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Volumn 24, Issue SUPPL. 2, 2011, Pages 143-152

Membrane anchored and lipid raft targeted β-secretase inhibitors for alzheimer's disease therapy

Author keywords

Alzheimer's disease; amyloid; BACE1; drug design; endocytosis; inhibitor; lipid rafts; membrane anchoring; targeting; secretase

Indexed keywords

BETA SECRETASE 1; BETA SECRETASE 2; BETA SECRETASE INHIBITOR; CHOLESTANOL; CHOLESTEROL; ERGOSTEROL; SPHINGOLIPID; STIGMASTEROL;

EID: 79955665531     PISSN: 13872877     EISSN: None     Source Type: Journal    
DOI: 10.3233/JAD-2011-110269     Document Type: Review
Times cited : (14)

References (65)
  • 1
    • 77951060145 scopus 로고    scopus 로고
    • Proteases and proteolysis in Alzheimer disease: A multifactorial view on the disease process
    • De Strooper B (2010) Proteases and proteolysis in Alzheimer disease: a multifactorial view on the disease process. Physiol Rev 90, 465-494.
    • (2010) Physiol Rev , vol.90 , pp. 465-494
    • De Strooper, B.1
  • 2
    • 33750731675 scopus 로고    scopus 로고
    • 100 Years and counting: Prospects for defeating Alzheimer's disease
    • DOI 10.1126/science.1132813
    • Roberson ED, Mucke L (2006) 100 years and counting: prospects for defeating Alzheimer's disease. Science 314, 781-784. (Pubitemid 44706637)
    • (2006) Science , vol.314 , Issue.5800 , pp. 781-784
    • Roberson, E.D.1    Mucke, L.2
  • 3
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • DOI 10.1038/nrm2101, PII NRM2101
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 8, 101-112. (Pubitemid 46432529)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 4
    • 24144441879 scopus 로고    scopus 로고
    • Uncovering gamma-secretase
    • Steiner H (2004) Uncovering gamma-secretase. Curr Alzheimer Res 1, 175-181.
    • (2004) Curr Alzheimer Res , vol.1 , pp. 175-181
    • Steiner, H.1
  • 5
    • 0035955693 scopus 로고    scopus 로고
    • The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner
    • Kimberly WT, Zheng JB, Guenette SY, Selkoe DJ (2001) The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner. J Biol Chem 276, 40288-40292.
    • (2001) J Biol Chem , vol.276 , pp. 40288-40292
    • Kimberly, W.T.1    Zheng, J.B.2    Guenette, S.Y.3    Selkoe, D.J.4
  • 6
    • 1442264828 scopus 로고    scopus 로고
    • Take five - BACE and the γ-secretase quartet conduct Alzheimer's amyloid β-peptide generation
    • DOI 10.1038/sj.emboj.7600061
    • Haass C (2004) Take five-BACE and the gamma-secretase quartet conduct Alzheimer's amyloid beta-peptide genera-tion. EMBO J 23, 483-488. (Pubitemid 38282380)
    • (2004) EMBO Journal , vol.23 , Issue.3 , pp. 483-488
    • Haass, C.1
  • 15
    • 0028924248 scopus 로고
    • Generation of amyloid beta protein from its precursor is sequence specific
    • Citron M, Teplow DB, Selkoe DJ (1995) Generation of amyloid beta protein from its precursor is sequence specific. Neuron 14, 661-670.
    • (1995) Neuron , vol.14 , pp. 661-670
    • Citron, M.1    Teplow, D.B.2    Selkoe, D.J.3
  • 17
    • 0037038816 scopus 로고    scopus 로고
    • β-secretase (BACE) as a drug target for Alzheimer's disease
    • DOI 10.1016/S0169-409X(02)00157-6, PII S0169409X02001576
    • Vassar R (2002) Beta-secretase (BACE) as a drug target for Alzheimer's disease. Adv Drug Deliv Rev 54, 1589-1602. (Pubitemid 35346833)
    • (2002) Advanced Drug Delivery Reviews , vol.54 , Issue.12 , pp. 1589-1602
    • Vassar, R.1
  • 18
    • 0033793248 scopus 로고    scopus 로고
    • Coordinated expression of beta-amyloid precursor protein and the putative betasecretase BACE and alpha-secretase ADAM10 in mouse and human brain
    • Marcinkiewicz M, Seidah NG (2000) Coordinated expression of beta-amyloid precursor protein and the putative betasecretase BACE and alpha-secretase ADAM10 in mouse and human brain, J Neurochem 75, 2133-2143.
    • (2000) J Neurochem , vol.75 , pp. 2133-2143
    • Marcinkiewicz, M.1    Seidah, N.G.2
  • 19
    • 27744501797 scopus 로고    scopus 로고
    • Lipids as modulators of proteolytic activity of BACE: Involvement of cholesterol, glycosphingolipids, and anionic phospholipids in vitro
    • DOI 10.1074/jbc.M504484200
    • Kalvodova L, Kahya N, Schwille P, Ehehalt R, Verkade P, Drechsel D, Simons K (2005) Lipids as modulators of proteolytic activity of BACE: involvement of cholesterol, glycosphingolipids, and anionic phospholipids in vitro. J Biol Chem 280, 36815-36823. (Pubitemid 41587762)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.44 , pp. 36815-36823
    • Kalvodova, L.1    Kahya, N.2    Schwille, P.3    Ehehalt, R.4    Verkade, P.5    Drechsel, D.6    Simons, K.7
  • 24
    • 77953280950 scopus 로고    scopus 로고
    • Membrane rafts in Alzheimer's disease beta-amyloid production
    • Vetrivel KS, Thinakaran G (2010) Membrane rafts in Alzheimer's disease beta-amyloid production. Biochim Bio-phys Acta 1801, 860-867.
    • (2010) Biochim Bio-phys Acta , vol.1801 , pp. 860-867
    • Vetrivel, K.S.1    Thinakaran, G.2
  • 27
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts
    • DOI 10.1083/jcb.200207113
    • Ehehalt R, Keller P, Haass C, Thiele C, Simons K (2003) Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J Cell Biol 160, 113-123. (Pubitemid 36091721)
    • (2003) Journal of Cell Biology , vol.160 , Issue.1 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 28
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid β-protein involves the endocytic pathway
    • Koo EH, Squazzo SL (1994) Evidence that production and release of amyloid beta-protein involves the endocytic path-way. J Biol Chem 269, 17386-17389. (Pubitemid 24218009)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.26 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 30
    • 40849097929 scopus 로고    scopus 로고
    • Flotillin-dependent clustering of the amyloid precursor protein regulates its endocytosis and amyloidogenic processing in neurons
    • Schneider A, Rajendran L, Honsho M, Gralle M, Donnert G, Wouters F, Hell SW, Simons M. Flotillin-dependent clustering of the amyloid precursor protein regulates its endocytosis and amyloidogenic processing in neurons. J Neurosci 28, 2874-2882.
    • J Neurosci , vol.28 , pp. 2874-2882
    • Schneider, A.1    Rajendran, L.2    Honsho, M.3    Gralle, M.4    Donnert, G.5    Wouters, F.6    Hell, S.W.7    Simons, M.8
  • 31
    • 0028866435 scopus 로고
    • The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway
    • Haass C, Lemere CA, Capell A, Citron M, Seubert P, Schenk D, Lannfelt L, Selkoe DJ (1995) The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway. Nat Med 1, 1291-1296.
    • (1995) Nat Med , vol.1 , pp. 1291-1296
    • Haass, C.1    Lemere, C.A.2    Capell, A.3    Citron, M.4    Seubert, P.5    Schenk, D.6    Lannfelt, L.7    Selkoe, D.J.8
  • 32
    • 0029942495 scopus 로고    scopus 로고
    • Metabolism of the "swedish" amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the "beta-secretase" site occurs in the golgi apparatus
    • Thinakaran G, Teplow DB, Siman R, Greenberg B, Sisodia SS (1996) Metabolism of the "Swedish" amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the "beta-secretase" site occurs in the golgi apparatus. JBiol Chem 271, 9390-9397.
    • (1996) J Biol Chem , vol.271 , pp. 9390-9397
    • Thinakaran, G.1    Teplow, D.B.2    Siman, R.3    Greenberg, B.4    Sisodia, S.S.5
  • 33
    • 33745038221 scopus 로고    scopus 로고
    • Inhibition of APP trafficking by tau protein does not increase the generation of amyloid-β peptides
    • DOI 10.1111/j.1600-0854.2006.00434.x
    • Goldsbury C, Mocanu MM, Thies E, Kaether C, Haass C, Keller P, Biernat J, Mandelkow E, Mandelkow EM (2006) Inhibition of APP trafficking by tau protein does not increase the generation of amyloid-beta peptides. Traffic 7, 873-888. (Pubitemid 43871776)
    • (2006) Traffic , vol.7 , Issue.7 , pp. 873-888
    • Goldsbury, C.1    Mocanu, M.-M.2    Thies, E.3    Kaether, C.4    Haass, C.5    Keller, P.6    Biernat, J.7    Mandelkow, E.8    Mandelkow, E.-M.9
  • 34
    • 33644862462 scopus 로고    scopus 로고
    • Amyloid precursor protein and Notch intracellular domains are generated after transport of their precursors to the cell surface
    • DOI 10.1111/j.1600-0854.2006.00396.x
    • Kaether C, Schmitt S, Willem M, Haass C (2006) Amyloid precursor protein and notch intracellular domains are gen-erated after transport of their precursors to the cell surface. Traffic 7, 408-415. (Pubitemid 43372750)
    • (2006) Traffic , vol.7 , Issue.4 , pp. 408-415
    • Kaether, C.1    Schmitt, S.2    Willem, M.3    Haass, C.4
  • 35
    • 25144501662 scopus 로고    scopus 로고
    • Intraneuronal Aβ accumulation and origin of plaques in Alzheimer's disease
    • DOI 10.1016/j.neurobiolaging.2005.05.022, PII S0197458005001624
    • Gouras GK, Almeida CG, Takahashi RH (2005) Intraneuronal Abeta accumulation and origin of plaques in Alzheimer's disease. Neurobiol Aging 26, 1235-1244. (Pubitemid 41338539)
    • (2005) Neurobiology of Aging , vol.26 , Issue.9 , pp. 1235-1244
    • Gouras, G.K.1    Almeida, C.G.2    Takahashi, R.H.3
  • 36
    • 34347257068 scopus 로고    scopus 로고
    • Increased Aβ production leads to intracellular accumulation of Aβ in flotillin-1-positive endosomes
    • DOI 10.1159/000101841
    • Rajendran L, Knobloch M, Geiger KD, Dienel S, Nitsch R, Simons K, Konietzko U (2007) Increased Abeta production leads to intracellular accumulation of Abeta in flotillin-1-positive endosomes. Neurodegener Dis 4, 164-170. (Pubitemid 47000410)
    • (2007) Neurodegenerative Diseases , vol.4 , Issue.2-3 , pp. 164-170
    • Rajendran, L.1    Knobloch, M.2    Geiger, K.D.3    Dienel, S.4    Nitsch, R.5    Simons, K.6    Konietzko, U.7
  • 39
    • 69249212436 scopus 로고    scopus 로고
    • Linking vascular disorders and Alzheimer's disease: Potential involvement of BACE1
    • Cole SL, Vassar R (2009) Linking vascular disorders and Alzheimer's disease: potential involvement of BACE1. Neu¬robiolAging30, 1535-1544.
    • (2009) Neu¬robiolAging , vol.30 , pp. 1535-1544
    • Cole, S.L.1    Vassar, R.2
  • 42
    • 0034613320 scopus 로고    scopus 로고
    • Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor
    • Hong L, Koelsch G, Lin X, Wu S, Terzyan S, Ghosh AK, Zhang XC, Tang J (2000) Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor. Sci-ence 290, 150-153.
    • (2000) Sci-ence , vol.290 , pp. 150-153
    • Hong, L.1    Koelsch, G.2    Lin, X.3    Wu, S.4    Terzyan, S.5    Ghosh, A.K.6    Zhang, X.C.7    Tang, J.8
  • 43
    • 63949088562 scopus 로고    scopus 로고
    • Function, regulation and therapeutic properties of beta-secretase (BACE1)
    • Willem M, Lammich S, Haass C (2009) Function, regulation and therapeutic properties of beta-secretase (BACE1). Semin Cell Dev Biol 20, 175-182.
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 175-182
    • Willem, M.1    Lammich, S.2    Haass, C.3
  • 46
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell mem-branes
    • Simons K, Ikonen E (1997) Functional rafts in cell mem-branes. Nature 387, 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 47
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D, Simons K (2010) Lipid rafts as a membrane-organizing principle. Science 327, 46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 49
    • 17244380947 scopus 로고    scopus 로고
    • Lipid rafts and membrane dynamics
    • DOI 10.1242/jcs.01681
    • Rajendran L, Simons K (2005) Lipid rafts and membrane dynamics. J Cell Sci 118, 1099-1102. (Pubitemid 40528680)
    • (2005) Journal of Cell Science , vol.118 , Issue.6 , pp. 1099-1102
    • Rajendran, L.1    Simons, K.2
  • 50
    • 33747591249 scopus 로고    scopus 로고
    • Dynamics in the plasma membrane: How to combine fluidity and order
    • DOI 10.1038/sj.emboj.7601204, PII 7601204
    • Marguet D, Lenne PF, Rigneault H, He HT (2006) Dynamics in the plasma membrane: how to combine fluidity and order. EMBO J 25, 3446-3457. (Pubitemid 44264856)
    • (2006) EMBO Journal , vol.25 , Issue.15 , pp. 3446-3457
    • Marguet, D.1    Lenne, P.-F.2    Rigneault, H.3    He, H.-T.4
  • 51
    • 34447273123 scopus 로고    scopus 로고
    • Mechanisms of disease: New therapeutic strategies for Alzheimer's disease - Targeting APP processing in lipid rafts
    • DOI 10.1038/ncpneuro0549, PII NCPNEURO0549
    • Cheng H, Vetrivel KS, Gong P, Meckler X, Parent A, Thi-nakaran G (2007) Mechanisms of disease: new therapeutic strategies for Alzheimer's disease-targeting APP processing in lipid rafts. Nat Clin Pract Neurol 3, 374-382. (Pubitemid 47040327)
    • (2007) Nature Clinical Practice Neurology , vol.3 , Issue.7 , pp. 374-382
    • Cheng, H.1    Vetrivel, K.S.2    Gong, P.3    Meckler, X.4    Parent, A.5    Thinakaran, G.6
  • 53
    • 33645299023 scopus 로고    scopus 로고
    • The involvement of lipid rafts in Alzheimer's disease
    • Cordy JM, Hooper NM, Turner AJ (2006) The involvement of lipid rafts in Alzheimer's disease. Mol Membr Biol 23, 111-122.
    • (2006) Mol Membr Biol , vol.23 , pp. 111-122
    • Cordy, J.M.1    Hooper, N.M.2    Turner, A.J.3
  • 62
    • 78651278930 scopus 로고    scopus 로고
    • Structural design, solid-phase synthesis and activity of membrane-anchored beta-secretase inhibitors on Abeta gen-eration from wild-type and Swedish-mutant APP
    • Schieb H, Weidlich S, Schlechtingen G, Linning P, Jennings G, Gruner M, Wiltfang J, Klafki HW, Knolker HJ (2010) Structural design, solid-phase synthesis and activity of membrane-anchored beta-secretase inhibitors on Abeta gen-eration from wild-type and Swedish-mutant APP Chemistry 16, 14412-14423.
    • (2010) Chemistry , vol.16 , pp. 14412-14423
    • Schieb, H.1    Weidlich, S.2    Schlechtingen, G.3    Linning, P.4    Jennings, G.5    Gruner, M.6    Wiltfang, J.7    Klafki, H.W.8    Knolker, H.J.9
  • 64
    • 0344791683 scopus 로고    scopus 로고
    • Endocytic sorting of lipid analogues differing solely in the chemistry of their hydrophobic tails
    • DOI 10.1083/jcb.144.6.1271
    • Mukherjee S, Soe TT, Maxfield FR (1999) Endocytic sorting of lipid analogues differing solely in the chemistry of their hydrophobic tails, J Cell Biol 144, 1271-1284. (Pubitemid 29157304)
    • (1999) Journal of Cell Biology , vol.144 , Issue.6 , pp. 1271-1284
    • Mukherjee, S.1    Soe, T.T.2    Maxfield, F.R.3
  • 65
    • 74049133619 scopus 로고    scopus 로고
    • Subcellular tar-geting strategies for drug design and delivery
    • Rajendran L, Knolker HJ, Simons K (2010) Subcellular tar-geting strategies for drug design and delivery. Nat Rev Drug Discov 9, 29-42.
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 29-42
    • Rajendran, L.1    Knolker, H.J.2    Simons, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.