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Volumn 450, Issue 1, 2013, Pages 189-197

Ca2+ enhances Aβ polymerization rate and fibrillar stability in a dynamic manner

Author keywords

Amyloid; Amyloid peptide (A ); Atomic force microscopy (AFM); Ca2+; NMR; Surface plasmon resonance (SPR)

Indexed keywords

AMYLOID BETA PROTEIN; CALCIUM ION; MONOMER;

EID: 84873020544     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20121583     Document Type: Article
Times cited : (24)

References (45)
  • 1
    • 0242298785 scopus 로고    scopus 로고
    • Distinct presenilin-dependent and presenilin-independent gamma-secretases are responsible for total cellular Aβ production
    • Wilson, C. A., Doms, R. W. and Lee, V. M. (2003) Distinct presenilin-dependent and presenilin-independent gamma-secretases are responsible for total cellular Aβ production. J. Neurosci. Res. 74, 361-369
    • (2003) J. Neurosci. Res. , vol.74 , pp. 361-369
    • Wilson, C.A.1    Doms, R.W.2    Lee, V.M.3
  • 2
    • 0028169925 scopus 로고
    • Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)
    • Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nukina, N. and Ihara, Y. (1994) Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: evidence that an initially deposited species is Aβ42(43). Neuron 13, 45-53
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 3
    • 0027425060 scopus 로고
    • The C-terminus of the β protein is critical in amyloidogenesis
    • Jarrett, J. T., Berger, E. P. and Lansbury, Jr, P. T. (1993) The C-terminus of the β protein is critical in amyloidogenesis. Ann. N.Y. Acad. Sci. 695, 144-148
    • (1993) Ann. N.Y. Acad. Sci. , vol.695 , pp. 144-148
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 5
    • 70350036064 scopus 로고    scopus 로고
    • Demonstration of aluminum in amyloid fibers in the cores of senile plaques in the brains of patients with Alzheimer's disease
    • Yumoto, S., Kakimi, S., Ohsaki, A. and Ishikawa, A. (2009) Demonstration of aluminum in amyloid fibers in the cores of senile plaques in the brains of patients with Alzheimer's disease. J. Inorg. Biochem. 103, 1579-1584
    • (2009) J. Inorg. Biochem. , vol.103 , pp. 1579-1584
    • Yumoto, S.1    Kakimi, S.2    Ohsaki, A.3    Ishikawa, A.4
  • 6
    • 23844434035 scopus 로고    scopus 로고
    • Aluminum-triggered structural modifications and aggregation of β-amyloids
    • Ricchelli, F., Drago, D., Filippi, B., Tognon, G. and Zatta, P. (2005) Aluminum-triggered structural modifications and aggregation of β-amyloids. Cell. Mol. Life Sci. 62, 1724-1733
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 1724-1733
    • Ricchelli, F.1    Drago, D.2    Filippi, B.3    Tognon, G.4    Zatta, P.5
  • 7
    • 0035872393 scopus 로고    scopus 로고
    • Effects of aluminum on the neurotoxicity of primary cultured neurons and on the aggregation of beta-amyloid protein
    • Kawahara, M., Kato, M. and Kuroda, Y. (2001) Effects of aluminum on the neurotoxicity of primary cultured neurons and on the aggregation of beta-amyloid protein. Brain Res. Bull. 55, 211-217
    • (2001) Brain Res. Bull. , vol.55 , pp. 211-217
    • Kawahara, M.1    Kato, M.2    Kuroda, Y.3
  • 8
    • 34249041646 scopus 로고    scopus 로고
    • Metal ions differentially influence the aggregation and deposition of Alzheimer's β-amyloid on a solid template
    • Ha, C., Ryu, J. and Park, C. B. (2007) Metal ions differentially influence the aggregation and deposition of Alzheimer's β-amyloid on a solid template. Biochemistry 46, 6118-6125
    • (2007) Biochemistry , vol.46 , pp. 6118-6125
    • Ha, C.1    Ryu, J.2    Park, C.B.3
  • 11
    • 15244352734 scopus 로고    scopus 로고
    • Calcium dysregulation, IP3 signaling, and Alzheimer's disease
    • Stutzmann, G. E. (2005) Calcium dysregulation, IP3 signaling, and Alzheimer's disease. Neuroscientist 11, 110-115
    • (2005) Neuroscientist , vol.11 , pp. 110-115
    • Stutzmann, G.E.1
  • 12
    • 0030891662 scopus 로고    scopus 로고
    • Alzheimer's PS-1 mutation perturbs calcium homeostasis and sensitizes PC12 cells to death induced by amyloid β-peptide
    • Guo, Q., Furukawa, K., Sopher, B. L., Pham, D. G., Xie, J., Robinson, N., Martin, G. M. and Mattson, M. P. (1996) Alzheimer's PS-1 mutation perturbs calcium homeostasis and sensitizes PC12 cells to death induced by amyloid β-peptide. NeuroReport 8, 379-383
    • (1996) NeuroReport , vol.8 , pp. 379-383
    • Guo, Q.1    Furukawa, K.2    Sopher, B.L.3    Pham, D.G.4    Xie, J.5    Robinson, N.6    Martin, G.M.7    Mattson, M.P.8
  • 13
    • 0042268132 scopus 로고    scopus 로고
    • Dysregulation of calcium in Alzheimer's disease
    • Brzyska, M. and Elbaum, D. (2003) Dysregulation of calcium in Alzheimer's disease. Acta Neurobiol. Exp. 63, 171-183
    • (2003) Acta Neurobiol. Exp. , vol.63 , pp. 171-183
    • Brzyska, M.1    Elbaum, D.2
  • 14
    • 79960247207 scopus 로고    scopus 로고
    • Calcium homoeostasis modulator 1 (CALHM1) reduces the calcium content of the endoplasmic reticulum (ER) and triggers ER stress
    • Gallego-Sandin, S., Alonso, M. T. and Garcia-Sancho, J. (2011) Calcium homoeostasis modulator 1 (CALHM1) reduces the calcium content of the endoplasmic reticulum (ER) and triggers ER stress. Biochem. J. 437, 469-475
    • (2011) Biochem. J. , vol.437 , pp. 469-475
    • Gallego-Sandin, S.1    Alonso, M.T.2    Garcia-Sancho, J.3
  • 15
    • 33748767364 scopus 로고    scopus 로고
    • Acceleration of amyloid β-peptide aggregation by physiological concentrations of calcium
    • Isaacs, A. M., Senn, D. B., Yuan, M., Shine, J. P. and Yankner, B. A. (2006) Acceleration of amyloid β-peptide aggregation by physiological concentrations of calcium. J. Biol. Chem. 281, 27916-27923
    • (2006) J. Biol. Chem. , vol.281 , pp. 27916-27923
    • Isaacs, A.M.1    Senn, D.B.2    Yuan, M.3    Shine, J.P.4    Yankner, B.A.5
  • 16
    • 79953141820 scopus 로고    scopus 로고
    • Calcium ions promote formation of amyloid β-peptide (1-40) oligomers causally implicated in neuronal toxicity of Alzheimer's disease
    • Itkin, A., Dupres, V., Dufrene, Y. F., Bechinger, B., Ruysschaert, J. M. and Raussens, V. (2011) Calcium ions promote formation of amyloid β-peptide (1-40) oligomers causally implicated in neuronal toxicity of Alzheimer's disease. PLoS ONE 6, e18250
    • (2011) PLoS ONE , vol.6
    • Itkin, A.1    Dupres, V.2    Dufrene, Y.F.3    Bechinger, B.4    Ruysschaert, J.M.5    Raussens, V.6
  • 17
    • 0032701484 scopus 로고    scopus 로고
    • Improving biosensor analysis
    • Myszka, D. G. (1999) Improving biosensor analysis. J. Mol. Recognit. 12, 279-284
    • (1999) J. Mol. Recognit. , vol.12 , pp. 279-284
    • Myszka, D.G.1
  • 18
    • 33644818046 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of Aβ1-40 amyloid fibril stability
    • Williams, A. D., Shivaprasad, S. and Wetzel, R. (2006) Alanine scanning mutagenesis of Aβ1-40 amyloid fibril stability. J. Mol. Biol. 357, 1283-1294
    • (2006) J. Mol. Biol. , vol.357 , pp. 1283-1294
    • Williams, A.D.1    Shivaprasad, S.2    Wetzel, R.3
  • 20
    • 80053294730 scopus 로고    scopus 로고
    • Aβ peptide fibrillar architectures controlled by conformational constraints of the monomer
    • Brannstrom, K., Ohman, A. and Olofsson, A. (2011) Aβ peptide fibrillar architectures controlled by conformational constraints of the monomer. PLoS ONE 6, e25157
    • (2011) PLoS ONE , vol.6
    • Brannstrom, K.1    Ohman, A.2    Olofsson, A.3
  • 21
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 22
    • 34249765651 scopus 로고
    • NMR View: A computer program for the visualization and analysis of NMR data
    • Johnson, B. A. and Blevins, R. A. (1994) NMR View: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4, 603-614
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 23
    • 33746335362 scopus 로고    scopus 로고
    • NMR reveals anomalous copper(II) binding to the amyloid Aβ peptide of Alzheimer's disease
    • Hou, L. and Zagorski, M. G. (2006) NMR reveals anomalous copper(II) binding to the amyloid Aβ peptide of Alzheimer's disease. J. Am. Chem. Soc. 128, 9260-9261
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 9260-9261
    • Hou, L.1    Zagorski, M.G.2
  • 24
    • 33644851439 scopus 로고    scopus 로고
    • The solvent protection of alzheimer amyloid-β-(1-42) fibrils as determined by solution NMR spectroscopy
    • Olofsson, A., Sauer-Eriksson, A. E. and Ohman, A. (2006) The solvent protection of alzheimer amyloid-β-(1-42) fibrils as determined by solution NMR spectroscopy. J. Biol. Chem. 281, 477-483
    • (2006) J. Biol. Chem. , vol.281 , pp. 477-483
    • Olofsson, A.1    Sauer-Eriksson, A.E.2    Ohman, A.3
  • 25
    • 34249051698 scopus 로고    scopus 로고
    • Amide solvent protection analysis demonstrate that Amyloid-β1-40 and Amyloid-β1-42 form different fibrillar structures under identical conditions
    • Olofsson, A., Lindhagen-Persson, M., Sauer-Eriksson, A. E. and Ohman, A. (2007) Amide solvent protection analysis demonstrate that Amyloid-β1-40 and Amyloid-β1-42 form different fibrillar structures under identical conditions. Biochem. J. 404, 63-70
    • (2007) Biochem. J. , vol.404 , pp. 63-70
    • Olofsson, A.1    Lindhagen-Persson, M.2    Sauer-Eriksson, A.E.3    Ohman, A.4
  • 27
    • 58149376285 scopus 로고    scopus 로고
    • Amyloid fibril dynamics revealed by combined hydrogen/deuterium exchange and nuclear magnetic resonance
    • Olofsson, A., Sauer-Eriksson, A. E. and Ohman, A. (2009) Amyloid fibril dynamics revealed by combined hydrogen/deuterium exchange and nuclear magnetic resonance. Anal. Biochem. 385, 374-376
    • (2009) Anal. Biochem. , vol.385 , pp. 374-376
    • Olofsson, A.1    Sauer-Eriksson, A.E.2    Ohman, A.3
  • 30
    • 33744510885 scopus 로고    scopus 로고
    • Kinetic analysis of β-amyloid peptide aggregation induced by metal ions based on surface plasmon resonance biosensing
    • Hu, W. P., Chang, G. L., Chen, S. J. and Kuo, Y. M. (2006) Kinetic analysis of β-amyloid peptide aggregation induced by metal ions based on surface plasmon resonance biosensing. J. Neurosci. Methods 154, 190-197
    • (2006) J. Neurosci. Methods , vol.154 , pp. 190-197
    • Hu, W.P.1    Chang, G.L.2    Chen, S.J.3    Kuo, Y.M.4
  • 31
    • 0037137225 scopus 로고    scopus 로고
    • Kinetic modeling and determination of reaction constants of Alzheimer's β-amyloid fibril extension and dissociation using surface plasmon resonance
    • Hasegawa, K., Ono, K., Yamada, M. and Naiki, H. (2002) Kinetic modeling and determination of reaction constants of Alzheimer's β-amyloid fibril extension and dissociation using surface plasmon resonance. Biochemistry 41, 13489-13498
    • (2002) Biochemistry , vol.41 , pp. 13489-13498
    • Hasegawa, K.1    Ono, K.2    Yamada, M.3    Naiki, H.4
  • 32
    • 79960017316 scopus 로고    scopus 로고
    • New therapeutic targets in Alzheimer's disease: Brain deregulation of calcium and zinc
    • Corona, C., Pensalfini, A., Frazzini, V. and Sensi, S. L. (2011) New therapeutic targets in Alzheimer's disease: brain deregulation of calcium and zinc. Cell Death Dis. 2, e176
    • (2011) Cell Death Dis. , vol.2
    • Corona, C.1    Pensalfini, A.2    Frazzini, V.3    Sensi, S.L.4
  • 33
    • 34548823253 scopus 로고    scopus 로고
    • The pathogenesis of Alzheimers disease is it a lifelong 'calciumopathy'?
    • Stutzmann, G. E. (2007) The pathogenesis of Alzheimers disease is it a lifelong 'calciumopathy'? Neuroscientist 13, 546-559
    • (2007) Neuroscientist , vol.13 , pp. 546-559
    • Stutzmann, G.E.1
  • 34
    • 79953141820 scopus 로고    scopus 로고
    • Calcium ions promote formation of amyloid β-peptide1-40 oligomers causally implicated in neuronal toxicity of Alzheimer's disease
    • Itkin, A., Dupres, V., Dufrene, Y. F., Bechinger, B., Ruysschaert, J. M. and Raussens, V. (2011) Calcium ions promote formation of amyloid β-peptide1-40 oligomers causally implicated in neuronal toxicity of Alzheimer's disease. PLoS ONE 6, e18250
    • (2011) PLoS ONE , vol.6
    • Itkin, A.1    Dupres, V.2    Dufrene, Y.F.3    Bechinger, B.4    Ruysschaert, J.M.5    Raussens, V.6
  • 36
    • 35748954015 scopus 로고    scopus 로고
    • The cytosolic N-terminus of presenilin-1 potentiates mouse ryanodine receptor single channel activity
    • Rybalchenko, V., Hwang, S. Y., Rybalchenko, N. and Koulen, P. (2008) The cytosolic N-terminus of presenilin-1 potentiates mouse ryanodine receptor single channel activity. Int. J. Biochem. Cell Biol. 40, 84-97
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 84-97
    • Rybalchenko, V.1    Hwang, S.Y.2    Rybalchenko, N.3    Koulen, P.4
  • 38
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivoby the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
    • Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W. et al. (1996) Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivoby the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nat. Med. 2, 864-870
    • (1996) Nat. Med. , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3    Song, X.4    Citron, M.5    Suzuki, N.6    Bird, T.D.7    Hardy, J.8    Hutton, M.9    Kukull, W.10
  • 41
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J. and Selkoe, D. J. (2002) Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 43
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers: A decade of discovery
    • Walsh, D. M. and Selkoe, D. J. (2007) Aβ oligomers: a decade of discovery. J. Neurochem. 101, 1172-1184
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 44
    • 78649754766 scopus 로고    scopus 로고
    • Amyloid-β oligomer specificity mediated by the IgM isotype: Implications for a specific protective mechanism exerted by endogenous auto-antibodies
    • Lindhagen-Persson, M., Brannstrom, K., Vestling, M., Steinitz, M. and Olofsson, A. (2010) Amyloid-β oligomer specificity mediated by the IgM isotype: implications for a specific protective mechanism exerted by endogenous auto-antibodies. PLoS ONE 5, e13928
    • (2010) PLoS ONE , vol.5
    • Lindhagen-Persson, M.1    Brannstrom, K.2    Vestling, M.3    Steinitz, M.4    Olofsson, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.