Cardiac amyloidosis or amyloid cardiomyopathy (ACM), commonly resulting from extracellular deposition of amyloid fibrils consisted of misfolded immunoglobulin light chain (AL) or transthyretin (TTR) protein, is an underestimated cause of heart failure and cardiac arrhythmias.
Hereditary transthyretin amyloidosis (ATTR) is a genetic disease caused by a point mutation in the TTR gene that causes the liver to produce an unstable TTR protein.
Homozygosity for the V122I mutation in transthyretin is associated with earlier onset of cardiac amyloidosis in the African American population in the seventh decade of life.
The aims of this study were to characterize RV involvement in patients with CA and to identify parameters that may help in the differential diagnosis between ALCA and transthyretin-derived CA subtypes.
Inotersen, a 2'-O-methyoxyethyl-modified antisense oligonucleotide, which acts by reducing the production of transthyretin, was recently demonstrated to improve disease course and quality of life in early hereditary transthyretin amyloidosis polyneuropathy in a 15-month Phase III study.
Prospective evaluation of the morbidity and mortality of wild-type and V122I mutant transthyretinamyloid cardiomyopathy: the Transthyretin Amyloidosis Cardiac Study (TRACS).
This study demonstrates significant proteomic differences between ATTRm patient and control sera, as well as ATTRm phenotype-associated variations in the circulating levels of several proteins including TTR.
Compared with controls (136.3 ± 24.4%, P < 0.05), mean values for MCF were significantly reduced in LVH (HHD:92.6 ± 20%, HCM:80 ± 20.3%, transthyretinCA:74.9 ± 32.2% and light-chain (AL) CA:50.5 ± 21.4%).
In Group III patients with non-Val30MetATTRs, the median age of onset was 51.5 years and 14 of the 20 patients had cardiac amyloidosis with congestive heart failure on admission or soon after a definite diagnosis.
Transthyretin (TTR) is a major amyloidogenic protein associated with hereditary (ATTRm) and nonhereditary (ATTRwt) intractable systemic transthyretin amyloidosis.
They also should prove useful for studying transthyretin synthesis by other cell types, as transthyretin has been implicated in many functions and conditions, including clearance of β-amyloid peptides associated with Alzheimer's disease, heat shock in neurons, processing of neuropeptides, nerve regeneration, astrocyte metabolism, and transthyretin amyloidosis.
Although the diagnostic sensitivity of FPFNA is substantially lower in transthyretinCA, particularly ATTRwt, it may nevertheless sometimes obviate the need for endomyocardial biopsy.
Transthyretin amyloidosis (ATTR amyloidosis) is a rare disease that results from the deposition of misfolded transthyretin (TTR) protein from the plasma into tissues as amyloid fibrils, leading to polyneuropathy and cardiomyopathy.
Cardiomyopathy is a major cause of death in both the hereditary form of transthyretin (TTR) amyloidosis and the sporadic late-age-onset transthyretin amyloidosis (ATTR wild-type (ATTR<sub>wt</sub>)).
Assessment of myocardial uptake of Tc-99m-pyrophosphate (Tc-99m PYP) is pivotal in distinguishing transthyretin-associated cardiac amyloidosis (ATTR) from light chain amyloid (AL).
We studied 40 patients with systemic amyloidosis: 10 AL-CMP patients, 20 patients with TTR-associated forms of cardiac amyloidosis, ie, senile systemic amyloidosis (involving wild-type TTR) or mutant TTR, and 10 patients with AL amyloidosis without cardiac involvement.