Researchers have identified a common structure among toxic transthyretin (TTR) clumps, called amyloid fibrils, in heart tissue from people carrying mutations linked to hereditary transthyretin amyloidosis with polyneuropathy (hATTR-PN).
Such structural similarity contrasts with previous reports of structural variability among heart amyloid fibrils from other primarily polyneuropathic forms of hereditary ATTR amyloidosis. The results suggest that amyloid fibril architecture alone may not fully explain the clinical diversity in ATTR amyloidosis, a group of diseases that includes hATTR-PN.
“This structural consistency is significant for the development of structure-guided diagnostic tools capable of addressing the diverse spectrum of ATTR amyloidosis,” the researchers wrote.