COVALENT INTERACTIONS OF ACETALDEHYDE WITH THE ACTIN/MICROFILAMENT SYSTEM

The covalent binding of [14C]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 bindin...

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Bibliographic Details
Published in:Alcohol and alcoholism (Oxford) 1989, Vol.24 (4), p.281-289
Main Authors: XU, D. S., JENNETT, R. B., SMITH, S. L., SORRELL, M. F., TUMA, D. J.
Format: Article
Language:English
Subjects:
Acetaldehyde - metabolism
Animals
Cell Survival
Cytoskeleton - metabolism
Liver - cytology
Liver - metabolism
Microfilament Proteins - metabolism
Muscles - cytology
Muscles - metabolism
Rabbits
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Summary:The covalent binding of [14C]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.
ISSN:0735-0414
1464-3502
DOI:10.1093/oxfordjournals.alcalc.a044914