COVALENT INTERACTIONS OF ACETALDEHYDE WITH THE ACTIN/MICROFILAMENT SYSTEM

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Abstract
The covalent binding of [ 14 C]acetaldehyde to purified rabbit skeletal muscle actin was characterized. As we have found for other cytoskeletal proteins, actin formed stable covalent adducts under reductive and non-reductive conditions. Under non-reductive conditions, individual and competition binding studies versus albumin both showed that the G-form of actin is more reactive toward acetaldehyde than the F-form. When proteins were compared on an ‘equi-lysine’ basis under non-reducing conditions, G-actin was found to preferentially complete with albumin for binding to acetaldehyde. Time-course dialysis studies indicated that acetaldehyde-actin adducts become more stable with prolonged incubation at 37°C. These data raise the possibility that actin could be a preferential target for adduct formationin cellular systems and will serve as the basis for ongoing studies aimed at defining the role of acetaldehyde-protein adducts in ethanol-induced cell injury.

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