Amyloidosis represents a largely unexplored field in medicine, with many grey areas remaining. The search for the mechanism triggering protein misfolding has been an important research topic for many decades. In recent years, cardiac involvement due to extracellular infiltration by transthyretin (TTR) amyloidosis, so-called ‘TTR amyloid cardiomyopathy’ (ATTR-AC), has proven to be a frequently unrecognized condition [1]. TTR is a homotetrameric carrier protein produced mostly by the liver [2]. A higher tendency to dissociate in misfolded monomers and to fibrillate is thought to occur in the presence of favourable conditions, such as ageing with associated failure of homoeostatic mechanisms in wild-type TTR (TTRwt) [3] or destabilizing mutations in variant TTR (TTRv) [1].
