FIND ARTICLE

Volume: 
Issue: 
2
Date of issue: 

Synucleins are a family of small (15–20 kDa), soluble, conserved proteins that are predominan- tly expressed in neurons and include α-, β-, γ-Synuclein and Synoretine. Among the synuclein family exclusively α-Synuclein is the precursor protein for highly hydrophobic 35-amino acid peptide NAC (non-amyloid β component of Alzheimer’s disease plaques). This presynaptic protein associated with synaptic vesicles is also present in cytosol. Under physiological conditions α-Synuclein is natively unfolded. Cellular function of this protein is till know poorly understood, however, several lines of evidence suggest its potential role in regulation of synaptic function, neuronal plasticity, as well as cell survival. Physiological functions of this protein are disturbed by its aggregation. Posttranslational modification, oxidative stress or catabolism defects can promote its aggregation and deposition in cells in the form of Lewy bodies. Aggregated form of α-Synuclein could be involved in cell death in several neurode- generative disorders, including Parkinson’s disease, subtype of Alzheimer’s disease with Lewy bodies, as well as in dementia with Lewy bodies. The understanding of processes responsible for α-Synuclein aggregation and NAC liberation is very important for the elucidation of pathomechanism of several neurodegenerative diseases and their effective therapy.

The Editorial Board
Andrzej Łukaszyk - przewodniczący, Zofia Bielańska-Osuchowska, Szczepan Biliński, Mieczysław Chorąży, Aleksander Koj, Włodzimierz Korochoda, Leszek Kuźnicki, Aleksandra Stojałowska, Lech Wojtczak

Editorial address:
Katedra i Zakład Histologii i Embriologii Uniwersytetu Medycznego w Poznaniu, ul. Święcickiego 6, 60-781 Poznań, tel. +48 61 8546453, fax. +48 61 8546440, email: mnowicki@ump.edu.pl

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