These results highlight the importance of a thorough evaluation of the GI function in patients with ATTRamyloidosis and should stimulate further studies on the phenotypic differences related to genotype and geographic origin.
In conclusion, we provide novel insights regarding the molecular basis of ATTRm and ATTRwt based on large-scale cohort, expanding our understanding of the phenotypic spectrum associated with TTR gene variation.
As previously seen for ATTRamyloidosis patients with mainly cardiomyopathy, the amyloid fibrils consisted of a mixture of full-length and fragmented TTR species.
The Japanese Ministry of Health, Labour and Welfare approved tafamidis (Vyndaqel<sup>®</sup>, Pfizer Inc.) for the treatment of cardiomyopathy caused by both wild-type and mutated transthyretin-derived amyloidoses.
TTR is a protein biomarker related to diverse types of amyloidosis, such as familial amyloidotic polyneuropathy type I (FAP-I), which is the most common hereditary systemic amyloidosis.
<b>Introduction</b>: Hereditary transthyretin-mediated amyloidosis (ATTRv; v for variant) is a rare, progressive, fatal multi-systemic disease, autosomal dominantly inherited with heterogeneous clinical phenotype caused by mutations in the <i>TTR</i> gene.
The effects of curcumin on ATTRamyloidosis will be reviewed and discussed in the current work in order to contribute to knowledge of the molecular mechanisms involved in TTRamyloidosis and propose more efficient drugs for therapy.
ATTR amyloidosis may be associated with abnormal metabolism of wild-type transthyretin (previously called senile systemic amyloidosis) or with hereditary variants in the transthyretin gene.
These results indicate that dendrimer (G2) may possess both inhibitory and breaking effects on ATTR V30M amyloid, suggesting that dendrimer has the potential as a dual effective agents against TTRamyloidosis.
Here, we present a 2.97 Å cryo electron microscopy structure of a fibril purified from the tissue of a patient with hereditary Val30MetATTRamyloidosis.
Patients diagnosed with light-chain amyloidosis has a poor prognosis compared with transthyretin-related amyloidosis, while no difference was proved in prognostic analysis between wild-type and mutated TTRamyloidosis.
Hereditary amyloidogenic transthyretin (ATTRv) amyloidosis with polyneuropathy (also known as familial amyloid polyneuropathy) is a condition with adult onset caused by mutation of transthyretin (TTR) and characterized by extracellular deposition of amyloid and destruction of the somatic and autonomic PNS, leading to loss of autonomy and death.
Familial amyloid polyneuropathy (FAP) or ATTRv (amyloid TTR variant) amyloidosis is a fatal hereditary disease characterized by the deposition of amyloid fibrils composed of transthyretin (TTR).
Tafamidis meglumine, a transthyretin (TTR) stabilizer, is effective in delaying the progression of neuropathy in TTRamyloidosis with Val30Met mutations.
The inherent amyloidogenic potentialof wild type transthyretin (TTR) is enhanced by a large number of point mutations, which destabilize the TTR tetramer, thereby promoting its disassembly and pathological aggregation responsible for TTR-related amyloidosis.
These developments have resulted in last year's approval of the first siRNA therapeutic, called Onpattro (patisiran), for treatment of hereditary amyloidogenic transthyretin (TTR) amyloidosis.
Since the phenotype of ATTRamyloidosis varies depending on its penetration rate, it is crucial to always keep in mind the possibility of hereditary ATTRamyloidosis even in the case of amyloidosis with no clear family history.