Selective changes in mitochondria respiratory properties in oxidative or glycolytic muscle fibers isolated from G93AhumanSOD1 transgenic mice

Neuromuscul Disord. 2001 Nov;11(8):722-7. doi: 10.1016/s0960-8966(01)00240-1.

Abstract

Cases of familial amyotrophic lateral sclerosis (FALS) are associated with mutations in cytosolic copper, zinc superoxide dismutase (SOD1). Total SOD activity and functional mitochondrial properties were studied in muscles and nervous tissues of control and transgenic mice mimicking the disease. It was found that total SOD activity was lower in nervous tissues than in muscles in both transgenic and control mice. In addition SOD activity increased during progression of disease in muscle but not in nervous tissue of transgenic mice. Maximal oxygen consumption and apparent Km for ADP were decreased in mitochondria from transgenic soleus (an oxidative muscle). However there was no difference between control and transgenic mice in respiratory parameters of mitochondria in the EDL muscle (a glycolytic muscle). These findings indicate that oxidative stress due to SOD1 mutations could alter energy metabolism in FALS mice, thereby affecting primarily oxidative muscle of the limbs, independently of motoneuron loss.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate / pharmacology
  • Amino Acid Substitution
  • Amyotrophic Lateral Sclerosis / genetics
  • Amyotrophic Lateral Sclerosis / metabolism*
  • Animals
  • Brain / metabolism
  • Cell Respiration / genetics*
  • Diaphragm / metabolism
  • Disease Models, Animal
  • Disease Progression
  • Enzyme Activation / genetics
  • Glycolysis / genetics
  • Humans
  • Mice
  • Mice, Transgenic
  • Mitochondria, Muscle / drug effects
  • Mitochondria, Muscle / metabolism*
  • Muscle, Skeletal / metabolism*
  • Organ Specificity
  • Oxidation-Reduction
  • Oxidative Phosphorylation / drug effects
  • Oxygen Consumption
  • Spinal Cord / metabolism
  • Superoxide Dismutase / genetics
  • Superoxide Dismutase / metabolism*
  • Superoxide Dismutase-1

Substances

  • SOD1 protein, human
  • Adenosine Diphosphate
  • Sod1 protein, mouse
  • Superoxide Dismutase
  • Superoxide Dismutase-1