We are analyzing https://link.springer.com/article/10.1007/s00401-007-0312-8.

Title:
Alzheimer disease models and human neuropathology: similarities and differences | Acta Neuropathologica
Description:
Animal models aim to replicate the symptoms, the lesions or the cause(s) of Alzheimer disease. Numerous mouse transgenic lines have now succeeded in partially reproducing its lesions: the extracellular deposits of Aβ peptide and the intracellular accumulation of tau protein. Mutated human APP transgenes result in the deposition of Aβ peptide, similar but not identical to the Aβ peptide of human senile plaque. Amyloid angiopathy is common. Besides the deposition of Aβ, axon dystrophy and alteration of dendrites have been observed. All of the mutations cause an increase in Aβ 42 levels, except for the Arctic mutation, which alters the Aβ sequence itself. Overexpressing wild-type APP alone (as in the murine models of human trisomy 21) causes no Aβ deposition in most mouse lines. Doubly (APP × mutated PS1) transgenic mice develop the lesions earlier. Transgenic mice in which BACE1 has been knocked out or overexpressed have been produced, as well as lines with altered expression of neprilysin, the main degrading enzyme of Aβ. The APP transgenic mice have raised new questions concerning the mechanisms of neuronal loss, the accumulation of Aβ in the cell body of the neurons, inflammation and gliosis, and the dendritic alterations. They have allowed some insight to be gained into the kinetics of the changes. The connection between the symptoms, the lesions and the increase in Aβ oligomers has been found to be difficult to unravel. Neurofibrillary tangles are only found in mouse lines that overexpress mutated tau or human tau on a murine tau −/− background. A triply transgenic model (mutated APP, PS1 and tau) recapitulates the alterations seen in AD but its physiological relevance may be discussed. A number of modulators of Aβ or of tau accumulation have been tested. A transgenic model may be analyzed at three levels at least (symptoms, lesions, cause of the disease), and a reading key is proposed to summarize this analysis.
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Keywords {🔍}

mice, google, scholar, pubmed, cas, article, transgenic, amyloid, app, tau, mouse, disease, human, alzheimers, deposits, protein, peptide, model, brain, deposition, pathology, apoe, neurosci, line, neuronal, gene, plaque, accumulation, mutation, van, loss, precursor, neurobiol, observed, lines, abeta, alzheimer, models, expressing, expression, found, plaques, increased, cognitive, happ, promoter, lesions, neurons, intracellular, aging,

Topics {✒️}

beta-site app-cleaving enzyme amyloid beta-protein-induced neurodegeneration hmg-coa reductase promoter article download pdf beta-amyloid-precursor protein app[v717i] double-transgenic mice app × ps1—ki lines developed amyloid-beta attenuates alzheimer-disease abeta oligomer-induced aberrations nmda-type glutamate receptor tetracycline operon-responsive element p1-derived artificial chromosomes β-secretase cleavage site β-pleated sheet structures bone-marrow-derived cells contribute beta-amyloid protein injections tgf-β1 overexpression promoted chartier-harlin mc nanoelectrospray/tandem mass spectrometry manganese-dependent superoxide dismutase circulating beta-amyloid peptide loxp/cre-recombinase strategy mapt×p301s transgenic mice membrane-embedded proteolytic ensemble mice expressing beta-app695 overexpressing wild-type app cerebral beta-amyloid angiopathy preserved fronto-striatal plasticity stable beta-amyloid deposition intraneuronal beta-amyloid aggregates × wild-type α-synuclein amyloid-beta chemical structure polyclonal anti-aβ42 antibody presenilin-1 double-transgenic mice alzheimer beta-amyloid peptides nonprogressive transgene-related callosal cholesterol-lowering drugs lower double transgenic tg2576 × ps1m146l producing n-truncated aβ introduce wild-type happ amyloid beta-peptide deposition amyloid precursor protein yeast artificial chromosome isoform-dependent amyloid deposition acetylcholinesterase-positive fiber deafferentation endoplasmic reticulum/intermediate compartment app[v717i] transgenic mice synaptophysin-immunoreactive presynaptic terminals wild-type human tau α-secretase cleaves app

Questions {❓}

Delatour B, Blanchard V, Pradier L, Duyckaerts C (2003) The innervation of senile plaques: a link between amyloid and neurofibrillary pathology?
Dodart JC, Mathis C, Bales KR, Paul SM (2002) Does my mouse have Alzheimer’s disease?
Gerlai R, Fitch T, Bales KR, Gitter BD (2002) Behavioral impairment of APP(V717F) mice in fear conditioning: is it only cognition?
In conclusion, the frequency of intracellular Aβ peptide accumulation and its temporal relationship with the extracellular deposits in transgenic mice raise new questions: does the intracellular accumulation also constitute a constant stage in the neuropathology of AD?
Is extracellular accumulation of Aβ peptide the cause of the deficit?
Rush DK, Aschmies S, Merriman MC (1992) Intracerebral beta-amyloid (25–35) produces tissue damage: is it neurotoxic?
What is the physiological relevance of a triple transgenic mouse to explain sporadic AD or even familial AD (FAD), which has never been found to be associated with a tau gene mutation?
Which animal models are to be reviewed here?

Schema {🗺️}

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         headline:Alzheimer disease models and human neuropathology: similarities and differences
         description:Animal models aim to replicate the symptoms, the lesions or the cause(s) of Alzheimer disease. Numerous mouse transgenic lines have now succeeded in partially reproducing its lesions: the extracellular deposits of Aβ peptide and the intracellular accumulation of tau protein. Mutated human APP transgenes result in the deposition of Aβ peptide, similar but not identical to the Aβ peptide of human senile plaque. Amyloid angiopathy is common. Besides the deposition of Aβ, axon dystrophy and alteration of dendrites have been observed. All of the mutations cause an increase in Aβ 42 levels, except for the Arctic mutation, which alters the Aβ sequence itself. Overexpressing wild-type APP alone (as in the murine models of human trisomy 21) causes no Aβ deposition in most mouse lines. Doubly (APP × mutated PS1) transgenic mice develop the lesions earlier. Transgenic mice in which BACE1 has been knocked out or overexpressed have been produced, as well as lines with altered expression of neprilysin, the main degrading enzyme of Aβ. The APP transgenic mice have raised new questions concerning the mechanisms of neuronal loss, the accumulation of Aβ in the cell body of the neurons, inflammation and gliosis, and the dendritic alterations. They have allowed some insight to be gained into the kinetics of the changes. The connection between the symptoms, the lesions and the increase in Aβ oligomers has been found to be difficult to unravel. Neurofibrillary tangles are only found in mouse lines that overexpress mutated tau or human tau on a murine tau −/− background. A triply transgenic model (mutated APP, PS1 and tau) recapitulates the alterations seen in AD but its physiological relevance may be discussed. A number of modulators of Aβ or of tau accumulation have been tested. A transgenic model may be analyzed at three levels at least (symptoms, lesions, cause of the disease), and a reading key is proposed to summarize this analysis.
         datePublished:2007-11-16T00:00:00Z
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      headline:Alzheimer disease models and human neuropathology: similarities and differences
      description:Animal models aim to replicate the symptoms, the lesions or the cause(s) of Alzheimer disease. Numerous mouse transgenic lines have now succeeded in partially reproducing its lesions: the extracellular deposits of Aβ peptide and the intracellular accumulation of tau protein. Mutated human APP transgenes result in the deposition of Aβ peptide, similar but not identical to the Aβ peptide of human senile plaque. Amyloid angiopathy is common. Besides the deposition of Aβ, axon dystrophy and alteration of dendrites have been observed. All of the mutations cause an increase in Aβ 42 levels, except for the Arctic mutation, which alters the Aβ sequence itself. Overexpressing wild-type APP alone (as in the murine models of human trisomy 21) causes no Aβ deposition in most mouse lines. Doubly (APP × mutated PS1) transgenic mice develop the lesions earlier. Transgenic mice in which BACE1 has been knocked out or overexpressed have been produced, as well as lines with altered expression of neprilysin, the main degrading enzyme of Aβ. The APP transgenic mice have raised new questions concerning the mechanisms of neuronal loss, the accumulation of Aβ in the cell body of the neurons, inflammation and gliosis, and the dendritic alterations. They have allowed some insight to be gained into the kinetics of the changes. The connection between the symptoms, the lesions and the increase in Aβ oligomers has been found to be difficult to unravel. Neurofibrillary tangles are only found in mouse lines that overexpress mutated tau or human tau on a murine tau −/− background. A triply transgenic model (mutated APP, PS1 and tau) recapitulates the alterations seen in AD but its physiological relevance may be discussed. A number of modulators of Aβ or of tau accumulation have been tested. A transgenic model may be analyzed at three levels at least (symptoms, lesions, cause of the disease), and a reading key is proposed to summarize this analysis.
      datePublished:2007-11-16T00:00:00Z
      dateModified:2007-11-16T00:00:00Z
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         Tg Mouse Lines
         Beta-site APP Cleaving Enzyme 1 (BACE)
         ATP-binding Cassette Transporter A1 (ABCA1)
         PDAPP Mice
         Tg Mice
         Pathology
         Neurosciences
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      name:CNRS, UMR7637 Ecole Supérieure de Physique Chimie de la Ville de Paris, Paris, France
      name:CNRS, UMR 8620 Université Paris Sud—Bât. 446, Orsay, France

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