Although not described previously, elevated IOP may develop in patients with vitreous amyloidosis due to a TTR Val30Gly mutation in the transthyretin gene.
Proportion between wild-type and mutant protein in truncated compared to full-length ATTR: an analysis on transplanted transthyretinT60Aamyloidosis patients.
Central nervous system (CNS) complications are increasingly noted in liver transplanted (LTx) hereditary transthyretinamyloid (ATTRm) amyloidosis patients; this suggests that the increased survival allows for intracranial ATTRm formation from brain synthesized mutant TTR.
Only one patient in our study had light chain amyloidosis and showed higher TBR than patients with transthyretinamyloid: TBR 3.0 versus TBR median 1.44, IQR 1.33-1.69.
Although not described previously, elevated IOP may develop in patients with vitreous amyloidosis due to a TTRVal30Gly mutation in the transthyretin gene.
Hereditary ATTRV30Mamyloidosis is a lethal autosomal dominant sensorimotor and autonomic neuropathy caused by deposition of aberrant transthyretin (TTR).
This case illustrated the clinical and pathologic phenotype of an ATTRamyloidosis patient who initially presented impaired renal function and p.Leu75Pro variant was found by sequencing the coding region of TTR gene.
(99m)Tc-DPD uptake was also absent (score of 0) among unaffected controls and in 2 unaffected relatives of patients with hereditary transthyretin-related amyloidosis who harbor a mutation in the TTR gene.
Predominant symptom presentation in patients with hereditary TTRamyloidosis differed according to the underlying disease-causing mutation (polyneuropathy for Val30Met, cardiomyopathy for Val122Ile and Leu111Met, and mixed for Glu89Gln).
Clinical and necessary examination materials were collected from nine patients of eight families with hereditary TTRamyloidosis at Peking University First Hospital from January 2007 to November 2014.
The secretion of transthyretin (TTR) variants contributes to the pathogenesis of amyloidosis because they form aggregates in the extracellular environment.
At the same time, for one family of proteinopathies, the rare TTRamyloidoses, disease-modifying therapy has existed for almost 3 decades and two new types of disease-modifying therapy have become available more recently.
Familial amyloidotic polyneuropathy (FAP) type I, the most common dominantly inherited form of amyloidosis, is caused by a Val-to-Met point mutation at position 30 (Val(30)-->Met) in the protein transthyretin.
This diboronic acid inhibits fibril formation by both wild-type TTR and a common disease-related variant, V30MTTR, as effectively as does tafamidis, a small-molecule drug used to treat TTR-related amyloidosis in the clinic.
The demonstration, in hereditary systemic transthyretinVal30Metamyloidosis, that such differences are consistently associated with amyloid fibrils composed of different length transthyretin fragments sheds new light on this question and will open the way to further informative studies.