Comparison of the reaction of methylglyoxal (MGO) with murine and human amyloid beta (Aβ): Insights into a mechanism of Alzheimer’s disease (AD)
| Autor: | Jake S. Hedges, Nathaniel J. Henning, Sebastian M. Fica-Contreras, Sydney O. Shuster, Sunhee Choi |
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| Rok vydání: | 2022 |
| Předmět: |
0301 basic medicine
Amyloid beta Biophysics Arginine medicine.disease_cause Biochemistry Mice 03 medical and health sciences chemistry.chemical_compound Residue (chemistry) 0302 clinical medicine Alzheimer Disease Superoxides Glycation medicine Animals Humans Molecular Biology Amyloid beta-Peptides biology Superoxide Mechanism (biology) Lysine Methylglyoxal Cell Biology Pyruvaldehyde Peptide Fragments 030104 developmental biology chemistry 030220 oncology & carcinogenesis Biochemistry and cell biology biology.protein Oxidative stress |
| DOI: | 10.57968/middlebury.21663260 |
| Popis: | Reacted with methylglyoxal (MGO), murine Aβ(1-40) (mAβ) produced significantly less superoxide anion (O2•–) compared to human Aβ(1-40) (hAβ). The reactions of MGO with mAβ(R13H), hAβ(H13F), Nα-acetyl-l-lysine, and Nα-acetyl-l-arginine implied that the lack of His13 in mAβ prohibits its Lys16 residue from reacting to produce cross-linked reaction products and O2•–. Our results suggest that murine brains are under less oxidative stress than human brains, which may be one of the reasons why rodents do not develop AD-like symptoms, and which provides further insight into a chemical mechanism for the development of AD in humans. |
| Databáze: | OpenAIRE |
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