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1

Circular dichroism and aggregation studies of amyloid beta [11-28] fragment and its variants

100%
Juszczyk P., Kolodziejczyk A. S., Grzonka Z.
Acta Biochimica Polonica
|
2005
|
tom 52
|
nr 2
Aggregation of Aβ peptides is a seminal event in Alzheimer’s disease. Detailed understanding of Aβ assembly would facilitate the targeting and design of fibrillogenesis inhibitors. Here comparative conformational and aggregation studies using CD spectroscopy and thioflavine T fluorescence assay are presented. As a model peptide, the 11–28 fragment of Aβ was used. This model peptide is known to contain the core region responsible for Aβ aggregation. The structural and aggregational behaviour of the peptide was compared with the properties of its variants corresponding to natural, clinically relevant mutants at positions 21-23 (A21G, E22K, E22G, E22Q and D23N). In HFIP (hexafluoro-2-propanol), a strong α-helix inducer, the CD spectra revealed an unexpectedly high amount of β-sheet conformation. The aggregation process of Aβ(11–28) variants provoked by water addition to HFIP was found to be consistent with a model of an α-helix-containing intermediate. The aggregation propensity of all Aβ(11–28) variants was also compared and discussed.
2

Amyloid-beta and tau proteins as biochemical markers of Alzheimer's disease

100%
Sobow T., Flirski M., Liberski P. P.
Acta Neurobiologiae Experimentalis
|
2004
|
tom 64
|
nr 1
3

Effects of rosmarinic acid on cognitive and biochemical alterations in ovariectomized rats treated with D-galactose

84%
Gok D. K., Ozturk N., Er H., Aslan M., Demir N., Derin N., Agar A., Yargicoglu P.
Folia Histochemica et Cytobiologica
|
2015
|
tom 53
|
nr 4
4

Alzheimer's disease and acetylcholine receptors

84%
Kihara T., Shimohama S.
Acta Neurobiologiae Experimentalis
|
2004
|
tom 64
|
nr 1
5

Mechanisms of immune regulation in Alzheimer's disease: a viewpoint

84%
Marx F., Blasko I., Grubeck-Loebenstein B.
Archivum Immunologiae et Therapiae Experimentalis
|
1999
|
tom 47
|
nr 4
6

Amyloid beta enhances cytosolic phospholipase A2 level and arachidonic acid release via nitric oxide in APP-transfected PC12 cells

84%
Chalimoniuk M., Stolecka A., Cakala M., Hauptmann S., Schulz K., Lipka U., Leuner K., Eckert A., Muller W. E., Strosznajder J. B.
Acta Biochimica Polonica
|
2007
|
tom 54
|
nr 3
Cytosolic phospholipase A2 (cPLA2) preferentially liberates arachidonic acid (AA), which is known to be elevated in Alzheimer's disease (AD). The aim of this study was to investigate the possible relationship between enhanced nitric oxide (NO) generation observed in AD and cPLA2 protein level, phosphorylation, and AA release in rat pheochromocytoma cell lines (PC12) differing in amyloid beta secretion. PC12 control cells, PC12 cells bearing the Swedish double mutation in amyloid beta precursor protein (APPsw), and PC12 cells transfected with human APP (APPwt) were used. The transfected APPwt and APPsw PC12 cells showed an about 2.8- and 4.8-fold increase of amyloid β (Aβ) secretion comparing to control PC12 cells. An increase of NO synthase activity, cGMP and free radical levels in APPsw and APPwt PC12 cells was observed. cPLA2 protein level was higher in APPsw and APPwt PC12 cells comparing to PC12 cells. Moreover, phosphorylated cPLA2 protein level and [3H]AA release were also higher in APP-transfected PC12 cells than in the control PC12 cells. An NO donor, sodium nitroprusside, stimulated [3H]AA release from prelabeled cells. The highest NO-induced AA release was observed in control PC12 cells, the effect in the other cell lines being statistically insignificant. Inhibition of cPLA2 by AACOCF3 significantly decreased the AA release. Inhibitors of nNOS and γ-secretase reduced AA release in APPsw and APPwt PC12 cells. The basal cytosolic [Ca2+]i and mitochondrial Ca2+ concentration was not changed in all investigated cell lines. Stimulation with thapsigargin increased the cytosolic and mitochondrial Ca2+ level, activated NOS and stimulated AA release in APP-transfected PC12 cells. These results indicate that Aβ peptides enhance the protein level and phosphorylation of cPLA2 and AA release by the NO signaling pathway.
7

Alzheimer's amyloid-beta [Abeta] is an essential synaptic protein, not neurotoxic junk

84%
Koudinov A. R., Berezov T. T.
Acta Neurobiologiae Experimentalis
|
2004
|
tom 64
|
nr 1
8

Molecular mechanisms initiating amyloid beta-fibril formation in Alzheimer's disease

67%
Kirkitadze M. D., Kowalska A.
Acta Biochimica Polonica
|
2005
|
tom 52
|
nr 2
The deposition of aggregated amyloid β-protein (Aβ) in the human brain is a major lesion in Alzheimer’s disease (AD). The process of Aβ fibril formation is associated with a cascade of neuropathogenic events that induces brain neurodegeneration leading to the cognitive and behavioral decline characteristic of AD. Although a detailed knowledge of Aβ assembly is crucial for the development of new therapeutic approaches, our understanding of the molecular mechanisms underlying the initiation of Aβ fibril formation remains very incomplete. The genetic defects responsible for familial AD influence fibrillogenesis. In a majority of familial cases determined by amyloid precursor protein (APP) and presenilin (PS) mutations, a significant overproduction of Aβ and an increase in the Aβ42/Aβ40 ratio are observed. Recently, it was shown that the two main alloforms of Aβ have distinct biological activity and behaviour at the earliest stage of assembly. In vitro studies demonstrated that Aβ42 monomers, but not Aβ40, form initial and minimal structures (pentamer/hexamer units called paranuclei) that can oligomerize to larger forms. It is now apparent that Aβ oligomers and protofibrils are more neurotoxic than mature Aβ fibrils or amyloid plaques. The neurotoxicity of the prefibrillar aggregates appears to result from their ability to impair fundamental cellular processes by interacting with the cellular membrane, causing oxidative stress and increasing free Ca2+ that eventually lead to apoptotic cell death.
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