Amyloidosis due to natural apoliprotein A-I Variants. Mechanisms involved in the pathogenicity pathways

TRICERRI, MA; RAMELLA; NA; ROSU; SA; GADDI, GM; GISONNO, R; SCHINELLA, G; PRIETO; ED; CALABRESE, G; BARANDIARÁN, A; FINARELLI; GS

KUMAMOTO

Simposio; ISA; 2018

ISA

The cascade of molecular events leading to amyloidosis is variable. Different protein conformations such as the precursor monomer, oligomeric or fibrillar structures could determine the pathology1. Components of the extracellular matrix, like glycoproteins or their glycosaminoglycan chains (GAGs) have in addition been suggested to induce the formation of amyloid aggregates2. Human apolipoprotein A-I (apoA-I)-derived amyloidosis is poorly known. About 20 naturally occurring mutations have been associated with hereditary amyloidosis causing multiple organ failure. Our previous studies strongly suggest that a decrease in apoA-I variants´ stability and changes in the microenvironment could elicit protein misfolding and tissue deposition3. Here we got deep insight into the mechanisms that could determine amyloidosis due to apoA-I.