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• W2058078504 startingPage "1913" @default.
• W2058078504 abstract "The transthyretin amyloidoses are diseases of protein misfolding characterized by the extracellular deposition of fibrils and other aggregates of the homotetrameric protein transthyretin (TTR) in peripheral nerves, heart, and other tissues. Age is the major risk factor for the development of these diseases. We hypothesized that an age-associated increase in the level of protein oxidation could be involved in the onset of the senile forms of the TTR amyloidoses. To test this hypothesis, we have produced and characterized relevant age-related oxidative modifications of the wild type (WT) and the Val122Ile (V122I) TTR variant, both involved in cardiac TTR deposition in the elderly. Our studies show that methionine/cysteine-oxidized TTR and carbonylated TTR from either the WT or the V122I variant are thermodynamically less stable than their nonoxidized counterparts. Moreover, carbonylated WT and carbonylated V122I TTR have a stronger propensity to form aggregates and fibrils than WT and V122I TTR, respectively, at physiologically attainable pH values. It is well-known that TTR tetramer dissociation, the limiting step for aggregation and amyloid fibril formation, can be prevented by small molecules that bind the TTR tetramer interface. Here, we report that carbonylated WT TTR is less amenable to resveratrol-mediated tetramer stabilization than WT TTR. All the oxidized forms of TTR tested are cytotoxic to a human cardiomyocyte cell line known to be a target for cardiac-specific TTR variants. Overall, these studies demonstrate that age-related oxidative modifications of TTR can contribute to the onset of the senile forms of the TTR amyloidoses." @default.
• W2058078504 created "2016-06-24" @default.
• W2058078504 creator A5002705877 @default.
• W2058078504 creator A5020895462 @default.
• W2058078504 creator A5050150743 @default.
• W2058078504 date "2013-03-04" @default.
• W2058078504 modified "2023-10-17" @default.
• W2058078504 title "Age-Related Oxidative Modifications of Transthyretin Modulate Its Amyloidogenicity" @default.
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• W2058078504 doi "https://doi.org/10.1021/bi301313b" @default.
• W2058078504 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3604100" @default.
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