Dimebon reduces the levels of aggregated amyloidogenic protein forms in detergent-insoluble fractions in vivo

Bull Exp Biol Med. 2012 Apr;152(6):731-3. doi: 10.1007/s10517-012-1618-7.
[Article in English, Russian]

Abstract

Aggregation of proteins liable to assembling into fibrils with subsequent formation of amyloid incorporations is an important component in the pathogenesis of many neurodegenerative diseases. Dimebon, a Russian drug, reduces the content of detergent-insoluble fibrillar forms of synuclein, the main protein component of pathological incorporations in neurons of transgenic mouse strain used in the study.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloidogenic Proteins / genetics
  • Amyloidogenic Proteins / metabolism
  • Animals
  • Detergents / chemistry
  • Gene Expression / drug effects
  • Indoles / administration & dosage*
  • Male
  • Mice
  • Mice, Transgenic
  • Neurodegenerative Diseases / drug therapy*
  • Neurodegenerative Diseases / genetics
  • Neurodegenerative Diseases / metabolism
  • Neurons / drug effects*
  • Neurons / metabolism
  • Neuroprotective Agents / administration & dosage*
  • Spinal Cord / drug effects
  • Spinal Cord / metabolism
  • Ubiquitin / metabolism
  • Ubiquitinated Proteins / genetics
  • Ubiquitinated Proteins / metabolism
  • gamma-Synuclein / genetics*
  • gamma-Synuclein / metabolism

Substances

  • Amyloidogenic Proteins
  • Detergents
  • Indoles
  • Neuroprotective Agents
  • Ubiquitin
  • Ubiquitinated Proteins
  • gamma-Synuclein
  • latrepirdine