Atg7 induces basal autophagy and rescues autophagic deficiency in CryABR120G cardiomyocytes.

ABSTRACT:

Rationale

Increasing evidence suggests that misfolded proteins and intracellular aggregates contribute to cardiac disease and heart failure. Several cardiomyopathies, including the αB-crystallin R120G mutation (CryAB(R120G)) model of desmin-related cardiomyopathy, accumulate cytotoxic misfolded proteins in the form of preamyloid oligomers and aggresomes. Impaired autophagic function is a potential cause of misfolded protein accumulations, cytoplasmic aggregate loads, and cardiac disease. Atg7, a mediator of autophagosomal biogenesis, is a putative regulator of autophagic function.

Objective

To determine whether autophagic induction by Atg7 is sufficient to reduce misfolded protein and aggregate content in protein misfolding-stressed cardiomyocytes.

Methods and results

SUBMITTER: Pattison JS 

PROVIDER: S-EPMC3150753 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature