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Updated: Jul 29, 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
Hsp27: novel regulator of intracellular redox state
1Centre de Génétique Moléculaire et Cellulaire, CNRS UMR5534, Université Claude Bernard Lyon-I, Villeurbanne, France. arrigo@univ-lyon1.fr
Abstract:
Small stress proteins are molecular chaperones that modulate the ability of cells to respond to several types of injuries. In this regard, a protection generated by the expression of mammalian small stress proteins against the cell death induced by oxidative stress has been described. This review summarizes the current knowledge of the protective mechanism generated by the expression of the major mammalian small stress protein Hsp27 in cells exposed to oxidative stress. A possible role of this chaperone protein in the presentation of oxidized proteins to the proteasome degradation machinery is proposed.
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