The sulfation code for propagation of neurodegeneration [Protein Structure and Folding]

Prion-like propagation of protein aggregates is thought to be an essential feature in many neurodegenerative diseases, but the mechanisms underlying transcellular transfer of protein aggregates remain unclear. Stopschinski et al. now demonstrate that the cellular uptake of tau, Aβ, and α-synuclein aggregates mediated by heparan sulfate proteoglycans (HSPGs) varies with distinct glycosaminoglycan chain length and sulfation patterns. The results help us to understand how different protein aggregates propagate, leading to distinct neurodegenerative pathologies.

Source: Journal of Biological Chemistry - July 6, 2018 Category: Chemistry Authors: Masahito Yamada, Tsuyoshi Hamaguchi Tags: Editors ' Picks Highlights Source Type: research