The Role of the Glyceraldehyde-3-phosphate Dehydrogenase and β-Amyloid Complex in the Activation of the Cellular Chaperone System

Objective: The aim of this study was to evaluate the cytotoxic effect of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and β-amyloid (Aβ1-42) co-aggregates on human mesenchymal cells reprogrammed into a neuronal phenotype. Methods: Co-aggregates were formed by incubating recombinant GAPDH and synthetic Aβ1-42 in the presence of tissue transglutaminase, which provides covalent cross-linking of proteins. Results: The data obtained demonstrate that GAPDH–Aβ1-42 co-aggregates have pronounced neurotoxicity, but are able to activate protective and compensatory mechanisms, including the chaperone apparatus. Conclusions: The results emphasize the need to develop therapeutic strategies aimed at blocking the GAPDH–Aβ1-42 interaction and supporting cellular protective pathways to prevent neurodegeneration

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Publication Details

Journal
Cell and Tissue Biology
Published
2025-09-30
DOI
https://doi.org/10.1134/s1990519x25060057
Primary Topic
Heat shock proteins research
Type
article
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article

The Role of the Glyceraldehyde-3-phosphate Dehydrogenase and β-Amyloid Complex in the Activation of the Cellular Chaperone System

Irina V. Guzhova, Vladimir F. Lazarev, Elizaveta A. Dutysheva, Boris A. Margulis et al.
Cell and Tissue Biology
Heat shock proteins research
article

The Role of the Glyceraldehyde-3-phosphate Dehydrogenase and β-Amyloid Complex in the Activation of the Cellular Chaperone System

Irina V. Guzhova, Vladimir F. Lazarev, Elizaveta A. Dutysheva, Boris A. Margulis, A. A. Sakharov, A. V. Yurakova
article en

Abstract

Objective: The aim of this study was to evaluate the cytotoxic effect of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and β-amyloid (Aβ1-42) co-aggregates on human mesenchymal cells reprogrammed into a neuronal phenotype. Methods: Co-aggregates were formed by incubating recombinant GAPDH and synthetic Aβ1-42 in the presence of tissue transglutaminase, which provides covalent cross-linking of proteins. Results: The data obtained demonstrate that GAPDH–Aβ1-42 co-aggregates have pronounced neurotoxicity, but are able to activate protective and compensatory mechanisms, including the chaperone apparatus. Conclusions: The results emphasize the need to develop therapeutic strategies aimed at blocking the GAPDH–Aβ1-42 interaction and supporting cellular protective pathways to prevent neurodegeneration

Cell and Tissue BiologyVol. 19(6)
Institute of Cytology (RU)
Openalex Percentile: Top 76%
Heat shock proteins research
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