Abstract
The majority of cell-stressing exposures affect proteins. Typical “proteotoxic” exposures such as heating, ultra-violet irradiation, de crease in pH and treatment with oxidants or heavy metals are able to damage various proteins both in vitro (in a solution) and in vivo (in a cell). Lack of ATP in artificially prepared protein solutions does not seem to be very critical for the stability of the soluted proteins; in contrast, the depletion of intracellular ATP destroys the cytoskeletal framework and evokes aggregation (or insolubility) of many cellular proteins including HSPs. Although this proteotoxic component is only one of the many harmful effects of ATP depletion on mammalian cells, we consider it the most crucial event coupling the mechanisms of cell injury and cell adaptation under metabolic (or ischemic) stress. That is why this phenomenon is considered substantially here.
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Kabakov, A.E., Gabai, V.L. (1997). “Proteotoxicity” of ATP Depletion: Disruption of the Cytoskeleton, Protein Aggregation and Involvement of Molecular Chaperones. In: Heat Shock Proteins and Cytoprotection. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-6007-4_3
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