Protein aggregates and novel presenilin gene variants in idiopathic dilated cardiomyopathy

Circulation. 2010 Mar 16;121(10):1216-26. doi: 10.1161/CIRCULATIONAHA.109.879510. Epub 2010 Mar 1.

Abstract

Background: Heart failure is a debilitating condition resulting in severe disability and death. In a subset of cases, clustered as idiopathic dilated cardiomyopathy (iDCM), the origin of heart failure is unknown. In the brain of patients with dementia, proteinaceous aggregates and abnormal oligomeric assemblies of beta-amyloid impair cell function and lead to cell death.

Methods and results: We have similarly characterized fibrillar and oligomeric assemblies in the hearts of iDCM patients, pointing to abnormal protein aggregation as a determinant of iDCM. We also showed that oligomers alter myocyte Ca(2+) homeostasis. Additionally, we have identified 2 new sequence variants in the presenilin-1 (PSEN1) gene promoter leading to reduced gene and protein expression. We also show that presenilin-1 coimmunoprecipitates with SERCA2a.

Conclusions: On the basis of these findings, we propose that 2 mechanisms may link protein aggregation and cardiac function: oligomer-induced changes on Ca(2+) handling and a direct effect of PSEN1 sequence variants on excitation-contraction coupling protein function.

Publication types

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

MeSH terms

  • Adult
  • Aged
  • Amyloid / analysis
  • Amyloid beta-Peptides / analysis
  • Calcium / metabolism
  • Cardiomyopathy, Dilated / genetics*
  • Cardiomyopathy, Dilated / metabolism*
  • Female
  • Humans
  • Immunohistochemistry
  • Male
  • Middle Aged
  • Mutation
  • Polymorphism, Single Nucleotide
  • Presenilin-1 / genetics*
  • Presenilin-2 / genetics
  • Proteins / chemistry*

Substances

  • Amyloid
  • Amyloid beta-Peptides
  • PSEN1 protein, human
  • PSEN2 protein, human
  • Presenilin-1
  • Presenilin-2
  • Proteins
  • Calcium