A possible role of glycation in the regulation of amyloid β precursor protein processing leading to amyloid β accumulation
| Autor: | Shabda E Kulsange, Mahesh J. Kulkarni, Rakesh Joshi, Rubina S. Kazi, Gouri V. Patil |
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| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Proteases medicine.medical_treatment 03 medical and health sciences Amyloid beta-Protein Precursor 0302 clinical medicine Glycation Alzheimer Disease Diabetes mellitus medicine Humans Protein precursor Aged chemistry.chemical_classification Protease Amyloid beta-Peptides biology General Medicine medicine.disease Cell biology 030104 developmental biology Enzyme chemistry Alpha secretase biology.protein Amyloid Precursor Protein Secretases Amyloid precursor protein secretase Protein Processing Post-Translational 030217 neurology & neurosurgery |
| Zdroj: | Medical hypotheses. 142 |
| ISSN: | 1532-2777 |
| Popis: | Alzheimer's disease (AD) is one of the most common forms of neurodegenerative diseases amongst the aged population. The disease is multifactorial, and diabetes has been considered as one of the major risk factors for the development of AD. Chronic hyperglycemic condition in diabetes promotes non-enzymatic protein modification by glucose termed as glycation, which affects protein structure and function. Previous studies have shown that many of the enzymes, including proteases, are affected by glycation. Conversely, glycated proteins are known to become resistant to protease action. In these hypotheses, we have extended these two concepts to the regulation of amyloid-β protein precursor (AβPP) by secretases leading to amyloid-β (Aβ) accumulation. The first hypothesis deals with the glycation of α-secretases leading to its reduced activity, while in the second hypothesis, AβPP glycation may prevent α-secretases action, rendering its processing by β secretase. As diabetes is a risk factor for the development of AD, either or both these pathways may operate, leading to the manifestation of AD. |
| Databáze: | OpenAIRE |
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