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Endosomal sorting related protein CHMP2B is localized in Lewy bodies and glial cytoplasmic inclusions in α-synucleinopathy

Authors
Journal
Neuroscience Letters
0304-3940
Publisher
Elsevier
Publication Date
Volume
527
Issue
1
Identifiers
DOI: 10.1016/j.neulet.2012.08.035
Keywords
  • α-Synuclein
  • Autophagy
  • Chmp2B (Charged Multivesicular Body Protein 2B)
  • Endosome
  • Lewy Body
Disciplines
  • Biology
  • Chemistry
  • Medicine

Abstract

Abstract Charged multivesicular body protein 2B (CHMP2B) is a component of the endosomal sorting complex required for transport-III, which is involved in the degradation of proteins in the endocytic and autophagic pathways. Mutations in the CHMP2B gene cause frontotemporal dementia and amyotrophic lateral sclerosis characterized by accumulation of ubiquitinated protein aggregates. Recent studies have shown that autophagosomal proteins are present in α-synuclein aggregates in neurons and glial cells in Parkinson's disease (PD), dementia with Lewy bodies (DLB) and multiple system atrophy (MSA). We therefore immunohistochemically examined the brains of various neurodegenerative diseases using CHMP2B-specific antibody. CHMP2B immunoreactivity was present in intracytoplasmic and axonal Lewy bodies in PD and DLB as well as in neuronal and glial cytoplasmic inclusions in MSA. No CHMP2B immunoreactivity was found in a variety of other neuronal and glial inclusions in TDP-43 proteinopathy and tauopathy. These findings suggest that endosomal and autophagic pathway is associated with degradation or formation of α-synuclein aggregates in α-synucleinopathy.

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