Document Type
Article
Publication Title
Journal of Enzyme Inhibition and Medicinal Chemistry
Abstract
Acrolein is a reactive lipid peroxidation byproduct, which is found in ischemic tissue. We examined the effects of acrolein on cytosolic aspartate aminotransferase (cAAT), which is an enzyme that was previously shown to be inhibited by glycating agents. cAAT is thought to protect against ischemic injury. We observed that acrolein cross-linked cAAT subunits as evidenced by the presence of high molecular weight bands following SDS-PAGE. Acrolein-modified cAAT resisted thermal denaturation when compared with native cAAT. We also observed a decrease in intrinsic fluorescence (290 nm, ex; 380 nm, em). These observations are consistent with an acrolein-induced change in conformation that is more rigid and compact than native cAAT, suggesting that intramolecular cross-links occurred. Acrolein also inhibited activity, and the inhibition of enzyme activity correlated with the acrolein-induced formation of cAAT cross-links.
DOI
10.1080/14756360290011753
Publication Date
2-2002
ISSN
1475-6374
Recommended Citation
Southwell J, Yeargans G, Kowalewski C, Seidler NW. Acrolein Modifies and Inhibits Cytosolic Aspartate Aminotransferase. Journal of Enzyme Inhibition and Medicinal Chemistry. 2002; 17(1). doi: 10.1080/14756360290011753.
