The Correlation Between Amyloidogenic Transthyretin Variants and Their Localization as Amyloids
Keywords:
Hereditary transthyretin amyloidosis, Transthyretin Variants, Protein Aggregation, Amyloid Fibrils, Localization, TTR StructureAbstract
Transthyretin (TTR) is a homotetrameric protein that can aggregate and misfold into amyloid fibrils when genetically mutated, resulting in hereditary TTR amyloidosis (hATTR) when deposited on organs and tissues. Unlike other types of TTR amyloidosis, hATTR is a phenotypically diverse disease in which TTR variants possess a propensity to target certain organs or tissues. This review aims to explore the current knowledge on the characteristics of phenotypically different amyloidogenic mutated TTR variants as well as a potential correlation between these variants and their localization in the body. Differentiating characteristics between central-nervous-system (CNS)-associated variants and non-CNS-associated variants have been reported on and some potential correlations have been suggested in V30M amyloidosis; however, these findings cannot be generalized to the majority of TTR variants.
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