Protection against protein aggregation by alpha-crystallin as a mechanism of preconditioning.
Neurochem Res
; 37(2): 244-52, 2012 Feb.
Article
in En
| MEDLINE
| ID: mdl-21984199
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Anesthetics, Inhalation
/
Alpha-Crystallins
/
Heat-Shock Proteins
Limits:
Humans
Language:
En
Journal:
Neurochem Res
Year:
2012
Document type:
Article
Affiliation country:
United States