ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions

Neuron. 1997 Feb;18(2):327-38. doi: 10.1016/s0896-6273(00)80272-x.

Abstract

High levels of familial Amyotrophic Lateral Sclerosis (ALS)-linked SOD1 mutants G93A and G37R were previously shown to mediate disease in mice through an acquired toxic property. We report here that even low levels of another mutant, G85R, cause motor neuron disease characterized by an extremely rapid clinical progression, without changes in SOD1 activity. Initial indicators of disease are astrocytic inclusions that stain intensely with SOD1 antibodies and ubiquitin and SOD1-containing aggregates in motor neurons, features common with some cases of SOD1 mutant-mediated ALS. Astrocytic inclusions escalate markedly as disease progresses, concomitant with a decrease in the glial glutamate transporter (GLT-1). Thus, the G85R SOD1 mutant mediates direct damage to astrocytes, which may promote the nearly synchronous degeneration of motor neurons.

Publication types

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

MeSH terms

  • ATP-Binding Cassette Transporters / metabolism*
  • Amino Acid Transport System X-AG
  • Amyotrophic Lateral Sclerosis / pathology
  • Amyotrophic Lateral Sclerosis / physiopathology*
  • Animals
  • Astrocytes / pathology
  • Astrocytes / physiology*
  • Axons / ultrastructure
  • Disease Models, Animal
  • Genes, Dominant
  • Humans
  • Mice
  • Mice, Transgenic
  • Microscopy, Electron
  • Nerve Degeneration / physiology
  • Neurons / physiology
  • Point Mutation
  • Spinal Cord / metabolism
  • Superoxide Dismutase / genetics*
  • Superoxide Dismutase / metabolism
  • Ubiquitins / metabolism

Substances

  • ATP-Binding Cassette Transporters
  • Amino Acid Transport System X-AG
  • Ubiquitins
  • Superoxide Dismutase