ribosylation rapidly induces α-synuclein to form highly cytotoxic molten globules of advanced glycation end products核糖基化迅速引发α-synuclein形成高细胞毒性晚期糖化终产物中的熔岩.pdfVIP

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ribosylation rapidly induces α-synuclein to form highly cytotoxic molten globules of advanced glycation end products核糖基化迅速引发α-synuclein形成高细胞毒性晚期糖化终产物中的熔岩.pdf

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ribosylation rapidly induces α-synuclein to form highly cytotoxic molten globules of advanced glycation end products核糖基化迅速引发α-synuclein形成高细胞毒性晚期糖化终产物中的熔岩

Ribosylation Rapidly Induces a-Synuclein to Form Highly Cytotoxic Molten Globules of Advanced Glycation End Products 1. 1,3. 1 1,2,3 Lan Chen , Yan Wei , Xueqing Wang , Rongqiao He * 1 State Key Laboratory of Brain and Cognitive Sciences, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China, 2 Laboratory of Mental Health, Institute of Psychology, Chinese Academy of Sciences, Beijing, China, 3 Graduate University of Chinese Academy of Sciences, Beijing, China Abstract Background: Alpha synuclein (a-Syn) is the main component of Lewy bodies which are associated with several neurodegenerative diseases such as Parkinson’s disease. While the glycation with D-glucose that results in a-Syn misfold and aggregation has been studied, the effects of glycation with D-ribose on a-Syn have not been investigated. Methodology/Principal Findings: Here, we show that ribosylation induces a-Syn misfolding and generates advanced glycation end products (AGEs) which form protein molten globules with high cytotoxcity. Results from native- and SDS- PAGE showed that D-ribose reacted rapidly with a-Syn, leading to dimerization and polymerization. Trypsin digestion and sequencing analysis revealed that during ribosylation the lysinyl residues (K58, K60, K80, K96, K97 and K102) in the C-terminal region reacted more quickly with D-ribose than those of the N-terminal region. Using Western blotting, AGEs resulting from the glycation of a-Syn were observed within 24 h in the presence of D-ribose, but were not observed in the presence of D- glucose. Changes in fluorescence at 410 nm demonstrated again that AGEs were formed during early ribosylation. Changes in the secondary structure of ribosylated a-Syn were not cl