title: Alcohol stress, membranes, and chaperones.
abstract: Ethanol, which affects all body organs, exerts a number of cytotoxic effects, most of them independent of cell type. Ethanol treatment leads to increased membrane fluidity and to changes in membrane protein composition. It can also interact directly with membrane proteins, causing conformational changes and thereby influencing their function. The cytotoxic action may include an increased level of oxidative stress. Heat shock protein molecular chaperones are ubiquitously expressed evolutionarily conserved proteins which serve as critical regulators of cellular homeostasis. Heat shock proteins can be induced by various forms of stresses such as elevated temperature, alcohol treatment, or ischemia, and they are also upregulated in certain pathological conditions. As heat shock and ethanol stress provoke similar responses, it is likely that heat shock protein activation also has a role in the protection of membranes and other cellular components during alcohol stress.
authors.forename: Melinda E
authors.initials: ME
authors.lastname: Tóth
authors.forename: László
authors.initials: L
authors.lastname: Vígh
authors.forename: Miklós
authors.initials: M
authors.lastname: Sántha
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D019610:Cytoprotection; D000431:Ethanol / Q000009:adverse effects*; D006360:Heat-Shock Proteins / Q000378:metabolism; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism*; D013312:Stress, Physiological / Q000187:drug effects*
chemical_list: D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D000431:Ethanol