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000281812 1001_ $$aVasili, Eftychia$$b0
000281812 245__ $$aGlycation of alpha-synuclein enhances aggregation and neuroinflammatory responses.
000281812 260__ $$a[London]$$bSpringer Nature$$c2025
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000281812 520__ $$aThe risk of developing Parkinson's disease (PD) is elevated in individuals with type 2 diabetes (T2DM), but the molecular pathways underlying this link remain unclear. Glycation, a non-enzymatic modification of lysine and arginine residues by reducing sugars or reactive dicarbonyls, may disrupt proteostasis and trigger pathology. Here, we investigated how methylglyoxal (MGO)- and ribose-mediated glycation influence aSyn aggregation, neuroinflammation, and detoxification pathways. Using SH-SY5Y cells, primary neurons, primary microglia and MGO-injected aSyn transgenic mice, we found that MGO-glycated aSyn promotes PD associated pathological features, including pS129-positive aSyn aggregates, neuroinflammation, and impairment of the glyoxalase detoxification pathway. Ribose-glycated aSyn, while immunogenic, exerts limited effects on aggregation and seeding. Both glycated species activates microglia and upregulate pro-inflammatory markers. We further developed a novel antibody specific for MGO-glycated aSyn, which selectively detects Lewy body-like deposits in dementia with Lewy bodies (DLB) tissue and MGO-injected mice. These findings implicate MGO-glycation in PD-T2DM comorbidity.
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000281812 7001_ $$aKönig, Annekatrin$$b1
000281812 7001_ $$aAl-Azzani, Mohammed$$b2
000281812 7001_ $$aBosbach, Clara$$b3
000281812 7001_ $$aGatzemeier, Luisa Maria$$b4
000281812 7001_ $$aThom, Searlait$$b5
000281812 7001_ $$aChegão, Ana$$b6
000281812 7001_ $$aMiranda, Hugo Vicente$$b7
000281812 7001_ $$aSteinem, Claudia$$b8
000281812 7001_ $$aErskine, Daniel$$b9
000281812 7001_ $$0P:(DE-2719)2814138$$aOuteiro, Tiago F$$b10$$eLast author$$udzne
000281812 773__ $$0PERI:(DE-600)2819218-7$$a10.1038/s41531-025-01159-w$$gVol. 11, no. 1, p. 307$$n1$$p307$$tnpj Parkinson's Disease$$v11$$x2373-8057$$y2025
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