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Short Communications |
From the Laboratory of Molecular and Cellular
Neuroscience*
and Fisher Center for Research on
Alzheimer’s Disease,
The Rockefeller
University; the Departments of Neurology and
Neuroscience
and
Pathology,||
Weill Medical College of Cornell
University; Mount Sinai School of Medicine,||
New York,
New York; and Institute de Pharmacologie Moleculaire et
Cellulaire,¶
Valbonne, France
Alzheimer’s disease (AD) is characterized by the deposition of
senile plaques (SPs) and neurofibrillary tangles (NFTs) in vulnerable
brain regions. SPs are composed of aggregated ß-amyloid (Aß)
40/42(43) peptides. Evidence implicates a central role for Aß in the
pathophysiology of AD. Mutations in ßAPP and presenilin 1 (PS1) lead
to elevated secretion of Aß, especially the more
amyloidogenic Aß42. Immunohistochemical studies have also emphasized
the importance of Aß42 in initiating plaque pathology. Cell
biological studies have demonstrated that Aß is generated
intracellularly. Recently, endogenous Aß42 staining was
demonstrated within cultured neurons by confocal immunofluorescence
microscopy and within neurons of PS1 mutant transgenic mice. A central
question about the role of Aß in disease concerns whether
extracellular Aß deposition or intracellular Aß accumulation
initiates the disease process. Here we report that human neurons in
AD-vulnerable brain regions specifically accumulate 
-cleaved Aß42
and suggest that this intraneuronal Aß42 immunoreactivity appears to
precede both NFT and Aß plaque deposition. This study suggests that
intracellular Aß42 accumulation is an early event in neuronal
dysfunction and that preventing intraneuronal Aß42 aggregation
may be an important therapeutic direction for the treatment of
AD.
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H.-Y. Wang, W. Li, N. J. Benedetti, and D. H. S. Lee {alpha}7 Nicotinic Acetylcholine Receptors Mediate {beta}-Amyloid Peptide-induced Tau Protein Phosphorylation J. Biol. Chem., August 22, 2003; 278(34): 31547 - 31553. [Abstract] [Full Text] [PDF]
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M. Hoshi, M. Sato, S. Matsumoto, A. Noguchi, K. Yasutake, N. Yoshida, and K. Sato Spherical aggregates of {beta}-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3{beta} PNAS, May 27, 2003; 100(11): 6370 - 6375. [Abstract] [Full Text] [PDF]
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E. B. Lee, D. M. Skovronsky, F. Abtahian, R. W. Doms, and V. M.-Y. Lee Secretion and Intracellular Generation of Truncated Abeta in beta -Site Amyloid-beta Precursor Protein-cleaving Enzyme Expressing Human Neurons J. Biol. Chem., February 7, 2003; 278(7): 4458 - 4466. [Abstract] [Full Text] [PDF]
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F. Dou, W. J. Netzer, K. Tanemura, F. Li, F. U. Hartl, A. Takashima, G. K. Gouras, P. Greengard, and H. Xu Chaperones increase association of tau protein with microtubules PNAS, January 21, 2003; 100(2): 721 - 726. [Abstract] [Full Text] [PDF]
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M. H. Mohajeri, K. Saini, J. G. Schultz, M. A. Wollmer, C. Hock, and R. M. Nitsch Passive Immunization against beta -Amyloid Peptide Protects Central Nervous System (CNS) Neurons from Increased Vulnerability Associated with an Alzheimer's Disease-causing Mutation J. Biol. Chem., August 30, 2002; 277(36): 33012 - 33017. [Abstract] [Full Text] [PDF]
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V. Fonte, V. Kapulkin, A. Taft, A. Fluet, D. Friedman, and C. D. Link Interaction of intracellular beta amyloid peptide with chaperone proteins PNAS, July 9, 2002; 99(14): 9439 - 9444. [Abstract] [Full Text] [PDF]
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M. Riemenschneider, S. Wagenpfeil, J. Diehl, N. Lautenschlager, T. Theml, B. Heldmann, A. Drzezga, T. Jahn, H. Forstl, and A. Kurz Tau and A{beta}42 protein in CSF of patients with frontotemporal degeneration Neurology, June 11, 2002; 58(11): 1622 - 1628. [Abstract] [Full Text] [PDF]
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P. Kienlen-Campard, S. Miolet, B. Tasiaux, and J.-N. Octave Intracellular Amyloid-beta 1-42, but Not Extracellular Soluble Amyloid-beta Peptides, Induces Neuronal Apoptosis J. Biol. Chem., May 3, 2002; 277(18): 15666 - 15670. [Abstract] [Full Text] [PDF]
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M. C. Sugarman, T. R. Yamasaki, S. Oddo, J. C. Echegoyen, M. P. Murphy, T. E. Golde, M. Jannatipour, M. A. Leissring, and F. M. LaFerla Inclusion body myositis-like phenotype induced by transgenic overexpression of beta APP in skeletal muscle PNAS, April 30, 2002; 99(9): 6334 - 6339. [Abstract] [Full Text] [PDF]
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A. Deng, M. C. Irizarry, R. M. Nitsch, J. H. Growdon, and G. W. Rebeck Elevation of Cystatin C in Susceptible Neurons in Alzheimer's Disease Am. J. Pathol., September 1, 2001; 159(3): 1061 - 1068. [Abstract] [Full Text] [PDF]
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L. Gasparini, G. K. Gouras, R. Wang, R. S. Gross, M. F. Beal, P. Greengard, and H. Xu Stimulation of {beta}-Amyloid Precursor Protein Trafficking by Insulin Reduces Intraneuronal {beta}-Amyloid and Requires Mitogen-Activated Protein Kinase Signaling J. Neurosci., April 15, 2001; 21(8): 2561 - 2570. [Abstract] [Full Text] [PDF]
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J.-H. Kim, R. Anwyl, Y.-H. Suh, M. B. A. Djamgoz, and M. J. Rowan Use-Dependen |
