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Volumn , Issue , 2011, Pages 177-194

Alzheimer's Disease as a Membrane-Associated Enzymopathy of β-Amyloid Precursor Protein (APP) Secretases

Author keywords

Alcadein processing; Alzheimer's disease; Amyloid ; Amyloid precursor protein; Intra membrane cleaving enzyme; Secretases

Indexed keywords


EID: 84874972275     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527634323.ch8     Document Type: Chapter
Times cited : (2)

References (64)
  • 1
    • 0028856460 scopus 로고
    • An English translation of Alzheimer's 1907 paper, "Uber eine eigenartige Erkankung der Hirnrinde"
    • Alzheimer, A., Stelzmann, R.A., Schnitzlein, H.N., and Murtagh, F.R. (1995) An English translation of Alzheimer's 1907 paper, "Uber eine eigenartige Erkankung der Hirnrinde". Clin. Anat., 8 (6), 429-431.
    • (1995) Clin. Anat. , vol.8 , Issue.6 , pp. 429-431
    • Alzheimer, A.1    Stelzmann, R.A.2    Schnitzlein, H.N.3    Murtagh, F.R.4
  • 2
    • 84880184726 scopus 로고    scopus 로고
    • Alzheimer's Disease; a Century of Scientific and Clinical Research
    • eds., IOS Press, Amsterdam
    • Perry, G., Avila, J., Kinoshita, J., and Smith, M.A. (eds.) (2006) Alzheimer's Disease; a Century of Scientific and Clinical Research, IOS Press, Amsterdam.
    • (2006)
    • Perry, G.1    Avila, J.2    Kinoshita, J.3    Smith, M.A.4
  • 3
    • 33750705653 scopus 로고    scopus 로고
    • A century of Alzheimer's disease
    • Goedert, M. and Spillantini, M.G. (2006) A century of Alzheimer's disease. Science, 314 (5800), 777-781.
    • (2006) Science , vol.314 , Issue.5800 , pp. 777-781
    • Goedert, M.1    Spillantini, M.G.2
  • 5
    • 57649210178 scopus 로고    scopus 로고
    • Regulation of amyloid β-protein precursor by phosphorylation and protein interactions
    • Suzuki, T. and Nakaya, T. (2008) Regulation of amyloid β-protein precursor by phosphorylation and protein interactions. J. Biol. Chem., 283 (44), 29633-29637.
    • (2008) J. Biol. Chem. , vol.283 , Issue.44 , pp. 29633-29637
    • Suzuki, T.1    Nakaya, T.2
  • 7
    • 76449085569 scopus 로고    scopus 로고
    • Gamma-secretases: from cell biology to therapeutic strategies
    • Bergmans, B.A. and De Strooper, B. (2010) Gamma-secretases: from cell biology to therapeutic strategies. Lancet Neurol., 9 (2), 215-226.
    • (2010) Lancet Neurol. , vol.9 , Issue.2 , pp. 215-226
    • Bergmans, B.A.1    De Strooper, B.2
  • 8
    • 57649221135 scopus 로고    scopus 로고
    • Amyloid precursor protein trafficking, processing, and function
    • Thinakaran, G. and Koo, E. (2008) Amyloid precursor protein trafficking, processing, and function. J. Biol. Chem., 283 (44), 29615-29619.
    • (2008) J. Biol. Chem. , vol.283 , Issue.44 , pp. 29615-29619
    • Thinakaran, G.1    Koo, E.2
  • 11
    • 3543104951 scopus 로고    scopus 로고
    • Thematic review series: brain lipids. Cholesterol metabolism in the central nervous system during early development and in the mature animal
    • Dietschy, J.M. and Turley, S.D. (2004) Thematic review series: brain lipids. Cholesterol metabolism in the central nervous system during early development and in the mature animal. J. Lipid. Res., 45 (8), 1375-1397.
    • (2004) J. Lipid. Res. , vol.45 , Issue.8 , pp. 1375-1397
    • Dietschy, J.M.1    Turley, S.D.2
  • 12
    • 70450219539 scopus 로고    scopus 로고
    • Cholesterol metabolism and transport in the pathogenesis of Alzheimer's disease
    • Martins, J.I., Berger, T., Sharman, J.M., Verdile, G., Fuller, J.S., and Martins, N.R. (2009) Cholesterol metabolism and transport in the pathogenesis of Alzheimer's disease. J. Neurochem., 111 (6), 1275-1308.
    • (2009) J. Neurochem. , vol.111 , Issue.6 , pp. 1275-1308
    • Martins, J.I.1    Berger, T.2    Sharman, J.M.3    Verdile, G.4    Fuller, J.S.5    Martins, N.R.6
  • 13
    • 0345669752 scopus 로고    scopus 로고
    • Alzheimer's disease: the cholesterol connection
    • Puglielli, L., Tanzi, R.E., and Kovacs, D.M. (2003) Alzheimer's disease: the cholesterol connection. Nat. Neurosci., 6 (4), 345-351.
    • (2003) Nat. Neurosci. , vol.6 , Issue.4 , pp. 345-351
    • Puglielli, L.1    Tanzi, R.E.2    Kovacs, D.M.3
  • 15
    • 67349270965 scopus 로고    scopus 로고
    • Apolipoprotein E and its receptors in Alzheimer's disease: pathways, pathogenesis and therapy
    • Bu, G. (2009) Apolipoprotein E and its receptors in Alzheimer's disease: pathways, pathogenesis and therapy. Nat. Rev. Neurosci., 10 (5), 333-344.
    • (2009) Nat. Rev. Neurosci. , vol.10 , Issue.5 , pp. 333-344
    • Bu, G.1
  • 17
    • 0030752288 scopus 로고    scopus 로고
    • Genetic association of the low-density lipoprotein receptor-related protein gene (LRP), an apolipoprotein E receptor, with late-onset Alzheimer's disease
    • Kang, D.E., Saitoh, T., Chen, X., Xia, Y., Masliah, E., Hansen, L.A., Thomas, R.G., Thal, L.J., and Katzman, R. (1997) Genetic association of the low-density lipoprotein receptor-related protein gene (LRP), an apolipoprotein E receptor, with late-onset Alzheimer's disease. Neurology, 49, 56-61.
    • (1997) Neurology , vol.49 , pp. 56-61
    • Kang, D.E.1    Saitoh, T.2    Chen, X.3    Xia, Y.4    Masliah, E.5    Hansen, L.A.6    Thomas, R.G.7    Thal, L.J.8    Katzman, R.9
  • 18
    • 33751173605 scopus 로고    scopus 로고
    • Lipoprotein receptors in Alzheimer's disease
    • Andersen, M.O. and Willnow, E.T. (2006) Lipoprotein receptors in Alzheimer's disease. Trends Neurosci., 29 (12), 687-694.
    • (2006) Trends Neurosci. , vol.29 , Issue.12 , pp. 687-694
    • Andersen, M.O.1    Willnow, E.T.2
  • 19
    • 32544435097 scopus 로고    scopus 로고
    • The lipoprotein receptor LR11 regulates amyloid beta production and amyloid precursor protein traffic in endosomal compartments
    • Offe, K., Dodson, S.E., Shoemaker, J.T., Fritz, J.J., Gearing, M., Levey, A.I., and Lah, J.J. (2006) The lipoprotein receptor LR11 regulates amyloid beta production and amyloid precursor protein traffic in endosomal compartments. J. Neurosci., 26 (5), 1596-1603.
    • (2006) J. Neurosci. , vol.26 , Issue.5 , pp. 1596-1603
    • Offe, K.1    Dodson, S.E.2    Shoemaker, J.T.3    Fritz, J.J.4    Gearing, M.5    Levey, A.I.6    Lah, J.J.7
  • 20
    • 63949084694 scopus 로고    scopus 로고
    • Lipoprotein receptors and cholesterol in APP trafficking and proteolytic processing, implications for Alzheimer's disease
    • Bu, G. and Marzolo, M. (2009) Lipoprotein receptors and cholesterol in APP trafficking and proteolytic processing, implications for Alzheimer's disease. Semin. Cell Dev. Biol., 20 (2), 191-200.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , Issue.2 , pp. 191-200
    • Bu, G.1    Marzolo, M.2
  • 21
    • 33745801153 scopus 로고    scopus 로고
    • Lipid rafts: contentious only from simplistic standpoints
    • Hancock, J.F. (2006) Lipid rafts: contentious only from simplistic standpoints. Nat. Rev. Mol. Cell. Biol., 7 (6), 456-462.
    • (2006) Nat. Rev. Mol. Cell. Biol. , vol.7 , Issue.6 , pp. 456-462
    • Hancock, J.F.1
  • 22
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown, D.A. and London, E. (1998) Functions of lipid rafts in biological membranes. Annu. Rev. Cell. Dev. Biol., 14, 111-136.
    • (1998) Annu. Rev. Cell. Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 24
    • 0034157389 scopus 로고    scopus 로고
    • Role of membrane organization and membrane domains in endocytic lipid trafficking
    • Mukherjee, S. and Maxfield, F.R. (2000) Role of membrane organization and membrane domains in endocytic lipid trafficking. Traffic, 1 (3), 203-211.
    • (2000) Traffic , vol.1 , Issue.3 , pp. 203-211
    • Mukherjee, S.1    Maxfield, F.R.2
  • 25
    • 1842588906 scopus 로고    scopus 로고
    • Lipids as targeting signals: lipid rafts and intracellular trafficking
    • Helms, J.B. and Zurzolo, C. (2004) Lipids as targeting signals: lipid rafts and intracellular trafficking. Traffic, 5 (4), 247-254.
    • (2004) Traffic , vol.5 , Issue.4 , pp. 247-254
    • Helms, J.B.1    Zurzolo, C.2
  • 26
    • 0141482022 scopus 로고    scopus 로고
    • Exclusively targeting beta-secretase to lipid rafts by GPI-anchor addition upregulates beta-site processing of the amyloid precursor protein
    • Cordy, J.M., Hussain, I., Dingwall, C., Hooper, N.M., and Turner, A.J. (2003) Exclusively targeting beta-secretase to lipid rafts by GPI-anchor addition upregulates beta-site processing of the amyloid precursor protein. Proc. Natl. Acad. Sci. USA, 100 (20), 11735-11740.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.20 , pp. 11735-11740
    • Cordy, J.M.1    Hussain, I.2    Dingwall, C.3    Hooper, N.M.4    Turner, A.J.5
  • 27
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
    • Ehehalt, R., Keller, P., Haass, C., Thiele, C., and Simons, K. (2003) Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J. Cell. Biol., 160 (1), 113-123.
    • (2003) J. Cell. Biol. , vol.160 , Issue.1 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 28
    • 27744501797 scopus 로고    scopus 로고
    • Lipids as modulators of proteolytic activity of BACE: involvement of cholesterol, glycosphingolipids, and anionic phospholipids in vitro
    • Kalvodova, L., Kahya, N., Schwille, P., Ehehalt, R., Verkade, P., Drechsel, D., and Simons, K. (2005) Lipids as modulators of proteolytic activity of BACE: involvement of cholesterol, glycosphingolipids, and anionic phospholipids in vitro. J. Biol. Chem., 280 (44), 36815-36823.
    • (2005) J. Biol. Chem. , 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
  • 29
    • 0033525077 scopus 로고    scopus 로고
    • Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated
    • Melkonian, K.A., Ostermeyer, A.G., Chen, J.Z., Roth, M.G., and Brown, D.A. (1999) Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated. J. Biol. Chem., 274 (6), 3910-3917.
    • (1999) J. Biol. Chem. , vol.274 , Issue.6 , pp. 3910-3917
    • Melkonian, K.A.1    Ostermeyer, A.G.2    Chen, J.Z.3    Roth, M.G.4    Brown, D.A.5
  • 30
    • 0035815635 scopus 로고    scopus 로고
    • Post-translational processing of beta-secretase (betaamyloid-converting enzyme) and its ectodomain shedding. The pro-and transmembrane/cytosolic domains affect its cellular activity and amyloid-beta production
    • Benjannet, S., Elagoz, A., Wickham, L., Mamarbachi, M., Munzer, J.S., Basak, A., Lazure, C., Cromlish, J.A., Sisodia, S., Checler, F., Chretien, M., and Seidah, N.G. (2001) Post-translational processing of beta-secretase (betaamyloid-converting enzyme) and its ectodomain shedding. The pro-and transmembrane/cytosolic domains affect its cellular activity and amyloid-beta production. J. Biol. Chem., 276 (14), 10879-10887.
    • (2001) J. Biol. Chem. , vol.276 , Issue.14 , pp. 10879-10887
    • Benjannet, S.1    Elagoz, A.2    Wickham, L.3    Mamarbachi, M.4    Munzer, J.S.5    Basak, A.6    Lazure, C.7    Cromlish, J.A.8    Sisodia, S.9    Checler, F.10    Chretien, M.11    Seidah, N.G.12
  • 33
    • 0033593480 scopus 로고    scopus 로고
    • Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein
    • Tomita, S., Ozaki, T., Taru, H., Oguchi, S., Takeda, S., Yagi, Y., Sakiyama, S., Kirino, Y., and Suzuki, T. (1999) Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein. J. Biol. Chem., 274 (4), 2243-2254.
    • (1999) J. Biol. Chem. , vol.274 , Issue.4 , pp. 2243-2254
    • Tomita, S.1    Ozaki, T.2    Taru, H.3    Oguchi, S.4    Takeda, S.5    Yagi, Y.6    Sakiyama, S.7    Kirino, Y.8    Suzuki, T.9
  • 34
    • 1542782550 scopus 로고    scopus 로고
    • Novel cadherin-related membrane proteins, alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism
    • Araki, Y., Tomita, S., Yamaguchi, H., Miyagi, N., Sumioka, A., Kirino, Y., and Suzuki, T. (2003) Novel cadherin-related membrane proteins, alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism. J. Biol. Chem., 278 (49), 49448-49458.
    • (2003) J. Biol. Chem. , vol.278 , Issue.49 , pp. 49448-49458
    • Araki, Y.1    Tomita, S.2    Yamaguchi, H.3    Miyagi, N.4    Sumioka, A.5    Kirino, Y.6    Suzuki, T.7
  • 35
    • 70350502866 scopus 로고    scopus 로고
    • Regulation of the physiological function and metabolism of AβPP by AβPP binding proteins
    • Taru, H. and Suzuki, T. (2009) Regulation of the physiological function and metabolism of AβPP by AβPP binding proteins. J. Alzheimers Dis., 18 (2), 253-265.
    • (2009) J. Alzheimers Dis. , vol.18 , Issue.2 , pp. 253-265
    • Taru, H.1    Suzuki, T.2
  • 36
    • 33845991184 scopus 로고    scopus 로고
    • Enhanced amyloidogenic metabolism of the amyloid beta-protein precursor in the X11Ldeficient mouse brain
    • Sano, Y., Syuzo Takabatake, A., Nakaya, T., Saito, Y., Tomita, S., Itohara, S., and Suzuki, T. (2006) Enhanced amyloidogenic metabolism of the amyloid beta-protein precursor in the X11Ldeficient mouse brain. J. Biol. Chem., 281 (49), 37853-37860.
    • (2006) J. Biol. Chem. , vol.281 , Issue.49 , pp. 37853-37860
    • Sano, Y.1    Syuzo Takabatake, A.2    Nakaya, T.3    Saito, Y.4    Tomita, S.5    Itohara, S.6    Suzuki, T.7
  • 38
    • 10344227214 scopus 로고    scopus 로고
    • The neuronal adaptor protein X11beta reduces amyloid beta-protein levels and amyloid plaque formation in the brains of transgenic mice
    • Lee, J.H., Lau, K.F., Perkinton, M.S., Standen, C.L., Rogelj, B., Falinska, A., McLoughlin, D.M., and Miller, C.C. (2004) The neuronal adaptor protein X11beta reduces amyloid beta-protein levels and amyloid plaque formation in the brains of transgenic mice. J. Biol. Chem., 279 (47), 49099-49104.
    • (2004) J. Biol. Chem. , vol.279 , Issue.47 , pp. 49099-49104
    • Lee, J.H.1    Lau, K.F.2    Perkinton, M.S.3    Standen, C.L.4    Rogelj, B.5    Falinska, A.6    McLoughlin, D.M.7    Miller, C.C.8
  • 39
    • 58149095671 scopus 로고    scopus 로고
    • X11 proteins regulate the translocation of amyloid beta-protein precursor (APP) into detergent-resistant membrane and suppress the amyloidogenic cleavage of APP by betasite-cleaving enzyme in brain
    • Saito, Y., Sano, Y., Vassar, R., Gandy, S., Nakaya, T., Yamamoto, T., and Suzuki, T. (2008) X11 proteins regulate the translocation of amyloid beta-protein precursor (APP) into detergent-resistant membrane and suppress the amyloidogenic cleavage of APP by betasite-cleaving enzyme in brain. J. Biol. Chem., 283 (51), 35763-35771.
    • (2008) J. Biol. Chem. , vol.283 , Issue.51 , pp. 35763-35771
    • Saito, Y.1    Sano, Y.2    Vassar, R.3    Gandy, S.4    Nakaya, T.5    Yamamoto, T.6    Suzuki, T.7
  • 41
    • 20044393582 scopus 로고    scopus 로고
    • Alzheimer Disease and Frontotemporal Dementia Mutation Database
    • Cruts, M. and Brouwers, N. Alzheimer Disease and Frontotemporal Dementia Mutation Database, http://www.molgen.ua.ac.be/ADMutations/.
    • Cruts, M.1    Brouwers, N.2
  • 42
    • 43049163813 scopus 로고    scopus 로고
    • Substrate specificity of gamma-secretase and other intramembrane proteases
    • Beel, A.J. and Sanders, C.R. (2008) Substrate specificity of gamma-secretase and other intramembrane proteases. Cell. Mol. Life Sci., 65 (9), 1311-1334.
    • (2008) Cell. Mol. Life Sci. , vol.65 , Issue.9 , pp. 1311-1334
    • Beel, A.J.1    Sanders, C.R.2
  • 43
    • 0033639117 scopus 로고    scopus 로고
    • Requirements for presenilin-dependent cleavage of notch and other transmembrane proteins
    • Struhl, G. and Adachi, A. (2000) Requirements for presenilin-dependent cleavage of notch and other transmembrane proteins. Mol. Cell, 6 (3), 625-636.
    • (2000) Mol. Cell , vol.6 , Issue.3 , pp. 625-636
    • Struhl, G.1    Adachi, A.2
  • 47
    • 0033772113 scopus 로고    scopus 로고
    • Decreased prevalence of Alzheimer disease associated with 3-hydroxy-3-methyglutaryl coenzyme A reductase inhibitors
    • Wolozin, B., Kellman, W., Ruosseau, P., Celesia, G.G., and Siegel, G. (2000) Decreased prevalence of Alzheimer disease associated with 3-hydroxy-3-methyglutaryl coenzyme A reductase inhibitors. Arch. Neurol., 57 (10), 1439-1443.
    • (2000) Arch. Neurol. , vol.57 , Issue.10 , pp. 1439-1443
    • Wolozin, B.1    Kellman, W.2    Ruosseau, P.3    Celesia, G.G.4    Siegel, G.5
  • 50
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the alpha-secretase ADAM 10
    • Kojro, E., Gimpl, G., Lammich, S., Marz, W., and Fahrenholz, F. (2001) Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the alpha-secretase ADAM 10. Proc. Natl. Acad. Sci. USA, 98 (10), 5815-5820.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.10 , pp. 5815-5820
    • Kojro, E.1    Gimpl, G.2    Lammich, S.3    Marz, W.4    Fahrenholz, F.5
  • 54
    • 0032999907 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble complexes containing the familial Alzheimer's disease-associated presenilins
    • Parkin, E.T., Hussain, I., Karran, E.H., Turner, A.J., and Hooper, N.M. (1999) Characterization of detergent-insoluble complexes containing the familial Alzheimer's disease-associated presenilins. J. Neurochem., 72 (4), 1534-1543.
    • (1999) J. Neurochem. , vol.72 , Issue.4 , pp. 1534-1543
    • Parkin, E.T.1    Hussain, I.2    Karran, E.H.3    Turner, A.J.4    Hooper, N.M.5
  • 63
    • 57649217285 scopus 로고    scopus 로고
    • The role Main_Text of amyloid precursor protein processing by BACE1, the β-secretase, in Alzheimer disease pathophysiology
    • Cole, S.L. and Vassar, R. (2008) The role Main_Text of amyloid precursor protein processing by BACE1, the β-secretase, in Alzheimer disease pathophysiology. J. Biol. Chem., 283 (4), 29621-29625.
    • (2008) J. Biol. Chem. , vol.283 , Issue.4 , pp. 29621-29625
    • Cole, S.L.1    Vassar, R.2


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