Mitochondria in motor nerve terminals: function in health and in mutant superoxide dismutase 1 mouse models of familial ALS

J Bioenerg Biomembr. 2011 Dec;43(6):581-6. doi: 10.1007/s10863-011-9392-1.

Abstract

Mitochondria contribute to neuronal function not only via their ability to generate ATP, but also via their ability to buffer large Ca(2+) loads. This review summarizes evidence that mitochondrial Ca(2+) sequestration is especially important for sustaining the function of vertebrate motor nerve terminals during repetitive stimulation. Motor terminal mitochondria can sequester large amounts of Ca(2+) because they have mechanisms for limiting both the mitochondrial depolarization and the increase in matrix free [Ca(2+)] associated with Ca(2+) influx. In mice expressing mutations of human superoxide dismutase -1 (SOD1) that cause some cases of familial amyotrophic lateral sclerosis (fALS), motor terminals degenerate well before the death of motor neuron cell bodies. This review presents evidence for early and progressive mitochondrial dysfunction in motor terminals of mutant SOD1 mice (G93A, G85R). This dysfunction would impair mitochondrial ability to sequester stimulation-associated Ca(2+) loads, and thus likely contributes to the early degeneration of motor terminals.

Publication types

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

MeSH terms

  • Amino Acid Substitution
  • Amyotrophic Lateral Sclerosis / enzymology*
  • Amyotrophic Lateral Sclerosis / genetics
  • Amyotrophic Lateral Sclerosis / pathology
  • Animals
  • Calcium / metabolism
  • Disease Models, Animal
  • Genetic Diseases, Inborn / enzymology*
  • Genetic Diseases, Inborn / genetics
  • Genetic Diseases, Inborn / pathology
  • Humans
  • Mice
  • Mice, Transgenic
  • Mitochondria / enzymology*
  • Mitochondria / genetics
  • Mitochondria / pathology
  • Motor Endplate / enzymology*
  • Motor Endplate / genetics
  • Motor Endplate / pathology
  • Motor Neurons / enzymology*
  • Motor Neurons / pathology
  • Mutation
  • Mutation, Missense
  • Superoxide Dismutase / genetics
  • Superoxide Dismutase / metabolism*
  • Superoxide Dismutase-1

Substances

  • SOD1 protein, human
  • Sod1 protein, mouse
  • Superoxide Dismutase
  • Superoxide Dismutase-1
  • Calcium