Glycation of α-synuclein hampers its binding to synaptic-like vesicles and its driving effect on their fusion.

ABSTRACT: Parkinson's disease (PD) is one of the most prevalent neurodegenerative disorders affecting the worldwide population. One of its hallmarks is the intraneuronal accumulation of insoluble Lewy bodies (LBs), which cause the death of dopaminergic neurons. α-Synuclein (αS) is the main component of these LBs and in them, it commonly contains non-enzymatic post-translational modifications, such as those resulting from its reaction with reactive carbonyl species arising as side products of the intraneuronal glycolysis (mainly methylglyoxal). Consequently, lysines of the αS found in LBs of diabetic individuals are usually carboxyethylated. A precise comprehension of the effect of N^ε-(carboxyethyl)lysine (CEL) on the aggregation of αS and on its physiological function becomes crucial to f

SUBMITTER: Uceda AB 

PROVIDER: S-EPMC9167179 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature