Chaperone proteins protect against desmin fragment amyloid aggregation

In desmin-related cardiomyopathy, cellular stresses cause desmin to cleave and aggregate in vivo. Cleaved desmin fragments are amyloidogenic and induce misfolding, aggregation, and amyloid fibril formation of full-length wild type desmin. Alongside this disease condition, cells overexpress αB-crystallin and heat shock protein (HSP) 27 as cardioprotective chaperones. Chaperone proteins may refold, sequester, or disaggregate misfolded or aggregating client proteins. Previously, little was known ab