Mutant superoxide dismutase disrupts cytoplasmic dynein in motor neurons

Neuroreport. 2005 Apr 25;16(6):533-6. doi: 10.1097/00001756-200504250-00002.

Abstract

Cytoplasmic dynein and dynactin drive retrograde axonal transport in neurons, and mutations in dynein/dynactin cause motor neuron degeneration. To test whether defects in dynein/dynactin function are involved in the neurodegenerative disease amyotrophic lateral sclerosis, we examined neurotracer transport from muscle to motor neuron in a transgenic mouse model of amyotrophic lateral sclerosis. Significant inhibition was observed, which was temporally correlated with declines in muscle strength. No decrease in dynein/dynactin expression was observed, but immunohistochemistry suggests that dynein associates with aggregates of mutant Cu/Zn superoxide dismutase 1. Expression of mutant Cu/Zn superoxide dismutase 1 in primary motor neurons altered the cellular localization of dynein, suggesting an inhibition of dynein/dynactin function. Thus, inhibition of dynein/dynactin function may have a role in motor neuron degeneration in amyotrophic lateral sclerosis.

Publication types

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

MeSH terms

  • Amyotrophic Lateral Sclerosis / metabolism*
  • Amyotrophic Lateral Sclerosis / physiopathology*
  • Animals
  • Cytoplasm / metabolism
  • Dynactin Complex
  • Dyneins / metabolism*
  • Male
  • Mice
  • Mice, Inbred Strains
  • Mice, Transgenic
  • Microtubule-Associated Proteins / metabolism
  • Molecular Motor Proteins / metabolism
  • Motor Neurons / metabolism*
  • Nerve Degeneration / metabolism
  • Nerve Degeneration / physiopathology
  • Superoxide Dismutase / genetics*
  • Superoxide Dismutase / metabolism
  • Superoxide Dismutase-1

Substances

  • Dynactin Complex
  • Microtubule-Associated Proteins
  • Molecular Motor Proteins
  • Sod1 protein, mouse
  • Superoxide Dismutase
  • Superoxide Dismutase-1
  • Dyneins