Mutant desmin substantially perturbs mitochondrial morphology, function and maintenance in skeletal muscle tissue.

ABSTRACT: Secondary mitochondrial dysfunction is a feature in a wide variety of human protein aggregate diseases caused by mutations in different proteins, both in the central nervous system and in striated muscle. The functional relationship between the expression of a mutated protein and mitochondrial dysfunction is largely unknown. In particular, the mechanism how this dysfunction drives the disease process is still elusive. To address this issue for protein aggregate myopathies, we performed a comprehensive, multi-level analysis of mitochondrial pathology in skeletal muscles of human patients with mutations in the intermediate filament protein desmin and in muscles of hetero- and homozygous knock-in mice carrying the R349P desmin mutation. We demonstrate that the expression of mutant desmin caus

SUBMITTER: Winter L 

PROVIDER: S-EPMC4992032 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature