CHARACTERIZING THE ROLE OF ALPHA-SYNUCLEIN IN MELANOMA

FLORENCIA MALIZIA; ANSELMINO, LUCIANO; LUCÍA ZANOTTI; MAURICIO MENACHO MÁRQUEZ

Congreso; Reunión Anual de Sociedades de Biociencias; 2020

The amyloid protein alpha synuclein (αS) is the main component ofLewy bodies, the neuropathological hallmark of Parkinson’s disease(PD). The mechanisms underlying αS aggregation, neurotoxicityand cell-to-cell transmission were explored in the context of PD.Recent evidence suggests that αS may also play a putative role inmelanoma, the most dangerous form of skin cancer. Current studiessuggested that αS could be protective for advanced melanoma butits role in this type of cancer was not deeply explored yet.Previously, we demonstrated by in vitro studies that melanomacells are able to uptake different aggregation species of αS. Thesespecies were not toxic for melanoma cells. Instead, they promotedproliferation, cytoskeleton rearrangement and migration. Here,we evaluated the ability of human SK-MEL 28 and mouse B16-F10melanoma cells to form clones in the presence of αS fibers by standardcolony forming assays. Cells were incubated (or not) with αSfibers for 24 hours and 300 cells were plated to form colonies. Forboth types of cells, incubation with αS promoted a higher number ofclones (P