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Volumn 44, Issue 2, 2004, Pages 227-238

The ACAT inhibitor CP-113,818 markedly reduces amyloid pathology in a mouse model of Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; CHOLESTEROL ACYLTRANSFERASE INHIBITOR; CHOLESTEROL ESTER; CP 113818; UNCLASSIFIED DRUG;

EID: 5144227934     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuron.2004.08.043     Document Type: Article
Times cited : (233)

References (45)
  • 1
    • 0242300624 scopus 로고    scopus 로고
    • Games played by rogue proteins in prion disorders and Alzheimer's disease
    • Aguzzi A., Haass C. Games played by rogue proteins in prion disorders and Alzheimer's disease. Science. 302:2003;814-818
    • (2003) Science , vol.302 , pp. 814-818
    • Aguzzi, A.1    Haass, C.2
  • 4
    • 0036452144 scopus 로고    scopus 로고
    • Cholesterol in Alzheimer's disease and tauopathy
    • Burns M., Duff K. Cholesterol in Alzheimer's disease and tauopathy. Ann. N Y Acad. Sci. 977:2002;367-375
    • (2002) Ann. N Y Acad. Sci. , vol.977 , pp. 367-375
    • Burns, M.1    Duff, K.2
  • 6
    • 0035102386 scopus 로고    scopus 로고
    • Augmented senile plaque load in aged female β-amyloid precursor protein-transgenic mice
    • Callahan M.J., Lipinski W.J., Bian F., Durham R.A., Pack A., Walker L.C. Augmented senile plaque load in aged female β-amyloid precursor protein-transgenic mice. Am. J. Pathol. 158:2001;1173-1177
    • (2001) Am. J. Pathol. , vol.158 , pp. 1173-1177
    • Callahan, M.J.1    Lipinski, W.J.2    Bian, F.3    Durham, R.A.4    Pack, A.5    Walker, L.C.6
  • 7
    • 0142028254 scopus 로고    scopus 로고
    • The cholesterol-lowering drug Probucol increases apolipoprotein e production in the hippocampus of aged rats: Implications for Alzheimer's disease
    • Champagne D., Pearson D., Dea D., Rochford J., Poirier J. The cholesterol-lowering drug Probucol increases apolipoprotein e production in the hippocampus of aged rats. implications for Alzheimer's disease Neuroscience. 121:2003;99-110
    • (2003) Neuroscience , vol.121 , pp. 99-110
    • Champagne, D.1    Pearson, D.2    Dea, D.3    Rochford, J.4    Poirier, J.5
  • 9
    • 0035665182 scopus 로고    scopus 로고
    • Catalysis of ACAT may be completed within the plane of the membrane. a working hypothesis
    • Chang T.Y., Chang C.C., Lu X., Lin S. Catalysis of ACAT may be completed within the plane of the membrane. A working hypothesis. J. Lipid Res. 42:2001;1933-1938
    • (2001) J. Lipid Res. , vol.42 , pp. 1933-1938
    • Chang, T.Y.1    Chang, C.C.2    Lu, X.3    Lin, S.4
  • 10
    • 0036828769 scopus 로고    scopus 로고
    • Alzheimer's disease: Treatments in discovery and development
    • Citron M. Alzheimer's disease. treatments in discovery and development Nat. Neurosci. Suppl. 5:2002;1055-1057
    • (2002) Nat. Neurosci. Suppl. , vol.5 , pp. 1055-1057
    • Citron, M.1
  • 11
    • 0842309491 scopus 로고    scopus 로고
    • β-secretase inhibition for the treatment of Alzheimer's disease - Promise and challenge
    • Citron M. β-secretase inhibition for the treatment of Alzheimer's disease - promise and challenge. Trends Pharmacol. Sci. 25:2004;92-97
    • (2004) Trends Pharmacol. Sci. , vol.25 , pp. 92-97
    • Citron, M.1
  • 12
    • 16944362157 scopus 로고    scopus 로고
    • Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice
    • Citron M., Westaway D., Xia W., Carlson G., Diehl T., Levesque G., Johnson-Wood K., Lee M., Seubert P., Davis A., et al. Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice. Nat. Med. 3:1997;67-72
    • (1997) Nat. Med. , vol.3 , pp. 67-72
    • Citron, M.1    Westaway, D.2    Xia, W.3    Carlson, G.4    Diehl, T.5    Levesque, G.6    Johnson-Wood, K.7    Lee, M.8    Seubert, P.9    Davis, A.10
  • 13
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, Pen-2, and Nicastrin with Presenilin generate an active γ-Secretase complex
    • De Strooper B. Aph-1, Pen-2, and Nicastrin with Presenilin generate an active γ-Secretase complex. Neuron. 38:2003;9-12
    • (2003) Neuron , vol.38 , pp. 9-12
    • De Strooper, B.1
  • 17
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner G.G., Wong C.W. Alzheimer's disease. initial report of the purification and characterization of a novel cerebrovascular amyloid protein Biochem. Biophys. Res. Commun. 120:1984;885-890
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 18
    • 0035929554 scopus 로고    scopus 로고
    • Distinct intramembrane cleavage of the β-amyloid precursor protein family resembling γ-secretase-like cleavage of Notch
    • Gu Y., Misonou H., Sato T., Dohmae N., Takio K., Ihara Y. Distinct intramembrane cleavage of the β-amyloid precursor protein family resembling γ-secretase-like cleavage of Notch. J. Biol. Chem. 276:2001;35235-35238
    • (2001) J. Biol. Chem. , vol.276 , pp. 35235-35238
    • Gu, Y.1    Misonou, H.2    Sato, T.3    Dohmae, N.4    Takio, K.5    Ihara, Y.6
  • 19
    • 0042810567 scopus 로고    scopus 로고
    • Cholesterol, Aβ and Alzheimer's disease
    • Hartmann T. Cholesterol, Aβ and Alzheimer's disease. Trends Neurosci. 24:2001;S45-S48
    • (2001) Trends Neurosci. , vol.24
    • Hartmann, T.1
  • 20
    • 0031914718 scopus 로고    scopus 로고
    • Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes
    • Holcomb L., Gordon M.N., McGowan E., Yu X., Benkovic S., Jantzen P., Wright K., Saad I., Mueller R., Morgan D., et al. Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes. Nat. Med. 4:1998;97-100
    • (1998) Nat. Med. , vol.4 , pp. 97-100
    • Holcomb, L.1    Gordon, M.N.2    McGowan, E.3    Yu, X.4    Benkovic, S.5    Jantzen, P.6    Wright, K.7    Saad, I.8    Mueller, R.9    Morgan, D.10
  • 21
    • 0027258525 scopus 로고
    • The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett J.T., Berger E.P., Lansbury P.T. Jr. The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation. implications for the pathogenesis of Alzheimer's disease Biochemistry. 32:1993;4693-4697
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 24
    • 0035863055 scopus 로고    scopus 로고
    • Age-dependent changes in brain, CSF, and plasma amyloid β protein in the Tg2576 transgenic mouse model of Alzheimer's disease
    • Kawarabayashi T., Younkin L.H., Saido T.C., Shoji M., Ashe K.H., Younkin S.G. Age-dependent changes in brain, CSF, and plasma amyloid β protein in the Tg2576 transgenic mouse model of Alzheimer's disease. J. Neurosci. 21:2001;372-381
    • (2001) J. Neurosci. , vol.21 , pp. 372-381
    • Kawarabayashi, T.1    Younkin, L.H.2    Saido, T.C.3    Shoji, M.4    Ashe, K.H.5    Younkin, S.G.6
  • 25
    • 0037146553 scopus 로고    scopus 로고
    • Nectin-1α, an immunoglobulin-like receptor involved in the formation of synapses, is a substrate for presenilin/γ-secretase-like cleavage
    • Kim D.Y., Ingano L.A., Kovacs D.M. Nectin-1α, an immunoglobulin-like receptor involved in the formation of synapses, is a substrate for presenilin/γ-secretase-like cleavage. J. Biol. Chem. 277:2002;49976-49981
    • (2002) J. Biol. Chem. , vol.277 , pp. 49976-49981
    • Kim, D.Y.1    Ingano, L.A.2    Kovacs, D.M.3
  • 26
    • 0037188530 scopus 로고    scopus 로고
    • Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice
    • Lee J.Y., Cole T.B., Palmiter R.D., Suh S.W., Koh J.Y. Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice. Proc. Natl. Acad. Sci. USA. 99:2002;7705-7710
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7705-7710
    • Lee, J.Y.1    Cole, T.B.2    Palmiter, R.D.3    Suh, S.W.4    Koh, J.Y.5
  • 27
    • 0038343343 scopus 로고    scopus 로고
    • Amyloid precursor protein (APP) and the biology of proteolytic processing: Relevance to Alzheimer's disease
    • Ling Y., Morgan K., Kalsheker N. Amyloid precursor protein (APP) and the biology of proteolytic processing. relevance to Alzheimer's disease Int. J. Biochem. Cell Biol. 35:2003;1505-1535
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 1505-1535
    • Ling, Y.1    Morgan, K.2    Kalsheker, N.3
  • 28
    • 0141429160 scopus 로고    scopus 로고
    • A CBP binding transcriptional repressor produced by the PS1/ε-cleavage of N-cadherin is inhibited by PS1 FAD mutations
    • Marambaud P., Wen P.H., Dutt A., Shioi J., Takashima A., Siman R., Robakis N.K. A CBP binding transcriptional repressor produced by the PS1/ε-cleavage of N-cadherin is inhibited by PS1 FAD mutations. Cell. 114:2003;635-645
    • (2003) Cell , vol.114 , pp. 635-645
    • Marambaud, P.1    Wen, P.H.2    Dutt, A.3    Shioi, J.4    Takashima, A.5    Siman, R.6    Robakis, N.K.7
  • 33
    • 0345669752 scopus 로고    scopus 로고
    • Alzheimer's disease: The cholesterol connection
    • Puglielli L., Tanzi R.E., Kovacs D.M. Alzheimer's disease. the cholesterol connection Nat. Neurosci. 6:2003;345-351
    • (2003) Nat. Neurosci. , vol.6 , pp. 345-351
    • Puglielli, L.1    Tanzi, R.E.2    Kovacs, D.M.3
  • 35
    • 0035889404 scopus 로고    scopus 로고
    • Early formation of mature amyloid-β protein deposits in a mutant APP transgenic model depends on levels of Aβ(1-42)
    • Rockenstein E., Mallory M., Mante M., Sisk A., Masliah E. Early formation of mature amyloid-β protein deposits in a mutant APP transgenic model depends on levels of Aβ(1-42). J. Neurosci. Res. 66:2001;573-582
    • (2001) J. Neurosci. Res. , vol.66 , pp. 573-582
    • Rockenstein, E.1    Mallory, M.2    Mante, M.3    Sisk, A.4    Masliah, E.5
  • 36
    • 0031969223 scopus 로고    scopus 로고
    • Alzheimer's disease as proteolytic disorders: Anabolism and catabolism of β-amyloid
    • Saido T.C. Alzheimer's disease as proteolytic disorders. anabolism and catabolism of β-amyloid Neurobiol. Aging. 19:1998;S69-S75
    • (1998) Neurobiol. Aging , vol.19
    • Saido, T.C.1
  • 37
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • Selkoe D.J. Translating cell biology into therapeutic advances in Alzheimer's disease. Nature. 399:1999;A23-A31
    • (1999) Nature , vol.399
    • Selkoe, D.J.1
  • 38
    • 0041827050 scopus 로고    scopus 로고
    • Emerging non-statin LDL-lowering therapies for dyslipidemia and atherosclerosis
    • Shah P.K. Emerging non-statin LDL-lowering therapies for dyslipidemia and atherosclerosis. Rev. Cardiovasc. Med. 4:2003;136-141
    • (2003) Rev. Cardiovasc. Med. , vol.4 , pp. 136-141
    • Shah, P.K.1
  • 40
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid β protein secreted by familial amyloid β protein precursor (β APP717) mutants
    • Suzuki N., Cheung T.T., Cai X.D., Odaka A., Otvos L. Jr., Eckman C., Golde T.E., Younkin S.G. An increased percentage of long amyloid β protein secreted by familial amyloid β protein precursor (β APP717) mutants. Science. 264:1994;1336-1340
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1    Cheung, T.T.2    Cai, X.D.3    Odaka, A.4    Otvos Jr., L.5    Eckman, C.6    Golde, T.E.7    Younkin, S.G.8
  • 42
    • 4344630985 scopus 로고    scopus 로고
    • BACE1: The β-secretase enzyme in alzheimer's disease
    • Vassar R. BACE1. the β-secretase enzyme in alzheimer's disease J. Mol. Neurosci. 23:2004;105-114
    • (2004) J. Mol. Neurosci. , vol.23 , pp. 105-114
    • Vassar, R.1
  • 43
    • 0346848902 scopus 로고    scopus 로고
    • Gender differences in the amount and deposition of amyloidβ in APPswe and PS1 double transgenic mice
    • Wang J., Tanila H., Puolivali J., Kadish I., van Groen T. Gender differences in the amount and deposition of amyloidβ in APPswe and PS1 double transgenic mice. Neurobiol. Dis. 14:2003;318-327
    • (2003) Neurobiol. Dis. , vol.14 , pp. 318-327
    • Wang, J.1    Tanila, H.2    Puolivali, J.3    Kadish, I.4    Van Groen, T.5
  • 44
    • 0347318065 scopus 로고    scopus 로고
    • Cholesterol and the biology of Alzheimer's disease
    • Wolozin B. Cholesterol and the biology of Alzheimer's disease. Neuron. 41:2004;7-10
    • (2004) Neuron , vol.41 , pp. 7-10
    • Wolozin, B.1
  • 45
    • 0042671326 scopus 로고    scopus 로고
    • Intramembrane proteolysis by presenilin and presenilin-like proteases
    • Xia W., Wolfe M.S. Intramembrane proteolysis by presenilin and presenilin-like proteases. J. Cell Sci. 116:2003;2839-2844
    • (2003) J. Cell Sci. , vol.116 , pp. 2839-2844
    • Xia, W.1    Wolfe, M.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.