Protein unfolding in cardiomyopathies.

For many years, protein misfolding was the basis for biochemical and biophysical studies in vitro or in microorganisms such as yeast. Recently, clinically related studies are merging the evidence collected from microorganisms with human diseases. Thus, a growing body of evidence is accumulating that identifies defects in protein folding or protein degradation as pathogenetic hallmarks for many disease entities predominantly of late onset, including cardiomyopathies and heart failure. Dissecting the pathogenetic pathways opens new opportunities for therapy aimed to re-equilibrate the folding capacities. The development of chemical and pharmacologic chaperones has helped to understand the mechanisms of some aspects of protein misfolding and may find new applications to direct target-specific therapy. Further understanding of the mechanisms of protein formation and its defects will address the important aspects of modern medicine of directing early diagnosis and prevention.