Controlled in situ preparation of Aβ(1–42) oligomers from the isopeptide “iso-Aβ(1–42)”, physicochemical and biological characterization

Bozsó, Zsolt; Penke, Botond; Simon, Dóra; Laczkó, Ilona; Juhász, Gábor; Szegedi, Viktor; Kasza, Ágnes; Soós, Katalin; Hetényi, Anasztázia; Wéber, Edit; Tóháti, Hajnalka M.; Csete, Mária; Zarándi, Márta; Fülöp, Lívia

doi:10.1016/j.peptides.2009.12.001

Cited by 47 publications

(55 citation statements)

References 36 publications

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“…LTP, a cellular correlate of learning and memory (Bliss and Colingridge 1993), was also investigated on hippocampal slices. Previously, it was demonstrated that soluble oligomers of Aβ are able to inhibit LTP and cause learning and memory deficit (Haas and Selkoe 2007;Bozso et al 2010). Our results have shown that LTP was impaired in APPswe/PS1dE9 mice indeed, but it was normalized upon Hsp27 overexpression.…”

Section: Discussionsupporting

confidence: 60%

Overexpression of Hsp27 ameliorates symptoms of Alzheimer's disease in APP/PS1 mice

Tóth

Szegedi

Varga

et al. 2013

Cell Stress and Chaperones

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Hsp27 belongs to the small heat shock protein family, which are ATP-independent chaperones. The most important function of Hsp27 is based on its ability to bind non-native proteins and inhibit the aggregation of incorrectly folded proteins maintaining them in a refolding-competent state. Additionally, it has anti-apoptotic and antioxidant activities. To study the effect of Hsp27 on memory and synaptic functions, amyloid-β (Aβ) accumulation, and neurodegeneration, we generated transgenic mice overexpressing human Hsp27 protein and crossed with APPswe/PS1dE9 mouse strain, a mouse model of Alzheimer's disease (AD). Using different behavioral tests, we found that spatial learning was impaired in AD model mice and was rescued by Hsp27 overexpression. Electrophysiological recordings have revealed that excitability of neurons was significantly increased, and long-term potentiation (LTP) was impaired in AD model mice, whereas they were normalized in Hsp27 overexpressing AD model mice. Using anti-amyloid antibody, we counted significantly less amyloid plaques in the brain of APPswe/PS1dE9/Hsp27 animals compared to AD model mice. These results suggest that overexpression of Hsp27 protein might ameliorate certain symptoms of AD.

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Section: Discussionsupporting

confidence: 60%

Overexpression of Hsp27 ameliorates symptoms of Alzheimer's disease in APP/PS1 mice

Tóth

Szegedi

Varga

et al. 2013

Cell Stress and Chaperones

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“…〈␤ 42 Preparation-A␤ 42 was prepared as described earlier (26). Then 0.2 mg of dry peptide was dissolved in 40 l of Milli-Q ultrapure water and sonicated for 5 min, and 360 l of PBS was added to the peptide, which was further sonicated for 5 min.…”

Section: Methodsmentioning

confidence: 99%

Interactions of Pathological Hallmark Proteins

Oláh

Vincze

Virók

et al. 2011

Journal of Biological Chemistry

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125

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Background:The disordered TPPP/p25 is a hallmark of synucleinopathies. Results: Tight binding of TPPP/p25 with ␤-amyloid results in the formation of massive aggregates both in vitro and in vivo. Conclusion:The presence of intracellular pathological-like TPPP/p25-␤-amyloid aggregates elucidates the partial co-localization of ␤-amyloid and TPPP/p25 in Lewy body dementia with Alzheimer disease. Significance: This new type of aggregation may form bridge to conjoin synucleopathies with other neuropathologies.

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“…Oligomerization of the peptide was checked by TEM. Sampling for TEM and image preparation was done by following a standard protocol [28,29]. According to the TEM investigations, samples contained globulomers with a diameter of 5-7 nm either alone or in chain-like or annular assemblies, but not classical protofibrillar aggregates, which are 50-200 nm long (Fig.…”

Section: Peptidesmentioning

confidence: 99%

Protection of the Blood-Brain Barrier by Pentosan Against Amyloid-β-Induced Toxicity

Deli

Veszelka

Csiszár

et al. 2010

JAD

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Abstract. Endothelial cells of brain capillaries forming the blood-brain barrier play an important role in the pathogenesis and therapy of Alzheimer's disease. Amyloid-β (Aβ) peptides are key pathological elements in the development of the disease. A blood-brain barrier model, based on primary rat brain endothelial cells was used in which the barrier properties were induced by glial cells. The effects of amyloid peptides have been tested on cell viability and barrier functions. Aβ showed toxic effects on primary rat brain endothelial cells measured by MTT dye conversion and the lactate dehydrogenase release. Morphologically cytoplasmic vacuolization, disruption of the structure of cytoplasmic organelles and tight junctions could be observed in brain endothelial cells. Treatment with Aβ1−42 decreased the electrical resistance, and increased the permeability of brain endothelial cell monolayers for both fluorescein and albumin. Serum amyloid P component which stabilizes Aβ fibrils in cortical amyloid plaques and cerebrovascular amyloid deposits significantly potentiated the barrier-weakening effect of Aβ1−42. Sulfated polysaccharide pentosan could decrease the toxic effects of Aβ peptides in brain endothelial cells. It could also significantly protect the barrier integrity of monolayers from damaging actions of peptides. Pentosan modified the size, and significantly decreased the number of amyloid aggregates demonstrated by atomic force microscopy. The present data further support the toxic effects of amyloid peptides on brain endothelial cells, and can contribute to the development of molecules protecting the blood-brain barrier in Alzheimer's disease.

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Controlled in situ preparation of Aβ(1–42) oligomers from the isopeptide “iso-Aβ(1–42)”, physicochemical and biological characterization

Cited by 47 publications

References 36 publications

Overexpression of Hsp27 ameliorates symptoms of Alzheimer's disease in APP/PS1 mice

Overexpression of Hsp27 ameliorates symptoms of Alzheimer's disease in APP/PS1 mice

Interactions of Pathological Hallmark Proteins

Protection of the Blood-Brain Barrier by Pentosan Against Amyloid-β-Induced Toxicity

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