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 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 compete with albumin for binding to acetaldehyde. Time-course dialysis studies indicated that acetaldehyde-actin adducts become more stable with prolonged incubation at 37 degrees C. These data raise the possibility that actin could be a preferential target for adduct formation in 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.
Xu
D S
DS
Liver Study Unit, Veterans Administration Medical Center, Omaha, NE.
Jennett
R B
RB
Smith
S L
SL
Sorrell
M F
MF
Tuma
D J
DJ
D000079:Acetaldehyde / Q000378:metabolism*; D000818:Animals; D002470:Cell Survival; D003599:Cytoskeleton / Q000378:metabolism; D008099:Liver / Q000166:cytology / Q000378:metabolism; D008840:Microfilament Proteins / Q000378:metabolism*; D009132:Muscles / Q000166:cytology / Q000378:metabolism; D011817:Rabbits
D008840:Microfilament Proteins; D000079:Acetaldehyde