This abstract aims at systematic review of meticulously synthesize existing research surrounding structure of Lewy bodies in Parkinson’s disease (PD). We explored the accumulation of Parkin in lewy body. The aim was to grasp atypical ubiquitination in context antigenic profile of Lewy bodies.

Lewy bodies in PD display a distinctive dual-zone with dense core, surrounding halo. The underlying mechanisms of core aposynthesis and halo ubiquitin presence, exploring their relevance in PD. The impact of proteasome on Parkin accumulation in lewy body. Study also examines enhanced sensitivity of anti-ubiquitin immunocytochemistry for precise detection Lewy bodies. 

Our investigation revealed a unique ubiquitin distribution within Lewy bodies ubiquitin in the halo while being absent in the core, indicating protein aggregates a failure of the ubiquitin-proteasome system and also increased Parkin accumulation. This pattern reflects dynamic interplay between ubiquitin-proteasome system and autophagy. In antiubiquitin immunocytochemistry demonstrated sensitivity in detecting ubiquitin accumulation, particularly in cases of diffuse Lewy body disease, within antigenic profile of Lewy bodies, indicating phosphorylation and ubiquitination. 

Core aposynthesis, and ubiquitin distribution at halo , with Parkin accumulation in lewy body provides understanding of pathogenesis in PD. Elevated sensitivity of antiubiquitin immunocytochemistry underscores its potential as a precise diagnostic tool for detecting diffuse Lewy body disease. This relationship between ubiquitin, alpha synuclein, and the structural components of Lewy bodies and neurodegeneration offers promising therapeutic strategies targeting ubiquitination in PD and neurodegenerative disorders.