scholarly journals In vivo oxidative stress in brain of Alzheimer disease transgenic mice: Requirement for methionine 35 in amyloid β-peptide of APP

2010 ◽  
Vol 48 (1) ◽  
pp. 136-144 ◽  
Author(s):  
D. Allan Butterfield ◽  
Veronica Galvan ◽  
Miranda Bader Lange ◽  
Huidong Tang ◽  
Renã A. Sowell ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Alzheimer Disease ◽  
Transgenic Mice ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Methionine 35

scholarly journals Covalent Protein Painting Reveals Structural Changes in the Proteome in Alzheimer Disease

2020 ◽  
Author(s):  
Casimir Bamberger ◽  
Sandra Pankow ◽  
Salvador Martínez-Bartolomé ◽  
Michelle Ma ◽  
Jolene Diedrich ◽  
...  
Keyword(s):  
Alzheimer Disease ◽  
Chemical Modification ◽  
Succinate Dehydrogenase ◽  
Structural Changes ◽  
Amyloid Β ◽  
Lewy Body Disease ◽  
Structural Proteomics ◽  
Amyloid Β Peptide ◽  
Lysine Residues

AbstractThe 3D structures of aberrant protein folds have been visualized in exquisite detail, yet no method has been able to quantitatively measure protein misfolding across a proteome. Here, we present Covalent Protein Painting (CPP), a mass spectrometry-based structural proteomics approach to quantify the accessibility of lysine ε-amines for chemical modification at the surface of natively folded proteins. We used CPP to survey 2,645 lysine residues in the proteome of HEK293T cells in vivo and found that mild heat shock increased rather than decreased lysine accessibility for chemical modification. CPP was able to differentiate patients with Alzheimer disease (AD) or Lewy body disease (LBD) or both from controls based on relative accessibility of lysine residues K147, K137, and K28 in Tubulin-β, Succinate dehydrogenase, and amyloid-β peptide, respectively. The alterations of Tubulin-β and Succinate dehydrogenase hint to broader perturbations of the proteome in AD beyond amyloid-β and hyper-phosphorylated tau.

Orally administered melatonin reduces oxidative stress and proinflammatory cytokines induced by amyloid-β peptide in rat brain: a comparative, in vivo study versus vitamin C and E

2003 ◽  
Vol 35 (2) ◽  
pp. 80-84 ◽  
Author(s):  
Sergio Rosales-Corral ◽  
Dun-Xian Tan ◽  
Russel J. Reiter ◽  
Miguel Valdivia-Velázquez ◽  
Gabriela Martínez-Barboza ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Vitamin C ◽  
Rat Brain ◽  
Proinflammatory Cytokines ◽  
Amyloid Β ◽  
In Vivo Study ◽  
Amyloid Β Peptide

In vivo protection by the xanthate tricyclodecan-9-yl-xanthogenate against amyloid β-peptide (1–42)-induced oxidative stress

Neuroscience ◽  
2006 ◽  
Vol 138 (4) ◽  
pp. 1161-1170 ◽  
Author(s):  
M. Perluigi ◽  
G. Joshi ◽  
R. Sultana ◽  
V. Calabrese ◽  
C. De Marco ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Amyloid Β ◽  
Amyloid Β Peptide

Insights into amyloid disease from fly models

2014 ◽  
Vol 56 ◽  
pp. 69-83 ◽  
Author(s):  
Ko-Fan Chen ◽  
Damian C. Crowther
Keyword(s):  
Drosophila Melanogaster ◽  
Neurodegenerative Disorders ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Disease Pathogenesis ◽  
Amyloid Aggregates ◽  
Aβ Amyloid ◽  
Polypeptide Chains ◽  
Amyloid Diseases

The formation of amyloid aggregates is a feature of most, if not all, polypeptide chains. In vivo modelling of this process has been undertaken in the fruitfly Drosophila melanogaster with remarkable success. Models of both neurological and systemic amyloid diseases have been generated and have informed our understanding of disease pathogenesis in two main ways. First, the toxic amyloid species have been at least partially characterized, for example in the case of the Aβ (amyloid β-peptide) associated with Alzheimer's disease. Secondly, the genetic underpinning of model disease-linked phenotypes has been characterized for a number of neurodegenerative disorders. The current challenge is to integrate our understanding of disease-linked processes in the fly with our growing knowledge of human disease, for the benefit of patients.

Phenolic Acids Exert Anticholinesterase and Cognition-Improving Effects

2018 ◽  
Vol 15 (6) ◽  
pp. 531-543 ◽  
Author(s):  
Dominik Szwajgier ◽  
Ewa Baranowska-Wojcik ◽  
Kamila Borowiec
Keyword(s):  
Phenolic Acids ◽  
Ex Vivo ◽  
Amyloid Β ◽  
Inhibitory Effect ◽  
In Vivo Studies ◽  
Amyloid Β Peptide ◽  
Beneficial Effects ◽  
Aβ Fibrils

Numerous authors have provided evidence regarding the beneficial effects of phenolic acids and their derivatives against Alzheimer's disease (AD). In this review, the role of phenolic acids as inhibitors of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) is discussed, including the structure-activity relationship. In addition, the inhibitory effect of phenolic acids on the formation of amyloid β-peptide (Aβ) fibrils is presented. We also cover the in vitro, ex vivo, and in vivo studies concerning the prevention and treatment of the cognitive enhancement.

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