Decreased amount of vimentin N-terminal truncated proteolytic products in parkin-mutant skin fibroblasts

Biochem Biophys Res Commun. 2020 Jan 15;521(3):693-698. doi: 10.1016/j.bbrc.2019.10.154. Epub 2019 Nov 4.

Abstract

Vimentin, a member of cytoskeleton intermediate filaments proteins, plays a critical role in cell structure and dynamics. The present proteomic study reveals reduced amount of six different lengths, N-terminal truncated proteolytic products of vimentin, in the primary skin fibroblasts from two unrelated PD patients, as compared to control fibroblasts. The decreased amount of N-terminal truncated forms of vimentin in parkin-mutant fibroblasts, could contribute to impairment of cellular function, potentially contributing to the pathogenesis of Parkinson disease.

Keywords: Human skin fibroblasts; Mass spectrometry; Parkinson’s disease; Proteomics; Two-dimensional gel electrophoresis.

Publication types

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

MeSH terms

  • Adult
  • Cells, Cultured
  • Female
  • Fibroblasts / metabolism*
  • Fibroblasts / pathology
  • Humans
  • Middle Aged
  • Mutation
  • Parkinson Disease / genetics
  • Parkinson Disease / metabolism*
  • Parkinson Disease / pathology
  • Protein Isoforms / analysis
  • Protein Isoforms / metabolism
  • Proteolysis
  • Proteomics
  • Skin / metabolism
  • Skin / pathology
  • Ubiquitin-Protein Ligases / genetics*
  • Vimentin / analysis
  • Vimentin / metabolism*

Substances

  • Protein Isoforms
  • Vimentin
  • Ubiquitin-Protein Ligases
  • parkin protein