Rapid Cross-Linking of Proteins by 4-Ketoaldehydes and 4-Hydroxy-2-alkenals Does Not Arise from the Lysine-Derived Monoalkylpyrroles
Citations Over Time
Abstract
Exposure of proteins to 4-hydroxy-2-nonenal (HNE) results in conversion of lysines in part to 2-pentylpyrroles that can be formed in higher yield by exposure to the isomeric 4-oxononanal. Since both HNE and 4-oxononanal cause protein cross-linking, and since pyrrolation of proteins by gamma-diketones is also known to result in protein cross-linking, it has been considered that the initially formed 2-pentylpyrroles are responsible for the protein cross-linking seen for HNE and 4-oxononanal. Here we show that protein-bound 2-alkylpyrrole products associated with modification by 4-hydroxy-2-alkenals and 4-oxoalkanals, possessing only monoalkyl substitution, induce undetectable levels of autoxidation-mediated protein cross-linking over time periods where the parent aldehydes effect extensive protein cross-linking, which then must be occurring through alternative mechanisms. Finally, using both RNase and BSA, our finding that reductive methylation of lysines blocks protein cross-linking induced by either HNE or 4-oxononanal (and development of fluorescence in the case of HNE) implicates the obligatory role of lysines in the cross-linking reactions.
Related Papers
- → Autoxidation of ketones and esters in basic solution(1971)30 cited
- → The autoxidation of aliphatic esters. Part 2. The autoxidation of neopentyl esters(2000)15 cited
- → Analysis of High Molecular Weight Autoxidation Products Using High Performance Size Exclusion Chromatography: I. Changes During Autoxidation(1993)13 cited
- → Autoxidation of Unsaturated Fatty Acid Methyl Esters. I.(1978)5 cited
- → Tocopherols as Antioxidants in Autoxidation of Methyl. Linoleate. II.(1977)