Glycolaldehyde is an endogenous source of lysine N-pyrrolation
Miho Chikazawa, Jun Yoshitake, Sei-Young Lim, Shiori Iwata, Lumi Negishi, Takahiro Shibata, Kôji Uchida
Abstract
-pyrrolation in proteins and found that GA-modified proteins are recognized by apolipoprotein E, a binding target of pyrrolated proteins. Moreover, GA-modified proteins triggered an immune response to pyrrolated proteins, and monoclonal antibodies generated from mice immunized with GA-modified proteins specifically recognized pyrrolated proteins. These findings reveal that GA is an endogenous source of DNA-mimicking pyrrolated proteins and may provide mechanistic insights relevant for innate and autoimmune responses associated with glucose metabolism and oxidative stress.
Topics & Concepts
LysineGlycolaldehydeChemistryBiochemistryGlyoxalGlycationGlycosylationMaillard reactionAmino acidReceptorOrganic chemistryCatalysisRedox biology and oxidative stressAdvanced Glycation End Products researchAdenosine and Purinergic Signaling