메뉴 건너뛰기




Volumn 84, Issue 3, 2003, Pages 471-479

Cholesterol is necessary both for the toxic effect of Aβ peptides on vascular smooth muscle cells and for Aβ binding to vascular smooth muscle cell membranes

Author keywords

A ; Cholesterol; VSMC membranes

Indexed keywords

AMYLOID BETA PROTEIN; CHOLESTEROL; HYPOCHOLESTEROLEMIC AGENT;

EID: 0037312139     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2003.01552.x     Document Type: Article
Times cited : (98)

References (51)
  • 2
    • 0030949517 scopus 로고    scopus 로고
    • Lipid binding to amyloid β-peptide aggregates: Preferential binding of cholesterol as compared to phosphatidylcholine and fatty acids
    • Avdulov N. A., Chochina S. V., Igbavboa U., O'Hare E. O., Schroeder F., Cleary J. P. and Wood W. G. (1997) Lipid binding to amyloid β-peptide aggregates: preferential binding of cholesterol as compared to phosphatidylcholine and fatty acids. J. Neurochem. 68, 2086-2091.
    • (1997) J. Neurochem. , vol.68 , pp. 2086-2091
    • Avdulov, N.A.1    Chochina, S.V.2    Igbavboa, U.3    O'Hare, E.O.4    Schroeder, F.5    Cleary, J.P.6    Wood, W.G.7
  • 3
    • 0033954766 scopus 로고    scopus 로고
    • Effect of membrane lipid composition on the conformational equilibria of the nicotinic acetylcholine receptor
    • Baenziger J. E., Morris M. L., Darsaut T. E. and Ryan S. E. (2000) Effect of membrane lipid composition on the conformational equilibria of the nicotinic acetylcholine receptor. J. Biol. Chem. 275, 777-784.
    • (2000) J. Biol. Chem. , vol.275 , pp. 777-784
    • Baenziger, J.E.1    Morris, M.L.2    Darsaut, T.E.3    Ryan, S.E.4
  • 5
    • 0034742113 scopus 로고    scopus 로고
    • Amyloid β-peptide (1-40) increases neuronal membrane fluidity. Role of cholesterol and brain region
    • Chochina S. V., Avdulov N. A., Igbavboa U., Cleary J. P., O'Hare E. O. and Wood W. G. (2001) Amyloid β-peptide (1-40) increases neuronal membrane fluidity. Role of cholesterol and brain region. J. Lipid Res. 42, 1292-1297.
    • (2001) J. Lipid Res. , vol.42 , pp. 1292-1297
    • Chochina, S.V.1    Avdulov, N.A.2    Igbavboa, U.3    Cleary, J.P.4    O'Hare, E.O.5    Wood, W.G.6
  • 7
    • 0025899234 scopus 로고
    • Use of an aqueous soluble tetrazolium assay for cell-growth assays in culture
    • Cory A. H., Owen T. C., Barltrop J. A. and Cory J. G. (1991) Use of an aqueous soluble tetrazolium assay for cell-growth assays in culture. Cancer Commun. 3, 207-212.
    • (1991) Cancer Commun. , vol.3 , pp. 207-212
    • Cory, A.H.1    Owen, T.C.2    Barltrop, J.A.3    Cory, J.G.4
  • 8
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid β binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits
    • Curtain C. C., Ali F., Volitakis I., Cherny R. A., Norton R. S., Beyreuther K., Barrow C. J., Masters C. L., Bush A. I. and Barnham K. J. (2001) Alzheimer's disease amyloid β binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits. J. Biol. Chem. 276, 20466-20473.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20466-20473
    • Curtain, C.C.1    Ali, F.2    Volitakis, I.3    Cherny, R.A.4    Norton, R.S.5    Beyreuther, K.6    Barrow, C.J.7    Masters, C.L.8    Bush, A.I.9    Barnham, K.J.10
  • 10
    • 0034125199 scopus 로고    scopus 로고
    • Cholesterol modulates the membrane-disordering effects of β-amyloid peptides in the hippocampus specific changes in Alzheimer's disease
    • Eckert G. P., Cairns N. J., Maras A., Gattaz W. F. and Muller W. E. (2000) Cholesterol modulates the membrane-disordering effects of β-amyloid peptides in the hippocampus specific changes in Alzheimer's disease. Dement. Geriatr. Cogn. Disord. 11, 181-186.
    • (2000) Dement. Geriatr. Cogn. Disord. , vol.11 , pp. 181-186
    • Eckert, G.P.1    Cairns, N.J.2    Maras, A.3    Gattaz, W.F.4    Muller, W.E.5
  • 13
    • 0034956750 scopus 로고    scopus 로고
    • Treatment with controlled-release lovastatin decreases serum concentrations of human β-amyloid (Aβ) peptide
    • Friedhoff L. T., Cullen E. I., Geoghagen N. S. and Buxbaum J. D. (2001) Treatment with controlled-release lovastatin decreases serum concentrations of human β-amyloid (Aβ) peptide. Int. J. Neuropsychopharmacol. 4, 127-130.
    • (2001) Int. J. Neuropsychopharmacol. , vol.4 , pp. 127-130
    • Friedhoff, L.T.1    Cullen, E.I.2    Geoghagen, N.S.3    Buxbaum, J.D.4
  • 14
    • 0021256895 scopus 로고
    • Alzheimers disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner G. G. and Wong C. W. (1984) Alzheimers disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120, 885-890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 15
    • 0042810567 scopus 로고    scopus 로고
    • Cholesterol, Aβ and Alzheimer's disease
    • Hartmann T. (2001) Cholesterol, Aβ and Alzheimer's disease. Trends Neurosci. 24, S45-S48.
    • (2001) Trends Neurosci. , vol.24
    • Hartmann, T.1
  • 16
    • 0030794309 scopus 로고    scopus 로고
    • Inhibition of the electrostatic interaction between β-amyloid peptide and membranes prevents β-amyloid-induced toxicity
    • Hertel C., Terzi E., Hauser N., Jakob-Rotne R., Seelig J. and Kemp J. A. (1997) Inhibition of the electrostatic interaction between β-amyloid peptide and membranes prevents β-amyloid-induced toxicity. Proc. Natl Acad. Sci. USA 94, 9412-9416.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 9412-9416
    • Hertel, C.1    Terzi, E.2    Hauser, N.3    Jakob-Rotne, R.4    Seelig, J.5    Kemp, J.A.6
  • 17
    • 0020657366 scopus 로고
    • Isolation of rat hepatocyte plasma membranes. I. Presence of three major domains
    • Hubbard A. L., Wall D. A. and Ma A. (1983) Isolation of rat hepatocyte plasma membranes. I. Presence of three major domains. J. Cell Biol. 96, 217-229.
    • (1983) J. Cell Biol. , vol.96 , pp. 217-229
    • Hubbard, A.L.1    Wall, D.A.2    Ma, A.3
  • 19
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett J. T. and Lansbury P. T. Jr (1993) Seeding 'one-dimensional crystallization' of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury P.T., Jr.2
  • 20
    • 0037155235 scopus 로고    scopus 로고
    • Cholesterol is an important factor affecting the membrane insertion of β-amyloid peptide (Aβ1-40), which may potentially inhibit the fibril formation
    • in press
    • Ji S. R., Wu Y. and Sui S. F. (2002) Cholesterol is an important factor affecting the membrane insertion of β-amyloid peptide (Aβ1-40), which may potentially inhibit the fibril formation. J. Biol. Chem. in press:.
    • (2002) J. Biol. Chem
    • Ji, S.R.1    Wu, Y.2    Sui, S.F.3
  • 23
    • 0032899322 scopus 로고    scopus 로고
    • Quantifying amyloid β-peptide (Aβ) aggregation using the Congo red-Aβ (CR-Aβ) spectrophotometric assay
    • Klunk W. E., Jacob R. F. and Mason R. P. (1999) Quantifying amyloid β-peptide (Aβ) aggregation using the Congo red-Aβ (CR-Aβ) spectrophotometric assay. Anal. Biochem. 266, 66-76.
    • (1999) Anal. Biochem. , vol.266 , pp. 66-76
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 24
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10
    • Kojro E., Gimpl G., Lammick S., Marz W. and Fahrenholz F. (2001) Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10. Proc. Natl Acad. Sci. USA 98, 5815-5820.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 5815-5820
    • Kojro, E.1    Gimpl, G.2    Lammick, S.3    Marz, W.4    Fahrenholz, F.5
  • 25
    • 0034702813 scopus 로고    scopus 로고
    • Correlation of β-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity in membranes
    • Kremer J. J., Pallitto M. M., Sklansky D. J. and Murphy R. M. (2000) Correlation of β-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity in 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
  • 26
    • 0035942997 scopus 로고    scopus 로고
    • Profile of changes in lipid bilayer structure caused by β-amyloid pepide
    • Kremer J. J., Sklansky D. J. and Murphy R. M. (2001) Profile of changes in lipid bilayer structure caused by β-amyloid pepide. Biochemistry 40, 8563-8471.
    • (2001) Biochemistry , vol.40 , pp. 8563-8471
    • Kremer, J.J.1    Sklansky, D.J.2    Murphy, R.M.3
  • 28
    • 0037192816 scopus 로고    scopus 로고
    • Identification of a common sphingolipid-binding domain in Alzheimer, prion, and HIV-1 proteins
    • Mahfoud R., Garmy N., Maresca M., Yahi N., Puigserver A. and Fantini J. (2002) Identification of a common sphingolipid-binding domain in Alzheimer, prion, and HIV-1 proteins. J. Biol. Chem. 277, 11292-11296.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11292-11296
    • Mahfoud, R.1    Garmy, N.2    Maresca, M.3    Yahi, N.4    Puigserver, A.5    Fantini, J.6
  • 30
    • 0032516749 scopus 로고    scopus 로고
    • Cholesterol dependant generation of a unique amyloid β-protein from apically missorted amyloid precursor protein in MDCK cells
    • Mizuno T., Haass C., Michikawa M. and Yanagisawa K. (1998) Cholesterol dependant generation of a unique amyloid β-protein from apically missorted amyloid precursor protein in MDCK cells. Biochim. Biophys. Acta 1373, 119-130.
    • (1998) Biochim. Biophys. Acta , vol.1373 , pp. 119-130
    • Mizuno, T.1    Haass, C.2    Michikawa, M.3    Yanagisawa, K.4
  • 31
    • 0035795730 scopus 로고    scopus 로고
    • Analysis of antimicrobial peptide interactions with hybrid bilayer membrane systems using surface plasmon resonance
    • Mozsolits H., Wirth H. J., Werkmeister J. and Aguilar M. I. (2001) Analysis of antimicrobial peptide interactions with hybrid bilayer membrane systems using surface plasmon resonance. Biochim. Biophys. Acta 1512, 64-76.
    • (2001) Biochim. Biophys. Acta , vol.1512 , pp. 64-76
    • Mozsolits, H.1    Wirth, H.J.2    Werkmeister, J.3    Aguilar, M.I.4
  • 32
    • 0034644836 scopus 로고    scopus 로고
    • Regulation of APP cleavage by α-, β- and γ-secretases
    • Nunan J. and Small D. H. (2000) Regulation of APP cleavage by α-, β- and γ-secretases. FEBS Lett. 483, 6-1.0.
    • (2000) FEBS Lett. , vol.483 , pp. 6-10
    • Nunan, J.1    Small, D.H.2
  • 33
    • 0025992417 scopus 로고
    • In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike C. J., Walencewicz A. J., Glabe C. G. and Cotman C. W. (1991) In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res. 563, 311-314.
    • (1991) Brain Res. , vol.563 , pp. 311-314
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 34
    • 0032539975 scopus 로고    scopus 로고
    • Oligomizeration of endogenous and synthetic amyloid β-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red
    • Podlinsny M. B., Walsh D. M., Amarante P., Ostaszewski B. L., Stimson E. R., Maggio J. E., Teplow D. B. and Selkoe D. J. (1998) Oligomizeration of endogenous and synthetic amyloid β-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red. Biochemistry 37, 3602-3611.
    • (1998) Biochemistry , vol.37 , pp. 3602-3611
    • Podlinsny, M.B.1    Walsh, D.M.2    Amarante, P.3    Ostaszewski, B.L.4    Stimson, E.R.5    Maggio, J.E.6    Teplow, D.B.7    Selkoe, D.J.8
  • 35
    • 0025770134 scopus 로고
    • The distribution of tangles, plaques and related immunohistochemical markers in healthy aging and Alzheimer's disease
    • Price J. L., Davis P. B., Morris J. C. and White D. L. (1991) The distribution of tangles, plaques and related immunohistochemical markers in healthy aging and Alzheimer's disease. Neurobiol. Aging 12, 295-312.
    • (1991) Neurobiol. Aging , vol.12 , pp. 295-312
    • Price, J.L.1    Davis, P.B.2    Morris, J.C.3    White, D.L.4
  • 38
  • 41
    • 0032568552 scopus 로고    scopus 로고
    • Simvastatin strongly reduces levels of ALzheimer's disease β-amyloid peptides Aβ42 and Aβ40 in vitro and in vivo
    • Simons M., Keller P., De Strooper B., Beyreuther K., Dotti C. and Simons K. (1998) Simvastatin strongly reduces levels of ALzheimer's disease β-amyloid peptides Aβ42 and Aβ40 in vitro and in vivo. Proc. Natl Acad. Sci. USA 95, 6460-6464.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6460-6464
    • Simons, M.1    Keller, P.2    De Strooper, B.3    Beyreuther, K.4    Dotti, C.5    Simons, K.6
  • 42
    • 0032814135 scopus 로고    scopus 로고
    • Alzheimer's disease and the amyloid β protein: What is the role of amyloid?
    • Small D. H. and McLean C. A. (1999) Alzheimer's disease and the amyloid β protein: What is the role of amyloid? J. Neurochem. 73, 443-449.
    • (1999) J. Neurochem. , vol.73 , pp. 443-449
    • Small, D.H.1    McLean, C.A.2
  • 43
    • 0035433962 scopus 로고    scopus 로고
    • Alzheirmer's disease and Aβ toxicity: From top to bottom
    • Small D. H., Mok S. S. and Bornstein J. C. (2001) Alzheirmer's disease and Aβ toxicity: from top to bottom. Nat. Rev. Neurosci. 2, 595-598.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 595-598
    • Small, D.H.1    Mok, S.S.2    Bornstein, J.C.3
  • 44
    • 0028177562 scopus 로고
    • Induction of Alzheimer-like β amyloid immunoreactivity in the brains of rabbits with dietary cholesterol
    • Sparks D. L., Scheff S. W., Hunsaker J. C., Liu H. and Gross D. R. (1994) Induction of Alzheimer-like β amyloid immunoreactivity in the brains of rabbits with dietary cholesterol. Exp. Neurol. 126, 88-94.
    • (1994) Exp. Neurol. , vol.126 , pp. 88-94
    • Sparks, D.L.1    Scheff, S.W.2    Hunsaker, J.C.3    Liu, H.4    Gross, D.R.5
  • 45
    • 0034808094 scopus 로고    scopus 로고
    • The structural role of cholesterol in biological membranes
    • Sugahara M., Uragami M., Yan X. and Regen S. L. (2001) The structural role of cholesterol in biological membranes. J. Am. Chem. Soc. 123, 7939-7940.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7939-7940
    • Sugahara, M.1    Uragami, M.2    Yan, X.3    Regen, S.L.4
  • 46
    • 0034968340 scopus 로고    scopus 로고
    • Neuropeptides interact with glycolipid receptors: A surface plasmon resonance study
    • Valdez-Gonzalez T., Inagawa J. and Ido T. (2001) Neuropeptides interact with glycolipid receptors: a surface plasmon resonance study. Peptides 22, 1099-1106.
    • (2001) Peptides , vol.22 , pp. 1099-1106
    • Valdez-Gonzalez, T.1    Inagawa, J.2    Ido, T.3
  • 47
    • 0023254674 scopus 로고
    • Cerebral amyloid angiopathy: A critical review
    • Vinters H. V. (1987) Cerebral amyloid angiopathy: a critical review. Stroke 18, 311-324.
    • (1987) Stroke , vol.18 , pp. 311-324
    • Vinters, H.V.1
  • 48
    • 0035834692 scopus 로고    scopus 로고
    • Reduction in cholesterol and sialic acid content protects cells from the toxic effects of β-amyloid peptides
    • Wang S. S. S., Rymer D. L. and Good T. A. (2001) Reduction in cholesterol and sialic acid content protects cells from the toxic effects of β-amyloid peptides. J. Biol. Chem. 276, 42027-42034.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42027-42034
    • Wang, S.S.S.1    Rymer, D.L.2    Good, T.A.3
  • 50
    • 0033772113 scopus 로고    scopus 로고
    • Decreased prevalence of Alzheimer's disease associated with 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors
    • Wolozin B., Kellman W., Ruosseau P., Celesia G. G. and Siegel G. (2000) Decreased prevalence of Alzheimer's disease associated with 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors. Arch. Neurol. 57, 1439-1443.
    • (2000) Arch. Neurol. , vol.57 , pp. 1439-1443
    • Wolozin, B.1    Kellman, W.2    Ruosseau, P.3    Celesia, G.G.4    Siegel, G.5
  • 51
    • 0029827792 scopus 로고    scopus 로고
    • Cholesterol protects PC12 cells from β amyloid-induced calcium disordering and cytotoxicity
    • Zhou Y. and Richardson J. S. (1996) Cholesterol protects PC12 cells from β amyloid-induced calcium disordering and cytotoxicity. Neuroreport 7, 2487-2490.
    • (1996) Neuroreport , vol.7 , pp. 2487-2490
    • Zhou, Y.1    Richardson, J.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.