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Intra-axonal protein aggregation in the peripheral nervous system.
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J Peripher Nerv Syst 2014 Mar; 19(1):44-9
Authors: Anne Vital, Wassillios G Meissner, Marie-Hélène Canron, Marie-Laure Martin-Negrier, Erwan Bezard, François Tison, Claude Vital
Intracellular protein aggregates are common pathological hallmarks of many neurodegenerative disorders, and a defect in axonal transport is also incriminated. Here, we studied intra-axonal abnormal protein aggregation and axonopathy by using immunohistochemistry and electron microscopy on peripheral nerve biopsies from 12 patients with chronic axonal peripheral neuropathy (PN) of unknown etiology. Among these patients, three had idiopathic Parkinson's disease (PD). Intra-axonal ubiquitin aggregates were more numerous in the patients with PD. Intra-axonal aggregates of tau AT8 were found in five patients without PD. Phosphorylated ?-synuclein aggregation was absent in all cases, while intra-axonal colocalization of 14-3-3 ? and ubiquitin was observed in two PD cases. Electron microscopy revealed enlarged axons crowded with organelles in six cases, including the three patients with PD, thus attesting a slowing of the axoplasmic flux. The number of ubiquitin aggregates was correlated with features of reduced axonal flux, while no such correlation was found for tau and 14-3-3 ?. Age did not correlate with the number of tau, ubiquitin, and 14-3-3 aggregates. Thus, both ubiquitin and/or abnormal tau intra-axonal aggregates may be found in chronic axonal PN. Ubiquitin aggregates might reduce the axonal flux or result from a disease producing slowing of axonal transport.
PMID: 24494664 [PubMed - as supplied by publisher]