Apolipoprotein E binds to and reduces serum levels of DNA-mimicking, pyrrolated proteins.

ABSTRACT: Lysine N-pyrrolation, converting lysine residues to N ^ϵ-pyrrole-l-lysine, is a recently discovered post-translational modification. This naturally occurring reaction confers electrochemical properties onto proteins that potentially produce an electrical mimic to DNA and result in specificity toward DNA-binding molecules such as anti-DNA autoantibodies. The discovery of this unique covalent protein modification provides a rationale for establishing the molecular mechanism and broad functional significance of the formation and regulation of N ^ϵ-pyrrole-l-lysine-containing proteins. In this study, we used microbeads coupled to pyrrolated or nonpyrrolated protein to screen for binding activities of human serum-resident nonimmunoglobin proteins to the

SUBMITTER: Hirose S 

PROVIDER: S-EPMC6635438 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature