Myotube elasticity of an amyotrophic lateral sclerosis mouse model

Sci Rep. 2018 Apr 12;8(1):5917. doi: 10.1038/s41598-018-24027-5.

Abstract

Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease that affects the motor system leading to generalized paralysis and death of patients. The understanding of early pathogenic mechanisms will help to define early diagnostics criteria that will eventually provide basis for efficient therapeutics. Early symptoms of ALS usually include muscle weakness or stiffness. Therefore, mechanical response of differentiated myotubes from primary cultures of mice, expressing the ALS-causing SOD1 G93A mutation, was examined by atomic force microscopy. Simultaneous acquisition of topography and cell elasticity of ALS myotubes was performed by force mapping method, compared with healthy myotubes and supplemented with immunofluorescence and qRT-PCR studies. Wild type myotubes reveal a significant difference in elasticity between a narrow and a wide population, consistent with maturation occurring with higher actin expression relative to myosin together with larger myotube width. However, this is not true for SOD1 G93A expressing myotubes, where a significant shift of thin population towards higher elastic modulus values was observed. We provide evidence that SOD1 mutant induces structural changes that occurs very early in muscle development and well before symptomatic stage of the disease. These findings could significantly contribute to the understanding of the role of skeletal muscle in ALS pathogenesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / genetics
  • Amyotrophic Lateral Sclerosis / genetics*
  • Amyotrophic Lateral Sclerosis / physiopathology
  • Animals
  • Cell Differentiation / genetics
  • Disease Models, Animal
  • Elasticity / physiology
  • Gene Expression Regulation / drug effects
  • Humans
  • Mechanical Phenomena
  • Mice
  • Microscopy, Atomic Force
  • Muscle Development / genetics*
  • Muscle Fibers, Skeletal / chemistry*
  • Muscle Fibers, Skeletal / pathology
  • Muscle Fibers, Skeletal / ultrastructure
  • Muscle Weakness / genetics
  • Mutation
  • Myosins / genetics
  • Superoxide Dismutase-1 / chemistry
  • Superoxide Dismutase-1 / genetics*

Substances

  • Actins
  • Sod1 protein, mouse
  • Superoxide Dismutase-1
  • Myosins