메뉴 건너뛰기




Volumn 96, Issue 10, 2009, Pages 4299-4307

Cholesterol modulates the interaction of β-amyloid peptide with lipid bilayers

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[25-35]; CHOLESTEROL; ERGOSTEROL; MONOMER; OLIGOMER; STEROL; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; DEHYDROERGOSTEROL; DRUG DERIVATIVE; PEPTIDE FRAGMENT; TYROSINE;

EID: 68049131387     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.02.036     Document Type: Article
Times cited : (47)

References (37)
  • 1
    • 33750731675 scopus 로고    scopus 로고
    • 100 years and counting: Prospects for defeating Alzheimer's disease
    • Roberson, E. D., and L. Mucke. 2006. 100 years and counting: prospects for defeating Alzheimer's disease. Science. 314:781-784.
    • (2006) Science , vol.314 , pp. 781-784
    • Roberson, E.D.1    Mucke, L.2
  • 2
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe, D. J. 1991. The molecular pathology of Alzheimer's disease. Neuron. 6:487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 3
    • 0347753786 scopus 로고    scopus 로고
    • Two types of Alzheimer's β-amyloid (1-40) peptide membrane interactions: Aggregation preventing transmembrane anchoring versus accelerated surface fibril formation
    • Bokvist, M., F. Lindstrom, A. Watts, and G. Grobner. 2004. Two types of Alzheimer's β-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation. J. Mol. Biol. 335:1039-1049.
    • (2004) J. Mol. Biol , vol.335 , pp. 1039-1049
    • Bokvist, M.1    Lindstrom, F.2    Watts, A.3    Grobner, G.4
  • 4
    • 0037155235 scopus 로고    scopus 로고
    • Cholesterol is an important factor affecting the membrane insertion of β-amyloid peptide (A β 1-40), which may potentially inhibit the fibril formation
    • Ji, S. R., Y. Wu, and S. F. Sui. 2002. Cholesterol is an important factor affecting the membrane insertion of β-amyloid peptide (A β 1-40), which may potentially inhibit the fibril formation. J. Biol. Chem. 277:6273-6279.
    • (2002) J. Biol. Chem , vol.277 , pp. 6273-6279
    • Ji, S.R.1    Wu, Y.2    Sui, S.F.3
  • 5
    • 0028982292 scopus 로고
    • Self-association of β-amyloid peptide (1-40) in solution and binding to lipid membranes
    • Terzi, E., G. Holzemann, and J. Seelig. 1995. Self-association of β-amyloid peptide (1-40) in solution and binding to lipid membranes. J. Mol. Biol. 252:633-642.
    • (1995) J. Mol. Biol , vol.252 , pp. 633-642
    • Terzi, E.1    Holzemann, G.2    Seelig, J.3
  • 7
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy, J. A., and G. A. Higgins. 1992. Alzheimer's disease: the amyloid cascade hypothesis. Science. 256:184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 8
    • 14844304305 scopus 로고    scopus 로고
    • Oxidation of cholesterol by amyloid precursor protein and β-amyloid peptide
    • Nelson, T. J., and D. L. Alkon. 2005. Oxidation of cholesterol by amyloid precursor protein and β-amyloid peptide. J. Biol. Chem. 280:7377-7387.
    • (2005) J. Biol. Chem , vol.280 , pp. 7377-7387
    • Nelson, T.J.1    Alkon, D.L.2
  • 9
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid b protein forms ion channels: Implications for Alzheimer's disease pathophysiology
    • Lin, H., R. Bhatia, and R. Lal. 2001. Amyloid b protein forms ion channels: implications for Alzheimer's disease pathophysiology. FASEB J. 15:2433-2444.
    • (2001) FASEB J , vol.15 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 10
    • 33748510160 scopus 로고    scopus 로고
    • Lipid headgroup superlattice modulates the activity of surface-acting cholesterol oxidase in ternary phospholipid/cholesterol bilayers
    • Cheng, K. H., B. Cannon, J. Metze, A. Lewis, J. Huang, et al. 2006. Lipid headgroup superlattice modulates the activity of surface-acting cholesterol oxidase in ternary phospholipid/cholesterol bilayers. Biochemistry. 45:10855-10864.
    • (2006) Biochemistry , vol.45 , pp. 10855-10864
    • Cheng, K.H.1    Cannon, B.2    Metze, J.3    Lewis, A.4    Huang, J.5
  • 11
    • 0028131711 scopus 로고
    • Evidence for regular distribution of sterols in liquid crystalline phosphatidylcholine bilayers
    • Chong, P. L. 1994. Evidence for regular distribution of sterols in liquid crystalline phosphatidylcholine bilayers. Proc. Natl. Acad. Sci. USA. 91:10069-10073.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10069-10073
    • Chong, P.L.1
  • 12
    • 0032817738 scopus 로고    scopus 로고
    • Lateral organisation of membrane lipids. The superlattice view
    • Somerharju, P., J. A. Virtanen, and K. H. Cheng. 1999. Lateral organisation of membrane lipids. The superlattice view. Biochim. Biophys. Acta. 1440:32-48.
    • (1999) Biochim. Biophys. Acta , vol.1440 , pp. 32-48
    • Somerharju, P.1    Virtanen, J.A.2    Cheng, K.H.3
  • 13
    • 1842482773 scopus 로고    scopus 로고
    • Model systems, lipid rafts, and cell membranes
    • Simons, K., and W. L. Vaz. 2004. Model systems, lipid rafts, and cell membranes. Annu. Rev. Biophys. Biomol. Struct. 33:269-295.
    • (2004) Annu. Rev. Biophys. Biomol. Struct , vol.33 , pp. 269-295
    • Simons, K.1    Vaz, W.L.2
  • 14
    • 0000914811 scopus 로고
    • The synthesis of a perdeuterated phospholipid: 1,2-dimyristoyl-sn-glycero-3-phosphocholine- d72
    • Kingsley, P. B., and G. W. Feigenson. 1979. The synthesis of a perdeuterated phospholipid: 1,2-dimyristoyl-sn-glycero-3-phosphocholine- d72. Chem. Phys. Lipids. 24:135-147.
    • (1979) Chem. Phys. Lipids , vol.24 , pp. 135-147
    • Kingsley, P.B.1    Feigenson, G.W.2
  • 15
    • 0034702813 scopus 로고    scopus 로고
    • Correlation of β-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity of model membranes
    • Kremer, J. J., M. M. Pallitto, D. J. Sklansky, and R. M. Murphy. 2000. Correlation of β-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity of model membranes. Biochemistry. 39:10309-10318.
    • (2000) Biochemistry , vol.39 , pp. 10309-10318
    • Kremer, J.J.1    Pallitto, M.M.2    Sklansky, D.J.3    Murphy, R.M.4
  • 16
    • 0035942997 scopus 로고    scopus 로고
    • Profile of changes in lipid bilayer structure caused by β-amyloid peptide
    • Kremer, J. J., D. J. Sklansky, and R. M. Murphy. 2001. Profile of changes in lipid bilayer structure caused by β-amyloid peptide. Biochemistry. 40:8563-8571.
    • (2001) Biochemistry , vol.40 , pp. 8563-8571
    • Kremer, J.J.1    Sklansky, D.J.2    Murphy, R.M.3
  • 17
    • 0036793543 scopus 로고    scopus 로고
    • Plasma membrane cholesterol controls the cytotoxicity of Alzheimer's disease AβP (1-40) and (1-42) peptides
    • Arispe, N., and M. Doh. 2002. Plasma membrane cholesterol controls the cytotoxicity of Alzheimer's disease AβP (1-40) and (1-42) peptides. FASEB J. 16:1526-1536.
    • (2002) FASEB J , vol.16 , pp. 1526-1536
    • Arispe, N.1    Doh, M.2
  • 18
    • 0037474240 scopus 로고    scopus 로고
    • Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-b peptide with membrane lipid
    • Curtain, C. C., F. E. Ali, D. G. Smith, A. I. Bush, C. L. Masters, et al. 2003. Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-b peptide with membrane lipid. J. Biol. Chem. 278:2977-2982.
    • (2003) J. Biol. Chem , vol.278 , pp. 2977-2982
    • Curtain, C.C.1    Ali, F.E.2    Smith, D.G.3    Bush, A.I.4    Masters, C.L.5
  • 19
    • 0033009037 scopus 로고    scopus 로고
    • A novel strategy for the preparation of liposomes: Rapid solvent exchange
    • Buboltz, J. T., and G. W. Feigenson. 1999. A novel strategy for the preparation of liposomes: rapid solvent exchange. Biochim. Biophys. Acta. 1417:232-245.
    • (1999) Biochim. Biophys. Acta , vol.1417 , pp. 232-245
    • Buboltz, J.T.1    Feigenson, G.W.2
  • 20
    • 27144531262 scopus 로고    scopus 로고
    • Cholesterol modulated antibody binding in supported lipid membranes as determined by total internal reflectance microscopy on a microfabricated high-throughput glass chip
    • Cannon, B., N. Weaver, Q. Pu, V. Thiagarajan, S. Liu, et al. 2005. Cholesterol modulated antibody binding in supported lipid membranes as determined by total internal reflectance microscopy on a microfabricated high-throughput glass chip. Langmuir. 21:9666-9674.
    • (2005) Langmuir , vol.21 , pp. 9666-9674
    • Cannon, B.1    Weaver, N.2    Pu, Q.3    Thiagarajan, V.4    Liu, S.5
  • 21
    • 33645811118 scopus 로고    scopus 로고
    • Cholesterol supports headgroup superlattice domain formation in fluid phospholipid/cholesterol bilayers
    • Cannon, B., A. Lewis, J. Metze, V. Thiagarajan, M. W. Vaughn, et al. 2006. Cholesterol supports headgroup superlattice domain formation in fluid phospholipid/cholesterol bilayers. J. Phys. Chem. B. 110:6339-6350.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 6339-6350
    • Cannon, B.1    Lewis, A.2    Metze, J.3    Thiagarajan, V.4    Vaughn, M.W.5
  • 22
    • 34248365632 scopus 로고    scopus 로고
    • Assess the nature of cholesterol-lipid interactions through the chemical potential of cholesterol in phosphatidylcholine bilayers
    • Ali, M. R., K. H. Cheng, and J. Huang. 2007. Assess the nature of cholesterol-lipid interactions through the chemical potential of cholesterol in phosphatidylcholine bilayers. Proc. Natl. Acad. Sci. USA. 104:5372-5377.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 5372-5377
    • Ali, M.R.1    Cheng, K.H.2    Huang, J.3
  • 25
    • 0042047094 scopus 로고    scopus 로고
    • Fluorescence studies of dehydroergosterol in phosphatidylethanolamine/phosphatidylcholine bilayers
    • Cheng, K. H., J. Virtanen, and P. Somerharju. 1999. Fluorescence studies of dehydroergosterol in phosphatidylethanolamine/phosphatidylcholine bilayers. Biophys. J. 77:3108-3119.
    • (1999) Biophys. J , vol.77 , pp. 3108-3119
    • Cheng, K.H.1    Virtanen, J.2    Somerharju, P.3
  • 26
    • 36849115843 scopus 로고
    • Influence of Brownian rotation and energy transfer upon the measurements of fluorescence lifetime
    • Spencer, R. D., and G. Weber. 1970. Influence of Brownian rotation and energy transfer upon the measurements of fluorescence lifetime. J. Chem. Phys. 52:1654-1663.
    • (1970) J. Chem. Phys , vol.52 , pp. 1654-1663
    • Spencer, R.D.1    Weber, G.2
  • 27
    • 0002821446 scopus 로고
    • Mouvement Brownien d'un ellipsoide. II. Rotation libre et dipolarisation des florescences. Transaction et diffusion de molecules ellipsoidoles.
    • Perrin, F. 1936. Mouvement Brownien d'un ellipsoide. II. Rotation libre et dipolarisation des florescences. Transaction et diffusion de molecules ellipsoidoles. J. Phys. Radium. 71:1-44.
    • (1936) J. Phys. Radium , vol.71 , pp. 1-44
    • Perrin, F.1
  • 28
    • 0023277161 scopus 로고
    • A fluorescence study of dehydroergosterol in phosphatidylcholine bilayer vesicles
    • Schroeder, F., Y. Barenholz, E. Gratton, and T. E. Thompson. 1987. A fluorescence study of dehydroergosterol in phosphatidylcholine bilayer vesicles. Biochemistry. 26:2441-2448.
    • (1987) Biochemistry , vol.26 , pp. 2441-2448
    • Schroeder, F.1    Barenholz, Y.2    Gratton, E.3    Thompson, T.E.4
  • 29
    • 0026640565 scopus 로고
    • Orientation factor in steady-state and time-resolved resonance energy transfer measurements
    • Wu, P., and L. Brand. 1992. Orientation factor in steady-state and time-resolved resonance energy transfer measurements. Biochemistry. 31:7939-7947.
    • (1992) Biochemistry , vol.31 , pp. 7939-7947
    • Wu, P.1    Brand, L.2
  • 30
    • 0021847707 scopus 로고
    • Fluorescence resonance energy transfer study of the associative state of membrane-bound complexes of complement proteins C5b-8
    • Cheng, K. H., T. Wiedmer, and P. J. Sims. 1985. Fluorescence resonance energy transfer study of the associative state of membrane-bound complexes of complement proteins C5b-8. J. Immunol. 135:459-464.
    • (1985) J. Immunol , vol.135 , pp. 459-464
    • Cheng, K.H.1    Wiedmer, T.2    Sims, P.J.3
  • 31
    • 0037763988 scopus 로고    scopus 로고
    • Time-resolved fluorescence and fourier transform infrared spectroscopic investigations of lateral packing defects and superlattice domains in compositionally uniform cholesterol/phosphatidylcholine bilayers
    • Cannon, B., G. Heath, J. Huang, P. Somerharju, J. A. Virtanen, et al. 2003. Time-resolved fluorescence and fourier transform infrared spectroscopic investigations of lateral packing defects and superlattice domains in compositionally uniform cholesterol/phosphatidylcholine bilayers. Biophys. J. 84:3777-3791.
    • (2003) Biophys. J , vol.84 , pp. 3777-3791
    • Cannon, B.1    Heath, G.2    Huang, J.3    Somerharju, P.4    Virtanen, J.A.5
  • 33
    • 0030947939 scopus 로고    scopus 로고
    • Cholesterol and ergosterol superlattices in three-component liquid crystalline lipid bilayers as revealed by dehydroergosterol fluorescence
    • Liu, F., I. P. Sugar, and P. L. Chong. 1997. Cholesterol and ergosterol superlattices in three-component liquid crystalline lipid bilayers as revealed by dehydroergosterol fluorescence. Biophys. J. 72:2243-2254.
    • (1997) Biophys. J , vol.72 , pp. 2243-2254
    • Liu, F.1    Sugar, I.P.2    Chong, P.L.3
  • 34
    • 1442300992 scopus 로고    scopus 로고
    • Cholesterol superlattice modulates the activity of cholesterol oxidase in lipid membranes
    • Wang, M. M., M. Olsher, I. P. Sugar, and P. L. Chong. 2004. Cholesterol superlattice modulates the activity of cholesterol oxidase in lipid membranes. Biochemistry. 43:2159-2166.
    • (2004) Biochemistry , vol.43 , pp. 2159-2166
    • Wang, M.M.1    Olsher, M.2    Sugar, I.P.3    Chong, P.L.4
  • 35
    • 0033616731 scopus 로고    scopus 로고
    • Evidence for a regulatory role of cholesterol superlattices in the hydrolytic activity of secretory phospholipase A2 in lipid membranes
    • Liu, F., and P. L. Chong. 1999. Evidence for a regulatory role of cholesterol superlattices in the hydrolytic activity of secretory phospholipase A2 in lipid membranes. Biochemistry. 38:3867-3873.
    • (1999) Biochemistry , vol.38 , pp. 3867-3873
    • Liu, F.1    Chong, P.L.2
  • 36
    • 34249821660 scopus 로고    scopus 로고
    • Critical factors for detection of biphasic changes in membrane properties at specific sterol mole fractions for maximal superlattice formation
    • Venegas, B., I. P. Sugar, and P. L. Chong. 2007. Critical factors for detection of biphasic changes in membrane properties at specific sterol mole fractions for maximal superlattice formation. J. Phys. Chem. B. 111:5180-5192.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 5180-5192
    • Venegas, B.1    Sugar, I.P.2    Chong, P.L.3
  • 37
    • 0001068789 scopus 로고    scopus 로고
    • Extraction of lipids from phospholipid membranes by steered molecular dynamics
    • Stepaniants, S., S. Izrailev, and K. Schulten. 1997. Extraction of lipids from phospholipid membranes by steered molecular dynamics. J. Mol. Model. 3:473-475.
    • (1997) J. Mol. Model , vol.3 , pp. 473-475
    • Stepaniants, S.1    Izrailev, S.2    Schulten, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.