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Volumn 47, Issue 3, 2000, Pages 725-733

Alzheimer's disease: Its origin at the membrane, evidence and questions

Author keywords

Alzheimer's disease; Lipid composition; Membrane microdomains; Membrane proteases; amyloid precursor protein

Indexed keywords

AMYLOID PRECURSOR PROTEIN; ASPARTIC PROTEINASE; BACE1 PROTEIN, HUMAN; MEMBRANE LIPID; PROTEINASE; SECRETASE;

EID: 0034576327     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.2000_3991     Document Type: Review
Times cited : (20)

References (49)
  • 1
    • 0028170818 scopus 로고
    • Cell biology of the amyloid β-protein precursor and the mechanism of Alzheimer's disease
    • Selkoe, D.J. (1994) Cell biology of the amyloid β-protein precursor and the mechanism of Alzheimer's disease. Annu. Rev. Cell Biol. 10, 373-403.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 373-403
    • Selkoe, D.J.1
  • 2
    • 0028883252 scopus 로고
    • Molecular genetics of Alzheimer disease: Identification of genes and gene mutations
    • Van Broeckhoven, C.L. (1995) Molecular genetics of Alzheimer disease: Identification of genes and gene mutations. Eur. Neurol. 35, 8-19.
    • (1995) Eur. Neurol. , vol.35 , pp. 8-19
    • Van Broeckhoven, C.L.1
  • 3
    • 0032814135 scopus 로고    scopus 로고
    • Alzheimer's disease and the amyloid β protein: What is the role of amyloid?
    • Small, D.H. & 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
  • 4
    • 0032939003 scopus 로고    scopus 로고
    • Amyloid precursor protein of Alzheimer's disease: Evidence for a stable, full-length, trans-membrane pool in primary neuronal cultures
    • Storey, E., Katz, M., Brickman, Y., Beyreuther, K. & Masters, C.L. (1999) Amyloid precursor protein of Alzheimer's disease: Evidence for a stable, full-length, trans-membrane pool in primary neuronal cultures. Eur. J. Neurosci. 11, 1779-1788.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 1779-1788
    • Storey, E.1    Katz, M.2    Brickman, Y.3    Beyreuther, K.4    Masters, C.L.5
  • 5
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • Hardy, J. (1997) Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci. 20, 154-159.
    • (1997) Trends Neurosci. , vol.20 , pp. 154-159
    • Hardy, J.1
  • 6
    • 0034237719 scopus 로고    scopus 로고
    • Energetics in the pathogenesis of neurodegenerative diseases
    • Flint Beal, M.F. (2000) Energetics in the pathogenesis of neurodegenerative diseases. Trends Neurosci. 23, 298-304.
    • (2000) Trends Neurosci. , vol.23 , pp. 298-304
    • Flint Beal, M.F.1
  • 7
    • 0002503154 scopus 로고    scopus 로고
    • β-Amyloid peptides as direct cholinergic neuro-modulators: A missing link?
    • Auld, D.S., Kar, S. & Quirion, R. (1998) β-Amyloid peptides as direct cholinergic neuro-modulators: A missing link? Trends Neurosci. 21, 43-49.
    • (1998) Trends Neurosci. , vol.21 , pp. 43-49
    • Auld, D.S.1    Kar, S.2    Quirion, R.3
  • 8
    • 0006325405 scopus 로고    scopus 로고
    • Alzheimer's disease: A re-examination of the amyloid hypothesis
    • Neve, R.L. & Robakis, N.K. (1998) Alzheimer's disease: A re-examination of the amyloid hypothesis. Trends Neurosci. 21, 15-19.
    • (1998) Trends Neurosci. , vol.21 , pp. 15-19
    • Neve, R.L.1    Robakis, N.K.2
  • 9
    • 0033213875 scopus 로고    scopus 로고
    • Rationalizing a pharmacological intervention on the amyloid precursor protein metabolism
    • Racchi, M. & Govoni, S. (1999) Rationalizing a pharmacological intervention on the amyloid precursor protein metabolism. Trends Pharmacol. Sci. 20, 418-423.
    • (1999) Trends Pharmacol. Sci. , vol.20 , pp. 418-423
    • Racchi, M.1    Govoni, S.2
  • 11
  • 12
    • 0031745753 scopus 로고    scopus 로고
    • Membrane instability, plasmalogen content, and Alzheimer's disease
    • Ginsberg, L., Xuereb, J.H. & Gershfeld, N.L. (1998) Membrane instability, plasmalogen content, and Alzheimer's disease. J. Neurochem. 70, 2533-2538.
    • (1998) J. Neurochem. , vol.70 , pp. 2533-2538
    • Ginsberg, L.1    Xuereb, J.H.2    Gershfeld, N.L.3
  • 13
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian, J.A. (1998) Hydrophobic mismatch between proteins and lipids in membranes. Biochim. Biophys. Acta 1376, 401-415.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 401-415
    • Killian, J.A.1
  • 14
    • 0033613129 scopus 로고    scopus 로고
    • Cellular mechanism of β-amyloid production and secretion
    • Sinha, S. & Lieberburg, I. (1999) Cellular mechanism of β-amyloid production and secretion. Proc. Natl. Acad. Sci. U.S.A. 96, 11049-11053.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 11049-11053
    • Sinha, S.1    Lieberburg, I.2
  • 15
    • 0031574374 scopus 로고    scopus 로고
    • Purification and spectroscopic characterization of β-amyloid precursor protein from porcine brains
    • de La Fournière-Bessueille, L., Grange, D. & Buchet, R. (1997) Purification and spectroscopic characterization of β-amyloid precursor protein from porcine brains. Eur. J. Biochem. 250, 705-711.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 705-711
    • De La Fournière-Bessueille, L.1    Grange, D.2    Buchet, R.3
  • 16
    • 0032513060 scopus 로고    scopus 로고
    • Cleavage of Alzheimer's amyloid precursor protein (APP) by secretases occurs after O-glycosylation of APP in the protein secretory pathway. Identification of intracellular compartments in which APP cleavage occurs without using toxic agents that interfere with protein metabolism
    • Tomita, S., Kirino, Y. & Suzuki, T. (1998) Cleavage of Alzheimer's amyloid precursor protein (APP) by secretases occurs after O-glycosylation of APP in the protein secretory pathway. Identification of intracellular compartments in which APP cleavage occurs without using toxic agents that interfere with protein metabolism. J. Biol. Chem. 273, 6277-6284.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6277-6284
    • Tomita, S.1    Kirino, Y.2    Suzuki, T.3
  • 17
    • 0033609449 scopus 로고    scopus 로고
    • Cleavage of Alzheimer's amyloid precursor protein by α-secretase occurs at the surface of neuronal cells
    • Parvathy, S., Hussain, I., Karran, E.H., Turner, A.J. & Hooper, N.M. (1999) Cleavage of Alzheimer's amyloid precursor protein by α-secretase occurs at the surface of neuronal cells. Biochemistry 38, 9728-9734.
    • (1999) Biochemistry , vol.38 , pp. 9728-9734
    • Parvathy, S.1    Hussain, I.2    Karran, E.H.3    Turner, A.J.4    Hooper, N.M.5
  • 18
    • 0032983125 scopus 로고    scopus 로고
    • A notable cleavage: Winding up with β-amyloid
    • Kosik, K.S. (1999) A notable cleavage: Winding up with β-amyloid. Proc. Natl. Acad. Sci. U.S.A. 96, 2574-2576.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 2574-2576
    • Kosik, K.S.1
  • 20
    • 0033621152 scopus 로고    scopus 로고
    • Are presenilins intramembrane-cleaving proteases? Implications for the molecular mechanism of Alzheimer's diseases
    • Wolfe, M.S., De Los Angeles, J., Miller, D.D., Xia, W. & Selkoe, D.J. (1999) Are presenilins intramembrane-cleaving proteases? Implications for the molecular mechanism of Alzheimer's diseases. Biochemistry 38, 11223-11230.
    • (1999) Biochemistry , vol.38 , pp. 11223-11230
    • Wolfe, M.S.1    De Los Angeles, J.2    Miller, D.D.3    Xia, W.4    Selkoe, D.J.5
  • 21
    • 0030720936 scopus 로고    scopus 로고
    • Mutations in the transmembrane domain of APP altering γ-secretase specificity
    • Lichtenthaler, S.F., Ida, N., Multhaup, G., Masters, C.L. & Beyreuther, K. (1997) Mutations in the transmembrane domain of APP altering γ-secretase specificity. Biochemistry 36, 15396-15403.
    • (1997) Biochemistry , vol.36 , pp. 15396-15403
    • Lichtenthaler, S.F.1    Ida, N.2    Multhaup, G.3    Masters, C.L.4    Beyreuther, K.5
  • 22
    • 0032502033 scopus 로고    scopus 로고
    • Alzheimer's amyloid precursor protein α-secretase is inhibited by hydroxamic acid-based zinc metallo-protease inhibitors: Similarities to the angiotensin converting enzyme secretase
    • Parvathy, S., Hussain, I., Karran, E.H., Turner, A.J. & Hooper, N.M. (1998) Alzheimer's amyloid precursor protein α-secretase is inhibited by hydroxamic acid-based zinc metallo-protease inhibitors: Similarities to the angiotensin converting enzyme secretase. Biochemistry 37, 1680-1685.
    • (1998) Biochemistry , vol.37 , pp. 1680-1685
    • Parvathy, S.1    Hussain, I.2    Karran, E.H.3    Turner, A.J.4    Hooper, N.M.5
  • 27
    • 0034652309 scopus 로고    scopus 로고
    • Human aspartic protease memapsin 2 cleaves the β-secretase site of β-amyloid precursor protein
    • Lin, X., Koelsch, G., Wu, S., Downs, D., Dashti, A. & Tang, J. (2000) Human aspartic protease memapsin 2 cleaves the β-secretase site of β-amyloid precursor protein. Proc. Natl. Acad. Sci. U.S.A. 97, 1456-1460.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 1456-1460
    • Lin, X.1    Koelsch, G.2    Wu, S.3    Downs, D.4    Dashti, A.5    Tang, J.6
  • 28
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
    • Wolfe, M.S., Xia, W., Ostaszewski, B.L., Diehl, T.S., Kimberly, W.T. & Selkoe, D.J. (1999) Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity. Nature 398, 513-517.
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.J.6
  • 30
    • 0033535508 scopus 로고    scopus 로고
    • Presenilin is required for activity and nuclear access of Notch in Drosophila
    • Struhl, G. & Greenwald, I. (1999) Presenilin is required for activity and nuclear access of Notch in Drosophila. Nature 398, 522-525.
    • (1999) Nature , vol.398 , pp. 522-525
    • Struhl, G.1    Greenwald, I.2
  • 31
    • 0033535555 scopus 로고    scopus 로고
    • Neurogenic phenotypes and altered Notch processing in Drosophila Presenilin mutants
    • Ye, Y., Lukinova, N. & Fortini, M.E. (1999) Neurogenic phenotypes and altered Notch processing in Drosophila Presenilin mutants. Nature 398, 525-529.
    • (1999) Nature , vol.398 , pp. 525-529
    • Ye, Y.1    Lukinova, N.2    Fortini, M.E.3
  • 33
    • 0030772145 scopus 로고    scopus 로고
    • The amyloid precursor protein is not enriched in caveolae-like, detergent-insoluble membrane microdomains
    • Parkin, E.T., Hussain, I., Turner, A.J. & Hoper, N.M. (1997) The amyloid precursor protein is not enriched in caveolae-like, detergent-insoluble membrane microdomains. J. Neurochem. 69, 2179-2188.
    • (1997) J. Neurochem. , vol.69 , pp. 2179-2188
    • Parkin, E.T.1    Hussain, I.2    Turner, A.J.3    Hoper, N.M.4
  • 34
    • 0033992140 scopus 로고    scopus 로고
    • Amyloid precursor protein in unique cholesterol-rich microdomains different from caveolae-like domains
    • Hayashi, H., Mizuno, T., Michikawa, M., Haass, C. & Yanagisawa, K. (2000) Amyloid precursor protein in unique cholesterol-rich microdomains different from caveolae-like domains. Biochim. Biophys. Acta 1483, 81-90.
    • (2000) Biochim. Biophys. Acta , vol.1483 , pp. 81-90
    • Hayashi, H.1    Mizuno, T.2    Michikawa, M.3    Haass, C.4    Yanagisawa, K.5
  • 35
    • 0033571721 scopus 로고    scopus 로고
    • Amyloid precursor protein, although partially detergent-insoluble in mouse cerebral cortex, behaves as an atypical lipid raft protein
    • Parkin, E.T., Turner, A.J. & Hoper, N.M. (1999) Amyloid precursor protein, although partially detergent-insoluble in mouse cerebral cortex, behaves as an atypical lipid raft protein. Biochem. J. 344, 23-30.
    • (1999) Biochem. J. , vol.344 , pp. 23-30
    • Parkin, E.T.1    Turner, A.J.2    Hoper, N.M.3
  • 37
    • 0032562615 scopus 로고    scopus 로고
    • Caveolae, plasma membrane microdomains for α-secretase-mediated processing of the amyloid precursor protein
    • Ikezu, T., Trapp, B.D., Song, K.S., Schlegel, A., Lisanti, M.P. & Okamoto, T. (1998) Caveolae, plasma membrane microdomains for α-secretase-mediated processing of the amyloid precursor protein. J. Biol. Chem. 273, 10485-10495.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10485-10495
    • Ikezu, T.1    Trapp, B.D.2    Song, K.S.3    Schlegel, A.4    Lisanti, M.P.5    Okamoto, T.6
  • 38
    • 0032480771 scopus 로고    scopus 로고
    • The presence of amyloid β-protein in the detergent-insoluble membrane compartment of human neuroblastoma cells
    • Morishima-Kawashima, M. & Ihara, Y. (1998) The presence of amyloid β-protein in the detergent-insoluble membrane compartment of human neuroblastoma cells. Biochemistry 37, 15247-15253.
    • (1998) Biochemistry , vol.37 , pp. 15247-15253
    • Morishima-Kawashima, M.1    Ihara, Y.2
  • 39
    • 0032999907 scopus 로고    scopus 로고
    • Characterization of detergentrinsoluble complexes containing the familial Alzheimer's disease-associated presenilins
    • Parkin, E.P., Hussain, I., Karran, E.H., Turner, A.J. & Hooper, N.M. (1999) Characterization of detergentrinsoluble complexes containing the familial Alzheimer's disease-associated presenilins. J. Neurochem. 72, 1534-1543.
    • (1999) J. Neurochem. , vol.72 , pp. 1534-1543
    • Parkin, E.P.1    Hussain, I.2    Karran, E.H.3    Turner, A.J.4    Hooper, N.M.5
  • 40
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike, C.J., Burdick, D., Walencewicz, A.J., Glabe, C.G. & Cotman, C.W. (1993) Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state. J. Neurosci. 13, 1676-1687.
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 43
    • 0031765281 scopus 로고    scopus 로고
    • Membrane perturbation by neurotoxic Alzheimer amyloid fragment β25-35 requires aggregation and β-sheet formation
    • Hirakura, Y., Satoh, Y., Hirashima, N., Suzuki, T., Kagan, B.L. & Kirino, Y. (1998) Membrane perturbation by neurotoxic Alzheimer amyloid fragment β25-35 requires aggregation and β-sheet formation. Biochem. Molec. Biol. Int. 46, 787-794.
    • (1998) Biochem. Molec. Biol. Int. , vol.46 , pp. 787-794
    • Hirakura, Y.1    Satoh, Y.2    Hirashima, N.3    Suzuki, T.4    Kagan, B.L.5    Kirino, Y.6
  • 44
    • 0032562547 scopus 로고    scopus 로고
    • Phosphatidylinositol and inositol involvement in Alzheimer amyloid-β fibril growth and arrest
    • McLaurin, J., Franklin, T., Chakrabartty, A. & Fraser, P.E. (1998) Phosphatidylinositol and inositol involvement in Alzheimer amyloid-β fibril growth and arrest. J. Mol. Biol. 278, 183-194.
    • (1998) J. Mol. Biol. , vol.278 , pp. 183-194
    • McLaurin, J.1    Franklin, T.2    Chakrabartty, A.3    Fraser, P.E.4
  • 45
    • 0030823756 scopus 로고    scopus 로고
    • Acceleration of amyloid fibril formation by specific binding of Aβ-(1-40) peptide to ganglioside-containing membrane vesicles
    • Choo-Smith, L.-P., Garzon-Rodriguez, W., Glabe, C.G. & Surewicz, W.K. (1997) Acceleration of amyloid fibril formation by specific binding of Aβ-(1-40) peptide to ganglioside-containing membrane vesicles. J. Biol. Chem. 272, 22987-22990.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22987-22990
    • Choo-Smith, L.-P.1    Garzon-Rodriguez, W.2    Glabe, C.G.3    Surewicz, W.K.4
  • 46
    • 0033616779 scopus 로고    scopus 로고
    • Interactions of amyloid β-peptide (1-40) with ganglioside-containing membranes
    • Matsuzaki, K. & Horikiri, C. (1999) Interactions of amyloid β-peptide (1-40) with ganglioside-containing membranes. Biochemistry 38, 4137-4142.
    • (1999) Biochemistry , vol.38 , pp. 4137-4142
    • Matsuzaki, K.1    Horikiri, C.2
  • 47
    • 0033569981 scopus 로고    scopus 로고
    • Structure of the Alzheimer β-amyloid peptide (25-35) and its interaction with negatively charged phospholipid vesicles
    • del Mar Martínez-Senac, M., Villalaín, J. & Gómez-Fernández, J.C. (1999) Structure of the Alzheimer β-amyloid peptide (25-35) and its interaction with negatively charged phospholipid vesicles. Eur. J. Biochem. 265, 744-753.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 744-753
    • Del Mar Martínez-Senac, M.1    Villalaín, J.2    Gómez-Fernández, J.C.3
  • 48
    • 0027508926 scopus 로고
    • Alzheimer disease amyloid β protein forms calcium channels in bilayer membranes: Blockade by tromethamine and aluminum
    • Arispe, M., Rojas, E. & Pollard, H.B. (1993) Alzheimer disease amyloid β protein forms calcium channels in bilayer membranes: Blockade by tromethamine and aluminum. Proc. Natl. Acad. Sci. U.S.A. 90, 567-571.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 567-571
    • Arispe, M.1    Rojas, E.2    Pollard, H.B.3
  • 49
    • 0033600590 scopus 로고    scopus 로고
    • 2+-sensitive channels in reconstituted lipid vesicles
    • 2+-sensitive channels in reconstituted lipid vesicles. Biochemistry 38, 11189-11196.
    • (1999) Biochemistry , vol.38 , pp. 11189-11196
    • Lin, H.1    Zhu, Y.J.2    Lal, R.3


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