164 (Pubitemid 39362784)
    • (2004) Biochemistry , vol.43 , Issue.41 , pp. 13156-13164
    • Zhu, H.L.1    Atkinson, D.2
  • 21
    • 54849438885 scopus 로고    scopus 로고
    • Conformational flexibility of the N-terminal domain of apolipoprotein A-I bound to spherical lipid particles
    • M. Kono, and Y. Okumura H. Saito Conformational flexibility of the N-terminal domain of apolipoprotein A-I bound to spherical lipid particles Biochemistry 47 2008 11340 11347
    • (2008) Biochemistry , vol.47 , pp. 11340-11347
    • Kono, M.1    Okumura, Y.2    Saito, H.3
  • 23
    • 0033796912 scopus 로고    scopus 로고
    • Dynamic interfacial properties of human apolipoproteins A-IV and B-17 at the air/water and oil/water interface
    • R.B. Weinberg, and V.R. Cook G.S. Shelness Dynamic interfacial properties of human apolipoproteins A-IV and B-17 at the air/water and oil/water interface J. Lipid Res. 41 2000 1419 1427
    • (2000) J. Lipid Res. , vol.41 , pp. 1419-1427
    • Weinberg, R.B.1    Cook, V.R.2    Shelness, G.S.3
  • 24
    • 0026808542 scopus 로고
    • Adsorption of apolipoprotein A-IV to phospholipid monolayers spread at the air/water interface. A model for its labile binding to high density lipoproteins
    • R.B. Weinberg, J.A. Ibdah, and M.C. Phillips Adsorption of apolipoprotein A-IV to phospholipid monolayers spread at the air/water interface. A model for its labile binding to high density lipoproteins J. Biol. Chem. 267 1992 8977 8983
    • (1992) J. Biol. Chem. , vol.267 , pp. 8977-8983
    • Weinberg, R.B.1    Ibdah, J.A.2    Phillips, M.C.3
  • 25
    • 0023911492 scopus 로고
    • A comparison of the surface activities of human apolipoproteins A-I and A-II at the air/water interface
    • K.E. Krebs, J.A. Ibdah, and M.C. Phillips A comparison of the surface activities of human apolipoproteins A-I and A-II at the air/water interface Biochim. Biophys. Acta 959 1988 229 237
    • (1988) Biochim. Biophys. Acta , vol.959 , pp. 229-237
    • Krebs, K.E.1    Ibdah, J.A.2    Phillips, M.C.3
  • 26
    • 0022556094 scopus 로고
    • Studies of apolipoproteins at the air-water interface
    • M.C. Phillips, and K.E. Krebs Studies of apolipoproteins at the air-water interface Methods Enzymol. 128 1986 387 403 (Pubitemid 16100906)
    • (1986) Methods in Enzymology , vol.128 , pp. 387-403
    • Phillips, M.C.1    Krebs, K.E.2
  • 27
    • 14244252324 scopus 로고    scopus 로고
    • The interfacial properties of ApoA-I and an amphipathic α-helix consensus peptide of exchangeable apolipoproteins at the triolein/water interface
    • DOI 10.1074/bc.M411618200
    • L. Wang, D. Atkinson, and D.M. Small The interfacial properties of ApoA-I and an amphipathic α-helix consensus peptide of exchangeable apolipoproteins at the triolein/water interface J. Biol. Chem. 280 2005 4154 4165 (Pubitemid 40288580)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.6 , pp. 4154-4165
    • Wang, L.1    Atkinson, D.2    Small, D.M.3
  • 28
    • 33646488780 scopus 로고    scopus 로고
    • Apolipoprotein B is conformationally flexible but anchored at a triolein/water interface: A possible model for lipoprotein surfaces
    • L. Wang, M.T. Walsh, and D.M. Small Apolipoprotein B is conformationally flexible but anchored at a triolein/water interface: a possible model for lipoprotein surfaces Proc. Natl. Acad. Sci. USA 103 2006 6871 6876
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6871-6876
    • Wang, L.1    Walsh, M.T.2    Small, D.M.3
  • 29
    • 0141733182 scopus 로고    scopus 로고
    • Interfacial properties of an amphipathic α-helix consensus peptide of exchangeable apolipoproteins at air/water and oil/water interfaces
    • DOI 10.1074/jbc.M303133200
    • L.B. Wang, D. Atkinson, and D.M. Small Interfacial properties of an amphipathic α-helix consensus peptide of exchangeable apolipoproteins at air/water and oil/water interfaces J. Biol. Chem. 278 2003 37480 37491 (Pubitemid 37175269)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37480-37491
    • Wang, L.1    Atkinson, D.2    Small, D.M.3
  • 30
    • 63249111806 scopus 로고    scopus 로고
    • Interfacial properties of a complex multi-domain 490 amino acid peptide derived from apolipoprotein B (residues 292-782)
    • M.A. Mitsche, and L.B. Wang D.M. Small Interfacial properties of a complex multi-domain 490 amino acid peptide derived from apolipoprotein B (residues 292-782) Langmuir 25 2009 2322 2330
    • (2009) Langmuir , vol.25 , pp. 2322-2330
    • Mitsche, M.A.1    Wang, L.B.2    Small, D.M.3
  • 31
    • 63449132409 scopus 로고    scopus 로고
    • Structural and dynamic interfacial properties of the lipoprotein initiating domain of apolipoprotein B
    • A.S. Ledford, and V.A. Cook R.B. Weinberg Structural and dynamic interfacial properties of the lipoprotein initiating domain of apolipoprotein B J. Lipid Res. 50 2009 108 115
    • (2009) J. Lipid Res. , vol.50 , pp. 108-115
    • Ledford, A.S.1    Cook, V.A.2    Weinberg, R.B.3
  • 32
    • 4644246194 scopus 로고    scopus 로고
    • Interfacial properties of amphipathic β strand consensus peptides of apolipoprotein B at oil/water interfaces
    • DOI 10.1194/jlr.M400106-JLR200
    • L.B. Wang, and D.M. Small Interfacial properties of amphipathic β strand consensus peptides of apolipoprotein B at oil/water interfaces J. Lipid Res. 45 2004 1704 1715 (Pubitemid 39296210)
    • (2004) Journal of Lipid Research , vol.45 , Issue.9 , pp. 1704-1715
    • Wang, L.1    Small, D.M.2
  • 33
    • 77749334427 scopus 로고    scopus 로고
    • Adsorption of egg-PC to an air/water and triolein/water bubble interface: Use of the two-dimensional phase rule to estimate the surface composition of a phospholipid/triolein/water surface as a function of surface pressure
    • M.A. Mitsche, L. Wang, and D.M. Small Adsorption of egg-PC to an air/water and triolein/water bubble interface: use of the two-dimensional phase rule to estimate the surface composition of a phospholipid/triolein/water surface as a function of surface pressure J. Phys. Chem. B 114 2010 3276 3284
    • (2010) J. Phys. Chem. B , vol.114 , pp. 3276-3284
    • Mitsche, M.A.1    Wang, L.2    Small, D.M.3
  • 34
    • 49049139770 scopus 로고
    • The phase behavior of triolein, cholesterol, and lecithin emulsions
    • K.W. Miller, and D.M. Small The phase behavior of triolein, cholesterol, and lecithin emulsions J. Colloid Interf. Sci. 89 1982 466 477
    • (1982) J. Colloid Interf. Sci. , vol.89 , pp. 466-477
    • Miller, K.W.1    Small, D.M.2
  • 36
    • 33749317533 scopus 로고    scopus 로고
    • Defining lipid-interacting domains in the N-terminal region of apolipoprotein B
    • DOI 10.1021/bi060600w
    • Z.G. Jiang, and D. Gantz C.J. McKnight Defining lipid-interacting domains in the N-terminal region of apolipoprotein B Biochemistry 45 2006 11799 11808 (Pubitemid 44497807)
    • (2006) Biochemistry , vol.45 , Issue.39 , pp. 11799-11808
    • Jiang, Z.G.1    Gantz, D.2    Bullitt, E.3    McKnight, C.J.4
  • 38
    • 0025383223 scopus 로고
    • Automation of axisymmetric drop shape analysis for measurements of interfacial tensions and contact angles
    • DOI 10.1016/0166-6622(90)80286-D
    • P. Cheng, and D. Li A.W. Neumann Automation of axisymmetric drop shape-analysis for measurement of interfacial-tensions and contact angles Colloids Surf. 43 1990 151 167 (Pubitemid 20664065)
    • (1990) Colloids and surfaces , vol.43 , Issue.2-3 , pp. 151-167
    • Cheng, P.1    Li, D.2    Boruvka, L.3    Rotenberg, Y.4    Neumann, A.W.5
  • 40
    • 0037406006 scopus 로고    scopus 로고
    • Dynamics of surfactant sorption at the air/water interface: Continuous-flow tensiometry
    • DOI 10.1016/S0021-9797(02)00241-2
    • T.F. Svitova, M.J. Wetherbee, and C.J. Radke Dynamics of surfactant sorption at the air/water interface: continuous-flow tensiometry J. Colloid Interface Sci. 261 2003 170 179 (Pubitemid 36506550)
    • (2003) Journal of Colloid and Interface Science , vol.261 , Issue.1 , pp. 170-179
    • Svitova, T.F.1    Wetherbee, M.J.2    Radke, C.J.3
  • 42
    • 0018280233 scopus 로고
    • Plasma high-density lipoproteins
    • A.R. Tall, and D.M. Small Plasma high-density lipoproteins N. Engl. J. Med. 299 1978 1232 1236
    • (1978) N. Engl. J. Med. , vol.299 , pp. 1232-1236
    • Tall, A.R.1    Small, D.M.2
  • 43
    • 0018750544 scopus 로고
    • Quantitation of the transfer of surface phospholipid of chylomicrons to the high density lipoprotein fraction during the catabolism of chylomicrons in the rat
    • T.G. Redgrave, and D.M. Small Quantitation of the transfer of surface phospholipid of chylomicrons to the high density lipoprotein fraction during the catabolism of chylomicrons in the rat J. Clin. Invest. 64 1979 162 171 (Pubitemid 9216531)
    • (1979) Journal of Clinical Investigation , vol.64 , Issue.1 , pp. 162-171
    • Redgrave, T.G.1    Small, D.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.