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Updated: Jun 27, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
Published on: June 7, 2018
Oxidative stress and molecular chaperones: a dynamic crosstalk in neurodegenerative disorders
Leila Noori1, Yousef Mohamadi2, Francesco Cappello1
1Department of Biomedicine, Neuroscience and Advanced Diagnostics (BiND), University of Palermo, Palermo, Italy.
Abstract:
Neurodegenerative diseases (NDs), such as Alzheimer's disease, Parkinson's disease, and Huntington's disease are discussed as representative examples of conditions in which oxidative stress and proteostasis imbalance contribute to progressive neuronal dysfunction. Oxidative stress, defined as an imbalance between reactive oxygen species (ROS) production and antioxidant defenses, is widely recognized as a key contributor to ND pathogenesis. Excessive ROS disrupt cellular homeostasis and promotes protein misfolding and aggregation, thereby compromising the proteostasis network. In response to this stress, molecular chaperones, including members of heat shock protein (Hsp) family, play a crucial protective role by maintaining protein folding integrity and preventing toxic aggregation. Furthermore, mesenchymal stem cell-derived extracellular vesicles (MSC-EVs) serve as carriers of bioactive molecules, including antioxidants and molecular chaperones, offering a unique mechanism to restore cellular homeostasis. This review explores the interplay between oxidative stress and molecular chaperones in the pathogenesis of NDs and highlights the emerging therapeutic potential of MSC-EVs as modulators of oxidative and proteostatic imbalance.
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