Chaperone-like activity of synucleins

FEBS Lett. 2000 May 26;474(1):116-9. doi: 10.1016/s0014-5793(00)01563-5.

Abstract

Synucleins are a family of small proteins that are predominantly expressed in neurons. The functions of the synucleins are not entirely understood, but they have been implicated in the pathogenesis of several neurodegenerative diseases. Our data show that alpha-, beta- or gamma-synuclein suppresses the aggregation of thermally denatured alcohol dehydrogenase and chemically denatured insulin. The A53T but not the A30P mutant alpha-synuclein was able to inhibit the aggregation of insulin and the chaperone-like activity of alpha-synuclein was lost upon removal of its C-terminal residues 98-140. These results demonstrate that synucleins with the exception of the A30P mutant possess chaperone-like activity.

Publication types

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

MeSH terms

  • Alcohol Dehydrogenase / chemistry
  • Disulfides / chemistry
  • Dithiothreitol / pharmacology
  • Escherichia coli
  • Hot Temperature
  • Humans
  • Insulin / chemistry
  • Molecular Chaperones / pharmacology*
  • Mutation
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / pharmacology*
  • Protein Denaturation
  • Recombinant Proteins / pharmacology
  • Ribonuclease, Pancreatic / chemistry
  • Synucleins
  • alpha-Synuclein
  • gamma-Synuclein

Substances

  • Disulfides
  • Insulin
  • Molecular Chaperones
  • Nerve Tissue Proteins
  • Recombinant Proteins
  • SNCA protein, human
  • Synucleins
  • alpha-Synuclein
  • gamma-Synuclein
  • Alcohol Dehydrogenase
  • Ribonuclease, Pancreatic
  • Dithiothreitol