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Published on: May 9, 2012
Muscle-restricted Nox4 knockout partially corrects muscle contractility following spinal cord injury in mice
Carlos A Toro1,2, Rita De Gasperi1,2,3,4, Abdurrahman Aslan1,2
1Spinal Cord Damage Research Center, James J Peters VA Medical Center.
Abstract:
Spinal cord injury (SCI) results in severe atrophy of skeletal muscle in paralyzed regions, and a decrease in the force generated by muscle per unit of cross-sectional area. Oxidation of skeletal muscle ryanodine 1 receptors (RyR1) reduces contractile force due to reduced binding of calstabin 1 to RyR1 together with altered gating of RyR1. One cause of RyR1 oxidation is NADPH oxidase 4 (Nox4). We have previously shown that in rats, RyR1 was oxidized and bound less calstabin 1 at 56 days after spinal cord injury (SCI) by transection. Here, we used a conditional knock-out mouse model of Nox4 in muscle to investigate the role of Nox4 in reduced muscle specific force after SCI. Peak twitch force in control mice after SCI was reduced by 42% compared to sham-operated controls but was increased by approximately 43% in SCI Nox4 conditional KO mice compared to SCI controls although it remained less than that for sham-operated controls. Unlike what observed in rats, after SCI the expression of Nox4 was not increased in gastrocnemius muscle and binding of calstabin 1 to RyR1 was not reduced in this muscle. The results suggest a link between Nox4 expression in muscle tissue and reduction in muscle twitch force, however further studies are needed to understand the mechanistic basis for this linkage.
Insights
Spinal cord injury (SCI) causes muscle atrophy and reduced force. Targeting NADPH oxidase 4 (Nox4) in muscle may improve muscle function after SCI, though mechanisms require further study.
Area of Science:
- Biomedical Engineering
- Neuroscience
- Muscle Physiology
Background:
- Spinal cord injury (SCI) leads to significant skeletal muscle atrophy and decreased force generation in paralyzed limbs.
- Oxidation of skeletal muscle ryanodine receptors (RyR1) impairs muscle contraction by reducing calstabin 1 binding and altering receptor gating.
- NADPH oxidase 4 (Nox4) is implicated as a cause of RyR1 oxidation.
Conclusions:
- Results suggest a correlation between Nox4 expression in muscle and diminished muscle twitch force following SCI.
- Further research is necessary to elucidate the precise molecular mechanisms linking Nox4 to reduced muscle force after spinal cord injury.

