Following the fate of endocytosed fibrils

J Biol Chem. 2017 Aug 11;292(32):13498-13499. doi: 10.1074/jbc.H117.780296.

Abstract

Cell-to-cell transmission of intracellular protein aggregates is considered a central event in many neurodegenerative diseases, but little is known about the underlying molecular mechanisms. A new study employs fluorescence quenching to examine the fate of α-synuclein, a key molecule in the pathology of Parkinson's disease and related disorders, in primary cultured neurons, finding that endocytosis and lysosomal processing of exogenous fibrils may explain the transmission of α-synuclein pathology.

Publication types

  • Editorial
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Endocytosis*
  • Humans
  • Lysosomes / metabolism*
  • Lysosomes / pathology
  • Lysosomes / ultrastructure
  • Models, Biological*
  • Neurons / metabolism*
  • Neurons / pathology
  • Neurons / ultrastructure
  • Protein Aggregation, Pathological / metabolism*
  • Protein Aggregation, Pathological / pathology
  • alpha-Synuclein / chemistry
  • alpha-Synuclein / metabolism*

Substances

  • SNCA protein, human
  • alpha-Synuclein