Protection Against Protein Aggregation by Alpha-Crystallin as a Mechanism of Preconditioning
Document Type
Article
Publication Title
Neurochemical Research
Abstract
Anesthetic preconditioning occurs when cells previously exposed to inhaled anesthetics are protected against subsequent injury. We hypothesize that inhaled anesthetics may cause slight protein misfolding that involves site-specific dehydration, stimulating cytoprotective mechanisms. Human neuroblastoma cells were exposed to ethanol (as the dehydration agent) followed by quantitative analysis of the expression of five heat shock genes: DNAJC5G, CRYAA, HSPB2, HSF4 and HSF2. There was an ethanol-induced upregulation of all genes except HSF4, similar to previous observations using isoflurane. CRYAA (the gene for alphaA-crystallin) exhibited a 23.19 and 17.15-fold increase at 24 and 48 h post ethanol exposure, respectively. Additionally, we exposed glyceraldehyde 3-phosphate dehydrogenase to ethanol, which altered oligomeric subspecies and caused protein aggregation in a concentration-dependent manner. Ethanol-mediated dehydration-induced protein aggregation was prevented by incubation with alpha-crystallin. These data indicate that ethanol mimics the effects of isoflurane presumably through a cellular preconditioning mechanism that involves dehydration-induced protein aggregation.
DOI
10.1007/s11064-011-0601-4
Publication Date
2-2012
Keywords
Alpha-crystallin, Ethanol, Heat shock proteins, Preconditioning, Protein aggregation
ISSN
1573-6903
Recommended Citation
Ferns JE, Theisen CS, Fibuch EE, Seidler NW. Protection Against Protein Aggregation by Alpha-Crystallin as a Mechanism of Preconditioning. Neurochemical Research. 2012; 37(2). doi: 10.1007/s11064-011-0601-4.
