MnSOD deficiency has a differential effect on disease progression in two different ALS mutant mouse models

Muscle Nerve. 2008 Sep;38(3):1173-83. doi: 10.1002/mus.21049.

Abstract

Mitochondrial dysfunction and oxidative stress are thought to participate in the pathogenesis of amyotrophic lateral sclerosis (ALS). The purpose of this study was to determine the effect of reduced mitochondrial antioxidant defense on lifespan and disease progression in two mouse models of familial ALS (G93A and H46R/H48Q mutant lines) that represent pseudo-wildtype and metal-deficient ALS mutants, respectively. The metal-deficient H46R/H48Q mutant differs from the G93A mutant in that it cannot bind copper in the active site and thus lacks SOD activity. We crossed each of these mutant lines with mice deficient in the mitochondrial matrix antioxidant enzyme MnSOD (Sod2+/- mice). In both high (G93A1Gur) and low (G93ADL) copy G93A strains, MnSOD deficiency caused a decrease in lifespan that was associated with a reduced disease duration rather than earlier disease onset. In contrast, MnSOD deficiency had no effect on lifespan or disease parameters of H46R/H48Q mutant mice. MnSOD deficiency thus has a differential effect on disease progression in different mutant SOD1 ALS mouse models, suggesting that different ALS-causing mutations in SOD1 result in disease progression by at least proximally different mechanisms/pathways.

Publication types

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

MeSH terms

  • Age Factors
  • Amyotrophic Lateral Sclerosis / genetics*
  • Amyotrophic Lateral Sclerosis / mortality
  • Amyotrophic Lateral Sclerosis / physiopathology*
  • Analysis of Variance
  • Animals
  • Disease Models, Animal*
  • Disease Progression
  • Female
  • Male
  • Mice
  • Mice, Transgenic
  • Motor Activity / genetics
  • Mutation / genetics*
  • Severity of Illness Index
  • Sex Factors
  • Superoxide Dismutase / deficiency*
  • Survival Analysis

Substances

  • SOD1 G93A protein
  • Superoxide Dismutase