메뉴 건너뛰기




Volumn 49, Issue 11, 2008, Pages 2419-2426

Conformational change of apolipoprotein A-I and HDL formation from model membranes under intracellular acidic conditions

Author keywords

Endosome; Golgi; Phosphatidylcholine; Phosphatidylserine; Reconstituted HDL; Translocase activity

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ABC TRANSPORTER A1; APOLIPOPROTEIN A1; HIGH DENSITY LIPOPROTEIN; LIPOSOME; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLSERINE; HIGH DENSITY LIPOPROTEIN CHOLESTEROL; PRE BETA HIGH DENSITY LIPOPROTEIN;

EID: 58149469594     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.M800287-JLR200     Document Type: Article
Times cited : (24)

References (53)
  • 1
    • 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
  • 2
    • 0016433018 scopus 로고
    • Plasma-high-density-lipoprotein concentration and development of ischaemic heart-disease
    • Miller, G. J., and N. E. Miller. 1975. Plasma-high-density-lipoprotein concentration and development of ischaemic heart-disease. Lancet. 1: 16-19.
    • (1975) Lancet , vol.1 , pp. 16-19
    • Miller, G.J.1    Miller, N.E.2
  • 4
    • 14744302026 scopus 로고    scopus 로고
    • ATP-binding cassette transporter AI and its role in HDL formation
    • Lee, J. Y., and J. S. Parks. 2005. ATP-binding cassette transporter AI and its role in HDL formation. Curr. Opin. Lipidol. 16: 19-25.
    • (2005) Curr. Opin. Lipidol , vol.16 , pp. 19-25
    • Lee, J.Y.1    Parks, J.S.2
  • 5
    • 33144485711 scopus 로고    scopus 로고
    • Crystal structure of human apolipoprotein A-I: Insights into its protective effect against cardiovascular diseases
    • Ajees, A. A., G. M. Anantharamaiah, V. K. Mishra, M. M. Hussain, and H. M. Murthy. 2006. Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases. Proc. Natl. Acad. Sci. USA. 103: 2126-2131.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 2126-2131
    • Ajees, A.A.1    Anantharamaiah, G.M.2    Mishra, V.K.3    Hussain, M.M.4    Murthy, H.M.5
  • 7
    • 0030732162 scopus 로고    scopus 로고
    • Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation
    • Borhani, D. W., D. P. Rogers, J. A. Engler, and C. G. Brouillette. 1997. Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Proc. Natl. Acad. Sci. USA. 94: 12291-12296.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12291-12296
    • Borhani, D.W.1    Rogers, D.P.2    Engler, J.A.3    Brouillette, C.G.4
  • 9
    • 25444463073 scopus 로고    scopus 로고
    • ATP-binding cassette transporter A1: A cell cholesterol exporter that protects against cardiovascular disease
    • Oram, J. F., and J. W. Heinecke. 2005. ATP-binding cassette transporter A1: a cell cholesterol exporter that protects against cardiovascular disease. Physiol. Rev. 85: 1343-1372.
    • (2005) Physiol. Rev , vol.85 , pp. 1343-1372
    • Oram, J.F.1    Heinecke, J.W.2
  • 13
    • 1342282993 scopus 로고    scopus 로고
    • Phosphorylation and stabilization of ATP binding cassette transporter A1 by synthetic amphiphilic helical peptides
    • Arakawa, R., M. Hayashi, A. T. Remaley, B. H. Brewer, Y. Yamauchi, and S. Yokoyama. 2004. Phosphorylation and stabilization of ATP binding cassette transporter A1 by synthetic amphiphilic helical peptides. J. Biol. Chem. 279: 6217-6220.
    • (2004) J. Biol. Chem , vol.279 , pp. 6217-6220
    • Arakawa, R.1    Hayashi, M.2    Remaley, A.T.3    Brewer, B.H.4    Yamauchi, Y.5    Yokoyama, S.6
  • 14
    • 34548364160 scopus 로고    scopus 로고
    • Mechanism of ATP-binding cassette transporter A1-mediated cellular lipid efflux to apolipoprotein A-I and formation of high density lipoprotein particles
    • Vedhachalam, C., P. T. Duong, M. Nickel, D. Nguyen, P. Dhanasekaran, H. Saito, G. H. Rothblat, S. Lund-Katz, and M. C. Phillips. 2007. Mechanism of ATP-binding cassette transporter A1-mediated cellular lipid efflux to apolipoprotein A-I and formation of high density lipoprotein particles. J. Biol. Chem. 282: 25123-25130.
    • (2007) J. Biol. Chem , vol.282 , pp. 25123-25130
    • Vedhachalam, C.1    Duong, P.T.2    Nickel, M.3    Nguyen, D.4    Dhanasekaran, P.5    Saito, H.6    Rothblat, G.H.7    Lund-Katz, S.8    Phillips, M.C.9
  • 16
    • 28844508568 scopus 로고    scopus 로고
    • Intracellular lipidation of newly synthesized apolipoprotein A-I in primary murine hepatocytes
    • Maric, J., R. S. Kiss, V. Franklin, and Y. L. Marcel. 2005. Intracellular lipidation of newly synthesized apolipoprotein A-I in primary murine hepatocytes. J. Biol. Chem. 280: 39942-39949.
    • (2005) J. Biol. Chem , vol.280 , pp. 39942-39949
    • Maric, J.1    Kiss, R.S.2    Franklin, V.3    Marcel, Y.L.4
  • 18
    • 0037124089 scopus 로고    scopus 로고
    • Evaluation of the role of phosphatidylserine translocase activity in ABCA1-mediated lipid efflux
    • Smith, J. D., C. Waelde, A. Horwitz, and P. Zheng. 2002. Evaluation of the role of phosphatidylserine translocase activity in ABCA1-mediated lipid efflux. J. Biol. Chem. 277: 17797-17803.
    • (2002) J. Biol. Chem , vol.277 , pp. 17797-17803
    • Smith, J.D.1    Waelde, C.2    Horwitz, A.3    Zheng, P.4
  • 19
    • 0033613166 scopus 로고    scopus 로고
    • Cholesterol efflux to apolipoprotein AI involves endocytosis and resecretion in a calciumdependent pathway
    • Takahashi, Y., and J. D. Smith. 1999. Cholesterol efflux to apolipoprotein AI involves endocytosis and resecretion in a calciumdependent pathway. Proc. Natl. Acad. Sci. USA. 96: 11358-11363.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11358-11363
    • Takahashi, Y.1    Smith, J.D.2
  • 20
    • 23844485910 scopus 로고    scopus 로고
    • A PEST deletion mutant of ABCA1 shows impaired internalization and defective cholesterol efflux from late endosomes
    • Chen, W., N. Wang, and A. R. Tall. 2005. A PEST deletion mutant of ABCA1 shows impaired internalization and defective cholesterol efflux from late endosomes. J. Biol. Chem. 280: 29277-29281.
    • (2005) J. Biol. Chem , vol.280 , pp. 29277-29281
    • Chen, W.1    Wang, N.2    Tall, A.R.3
  • 21
    • 0032499784 scopus 로고    scopus 로고
    • Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins
    • Llopis, J., J. M. McCaffery, A. Miyawaki, M. G. Farquhar, and R. Y. Tsien. 1998. Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins. Proc. Natl. Acad. Sci. USA. 95: 6803-6808.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6803-6808
    • Llopis, J.1    McCaffery, J.M.2    Miyawaki, A.3    Farquhar, M.G.4    Tsien, R.Y.5
  • 22
    • 0034647915 scopus 로고    scopus 로고
    • Determinants of the pH of the Golgi complex
    • Schapiro, F. B., and S. Grinstein. 2000. Determinants of the pH of the Golgi complex. J. Biol. Chem. 275: 21025-21032.
    • (2000) J. Biol. Chem , vol.275 , pp. 21025-21032
    • Schapiro, F.B.1    Grinstein, S.2
  • 23
    • 0033583073 scopus 로고    scopus 로고
    • Receptor-mediated targeting of fluorescent probes in living cells
    • Farinas, J., and A. S. Verkman. 1999. Receptor-mediated targeting of fluorescent probes in living cells. J. Biol. Chem. 274: 7603-7606.
    • (1999) J. Biol. Chem , vol.274 , pp. 7603-7606
    • Farinas, J.1    Verkman, A.S.2
  • 24
    • 0026949598 scopus 로고
    • The importance of being acid: The role of acidification in intracellular membrane traffic
    • Mellman, I. 1992. The importance of being acid: the role of acidification in intracellular membrane traffic. J. Exp. Biol. 172: 39-45.
    • (1992) J. Exp. Biol , vol.172 , pp. 39-45
    • Mellman, I.1
  • 25
    • 0022555867 scopus 로고
    • Acidification of the endocytic and exocytic pathways
    • Mellman, I., R. Fuchs, and A. Helenius. 1986. Acidification of the endocytic and exocytic pathways. Annu. Rev. Biochem. 55: 663-700.
    • (1986) Annu. Rev. Biochem , vol.55 , pp. 663-700
    • Mellman, I.1    Fuchs, R.2    Helenius, A.3
  • 26
    • 22144479426 scopus 로고    scopus 로고
    • A novel missense mutation in ABCA1 results in altered protein trafficking and reduced phosphatidylserine translocation in a patient with Scott syndrome
    • Albrecht, C., J. H. McVey, J. I. Elliott, A. Sardini, I. Kasza, A. D. Mumford, R. P. Naoumova, E. G. Tuddenham, K. Szabo, and C. F. Higgins. 2005. A novel missense mutation in ABCA1 results in altered protein trafficking and reduced phosphatidylserine translocation in a patient with Scott syndrome. Blood. 106: 542-549.
    • (2005) Blood , vol.106 , pp. 542-549
    • Albrecht, C.1    McVey, J.H.2    Elliott, J.I.3    Sardini, A.4    Kasza, I.5    Mumford, A.D.6    Naoumova, R.P.7    Tuddenham, E.G.8    Szabo, K.9    Higgins, C.F.10
  • 29
    • 0035914448 scopus 로고    scopus 로고
    • Endocytosis is enhanced in Tangier fibroblasts: Possible role of ATP-binding cassette protein A1 in endosomal vesicular transport
    • Zha, X., J. Genest, Jr., and R. McPherson. 2001. Endocytosis is enhanced in Tangier fibroblasts: possible role of ATP-binding cassette protein A1 in endosomal vesicular transport. J. Biol. Chem. 276: 39476-39483.
    • (2001) J. Biol. Chem , vol.276 , pp. 39476-39483
    • Zha, X.1    Genest Jr., J.2    McPherson, R.3
  • 31
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Bartlett, G. R. 1959. Phosphorus assay in column chromatography. J. Biol. Chem. 234: 466-468.
    • (1959) J. Biol. Chem , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 32
    • 0021017401 scopus 로고
    • Large divalent cations and electrostatic potentials adjacent to membranes. Experimental results with hexamethonium
    • Alvarez, O., M. Brodwick, R. Latorre, A. McLaughlin, S. McLaughlin, and G. Szabo. 1983. Large divalent cations and electrostatic potentials adjacent to membranes. Experimental results with hexamethonium. Biophys. J. 44: 333-342.
    • (1983) Biophys. J , vol.44 , pp. 333-342
    • Alvarez, O.1    Brodwick, M.2    Latorre, R.3    McLaughlin, A.4    McLaughlin, S.5    Szabo, G.6
  • 33
    • 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
    • Tanaka, M., P. Dhanasekaran, D. Nguyen, S. Ohta, S. Lund-Katz, M. C. Phillips, and H. Saito. 2006. Contributions of the N- and C-terminal helical segments to the lipid-free structure and lipid interaction of apolipoprotein A-I. Biochemistry. 45: 10351-10358.
    • (2006) Biochemistry , vol.45 , 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
  • 34
    • 0036689537 scopus 로고    scopus 로고
    • Structurefunction studies of apoA-I variants: Site-directed mutagenesis and natural mutations
    • Sviridov, D., A. Hoang, W. Huang, and J. Sasaki. 2002. Structurefunction studies of apoA-I variants: site-directed mutagenesis and natural mutations. J. Lipid Res. 43: 1283-1292.
    • (2002) J. Lipid Res , vol.43 , pp. 1283-1292
    • Sviridov, D.1    Hoang, A.2    Huang, W.3    Sasaki, J.4
  • 35
    • 0031028471 scopus 로고    scopus 로고
    • Apolipoprotein AI isoforms in serum determined by isoelectric focusing and immunoblotting
    • Contiero, E., R. Ferrari, G. M. Vaselli, and M. Folin. 1997. Apolipoprotein AI isoforms in serum determined by isoelectric focusing and immunoblotting. Electrophoresis. 18: 122-126.
    • (1997) Electrophoresis , vol.18 , pp. 122-126
    • Contiero, E.1    Ferrari, R.2    Vaselli, G.M.3    Folin, M.4
  • 36
    • 0017387917 scopus 로고
    • Structure and thermodynamic properties of high density lipoprotein recombinants
    • Tall, A. R., D. M. Small, R. J. Deckelbaum, and G. G. Shipley. 1977. Structure and thermodynamic properties of high density lipoprotein recombinants. J. Biol. Chem. 252: 4701-4711.
    • (1977) J. Biol. Chem , vol.252 , pp. 4701-4711
    • Tall, A.R.1    Small, D.M.2    Deckelbaum, R.J.3    Shipley, G.G.4
  • 37
    • 0017854716 scopus 로고
    • Kinetics of lipid-protein interactions: Interaction of apolipoprotein A-I from human plasma high density lipoproteins with phosphatidylcholines
    • Pownall, H. J., J. B. Massey, S. K. Kusserow, and A. M. Gotto, Jr. 1978. Kinetics of lipid-protein interactions: interaction of apolipoprotein A-I from human plasma high density lipoproteins with phosphatidylcholines. Biochemistry. 17: 1183-1188.
    • (1978) Biochemistry , vol.17 , pp. 1183-1188
    • Pownall, H.J.1    Massey, J.B.2    Kusserow, S.K.3    Gotto Jr., A.M.4
  • 38
    • 0018402975 scopus 로고
    • Kinetics of lipid-protein interactions: Effect of cholesterol on the association of human plasma high-density apolipoprotein A-I with L-alpha-dimyristoylphosphatidylcholine
    • Pownall, H. J., J. B. Massey, S. K. Kusserow, and A. M. Gotto, Jr. 1979. Kinetics of lipid-protein interactions: effect of cholesterol on the association of human plasma high-density apolipoprotein A-I with L-alpha-dimyristoylphosphatidylcholine. Biochemistry. 18: 574-579.
    • (1979) Biochemistry , vol.18 , pp. 574-579
    • Pownall, H.J.1    Massey, J.B.2    Kusserow, S.K.3    Gotto Jr., A.M.4
  • 39
    • 0019825953 scopus 로고
    • Kinetics and mechanism of association of human plasma apolipoproteins with dimyristoylphosphatidylcholine: Effect of protein structure and lipid clusters on reaction rates
    • Pownall, H., Q. Pao, D. Hickson, J. T. Sparrow, S. K. Kusserow, and J. B. Massey. 1981. Kinetics and mechanism of association of human plasma apolipoproteins with dimyristoylphosphatidylcholine: effect of protein structure and lipid clusters on reaction rates. Biochemistry. 20: 6630-6635.
    • (1981) Biochemistry , vol.20 , pp. 6630-6635
    • Pownall, H.1    Pao, Q.2    Hickson, D.3    Sparrow, J.T.4    Kusserow, S.K.5    Massey, J.B.6
  • 40
    • 34147113200 scopus 로고    scopus 로고
    • Spontaneous reconstitution of discoidal HDL from sphingomyelin-containing model membranes by apolipoprotein A-I
    • Fukuda, M., M. Nakano, S. Sriwongsitanont, M. Ueno, Y. Kuroda, and T. Handa. 2007. Spontaneous reconstitution of discoidal HDL from sphingomyelin-containing model membranes by apolipoprotein A-I. J. Lipid Res. 48: 882-889.
    • (2007) J. Lipid Res , vol.48 , pp. 882-889
    • Fukuda, M.1    Nakano, M.2    Sriwongsitanont, S.3    Ueno, M.4    Kuroda, Y.5    Handa, T.6
  • 41
    • 0022972981 scopus 로고
    • Human apolipoprotein A-I forms thermally stable complexes with anionic but not with zwitterionic phospholipids
    • Surewicz, W. K., R. M. Epand, H. J. Pownall, and S. W. Hui. 1986. Human apolipoprotein A-I forms thermally stable complexes with anionic but not with zwitterionic phospholipids. J. Biol. Chem. 261: 16191-16197.
    • (1986) J. Biol. Chem , vol.261 , pp. 16191-16197
    • Surewicz, W.K.1    Epand, R.M.2    Pownall, H.J.3    Hui, S.W.4
  • 42
    • 33645422479 scopus 로고    scopus 로고
    • The role of vesicular transport in ABCA1-dependent lipid efflux and its connection with NPC pathways
    • Boadu, E., and G. A. Francis. 2006. The role of vesicular transport in ABCA1-dependent lipid efflux and its connection with NPC pathways. J. Mol. Med. 84: 266-275.
    • (2006) J. Mol. Med , vol.84 , pp. 266-275
    • Boadu, E.1    Francis, G.A.2
  • 43
    • 0025784255 scopus 로고
    • Abnormal processing of Golgi elements and lysosomes in Tangier disease
    • Robenek, H., and G. Schmitz. 1991. Abnormal processing of Golgi elements and lysosomes in Tangier disease. Arterioscler. Thromb. 11: 1007-1020.
    • (1991) Arterioscler. Thromb , vol.11 , pp. 1007-1020
    • Robenek, H.1    Schmitz, G.2
  • 45
    • 0030481717 scopus 로고    scopus 로고
    • Apolipoprotein-mediated cellular cholesterol and phospholipid efflux depend on a functional Golgi apparatus
    • Mendez, A. J., and L. Uint. 1996. Apolipoprotein-mediated cellular cholesterol and phospholipid efflux depend on a functional Golgi apparatus. J. Lipid Res. 37: 2510-2524.
    • (1996) J. Lipid Res , vol.37 , pp. 2510-2524
    • Mendez, A.J.1    Uint, L.2
  • 46
    • 0030852447 scopus 로고    scopus 로고
    • Decreased reverse cholesterol transport from Tangier disease fibroblasts. Acceptor specificity and effect of brefeldin on lipid efflux
    • Remaley, A. T., U. K. Schumacher, J. A. Stonik, B. D. Farsi, H. Nazih, and H. B. Brewer, Jr. 1997. Decreased reverse cholesterol transport from Tangier disease fibroblasts. Acceptor specificity and effect of brefeldin on lipid efflux. Arterioscler. Thromb. Vasc. Biol. 17: 1813-1821.
    • (1997) Arterioscler. Thromb. Vasc. Biol , vol.17 , pp. 1813-1821
    • Remaley, A.T.1    Schumacher, U.K.2    Stonik, J.A.3    Farsi, B.D.4    Nazih, H.5    Brewer Jr., H.B.6
  • 47
    • 45549092878 scopus 로고    scopus 로고
    • Quantitative analysis of ABCA1-dependent compartmentalization and trafficking of apolipoprotein A-I: Implications for determining cellular kinetics of nascent high density lipoprotein biogenesis
    • Hassan, H. H., D. Bailey, D. Y. Lee, I. Iatan, A. Hafiane, I. Ruel, L. Krimbou, and J. Genest. 2008. Quantitative analysis of ABCA1-dependent compartmentalization and trafficking of apolipoprotein A-I: implications for determining cellular kinetics of nascent high density lipoprotein biogenesis. J. Biol. Chem. 283: 11164-11175.
    • (2008) J. Biol. Chem , vol.283 , pp. 11164-11175
    • Hassan, H.H.1    Bailey, D.2    Lee, D.Y.3    Iatan, I.4    Hafiane, A.5    Ruel, I.6    Krimbou, L.7    Genest, J.8
  • 48
    • 0031941594 scopus 로고    scopus 로고
    • Mechanism of acidification of the trans-Golgi network (TGN). In situ measurements of pH using retrieval of TGN38 and furin from the cell surface
    • Demaurex, N., W. Furuya, S. D'Souza, J. S. Bonifacino, and S. Grinstein. 1998. Mechanism of acidification of the trans-Golgi network (TGN). In situ measurements of pH using retrieval of TGN38 and furin from the cell surface. J. Biol. Chem. 273: 2044-2051.
    • (1998) J. Biol. Chem , vol.273 , pp. 2044-2051
    • Demaurex, N.1    Furuya, W.2    D'Souza, S.3    Bonifacino, J.S.4    Grinstein, S.5
  • 49
    • 0017064087 scopus 로고
    • Conformational and thermodynamic properties of apo A-1 of human plasma high density lipoproteins
    • Tall, A. R., G. G. Shipley, and D. M. Small. 1976. Conformational and thermodynamic properties of apo A-1 of human plasma high density lipoproteins. J. Biol. Chem. 251: 3749-3755.
    • (1976) J. Biol. Chem , vol.251 , pp. 3749-3755
    • Tall, A.R.1    Shipley, G.G.2    Small, D.M.3
  • 50
    • 0032516486 scopus 로고    scopus 로고
    • The lipid binding activity of the exchangeable apolipoprotein apolipophorin-III correlates with the formation of a partially folded conformation
    • Soulages, J. L., and O. J. Bendavid. 1998. The lipid binding activity of the exchangeable apolipoprotein apolipophorin-III correlates with the formation of a partially folded conformation. Biochemistry. 37: 10203-10210.
    • (1998) Biochemistry , vol.37 , pp. 10203-10210
    • Soulages, J.L.1    Bendavid, O.J.2
  • 51
    • 0035954398 scopus 로고    scopus 로고
    • Conformational changes of an exchangeable apolipoprotein, apolipophorin III from Locusta migratoria, at low pH: Correlation with lipid binding
    • Weers, P. M., C. M. Kay, and R. O. Ryan. 2001. Conformational changes of an exchangeable apolipoprotein, apolipophorin III from Locusta migratoria, at low pH: correlation with lipid binding. Biochemistry. 40: 7754-7760.
    • (2001) Biochemistry , vol.40 , pp. 7754-7760
    • Weers, P.M.1    Kay, C.M.2    Ryan, R.O.3
  • 52
    • 0034824483 scopus 로고    scopus 로고
    • Modulation of the lipid binding properties of the N-terminal domain of human apolipoprotein E3
    • Weers, P. M., V. Narayanaswami, and R. O. Ryan. 2001. Modulation of the lipid binding properties of the N-terminal domain of human apolipoprotein E3. Eur. J. Biochem. 268: 3728-3735.
    • (2001) Eur. J. Biochem , vol.268 , pp. 3728-3735
    • Weers, P.M.1    Narayanaswami, V.2    Ryan, R.O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.