Different NT-proBNP circulating levels for different types of cardiac amyloidosis.
Florence, Italy. In J Cardiovasc Med (hagerstown), Feb 2016
AIM: Several studies suggest that the N-terminal fragment of pro-brain natriuretic peptide levels are quite different in wild-type transthyretin (TTR)-related amyloidosis (ATTRwt) and mutated TTR-related amyloidosis (ATTRm) compared with immunoglobulin light-chain cardiac amyloidosis.
London, United Kingdom. In Lancet, Jan 2016
Systemic light chain (AL) amyloidosis is the most common of these conditions, but wild-type transthyretin cardiac amyloidosis (ATTRwt) is increasingly being diagnosed.
"Red-flag" symptom clusters in transthyretin familial amyloid polyneuropathy.
Lisbon, Portugal. In J Peripher Nerv Syst, Jan 2016
BACKGROUND: Transthyretin familial amyloid polyneuropathy (TTR-FAP) is a rare, progressive, life-threatening, hereditary disorder caused by mutations in the transthyretin gene and characterized by extracellular deposition of transthyretin-derived amyloid fibrils in peripheral and autonomic nerves, heart, and other organs.
The amyloidogenic V122I transthyretin variant in elderly black Americans.
Houston, United States. In N Engl J Med, 2015
METHODS: We determined genotype status for the transthyretin gene (TTR) in 3856 black participants in the Atherosclerosis Risk in Communities study and assessed clinical profiles, mortality, and the risk of incident heart failure in V122I TTR variant carriers (124 participants [3%]) versus noncarriers (3732 participants).
Genetic profile of hypertrophic cardiomyopathy in Tunisia: Is it different?
Monastir, Tunisia. In Glob Cardiol Sci Pract, 2014
Using the Illumina platform, a panel of 12 genes was analyzed including myosin binding protein C (MYBPC3), beta-myosin heavy chain (MYH7), regulatory and essential light chains (MYL2 and MYL3), troponin-T (TNNT2), troponin-I (TNNI3), troponin-C (TNNC1), alpha-tropomyosin (TPM1), alpha-actin (ACTC1), alpha-actinin-2 (ACTN2) as well as alfa-galactosidase (GLA), 5'-AMP-activated protein (PKRAG2), transthyretin (TTR) and lysosomal-associated membrane protein-2 (LAMP2) for exclusion of phenocopies.
Amyloid fibrils nucleated and organized by DNA origami constructions.
New York City, United States. In Nat Nanotechnol, 2014
The fibrils are built by modifying the synthetic peptide fragment corresponding to residues 105-115 of the amyloidogenic protein transthyretin and a DNA origami construct is used to form 20-helix DNA nanotubes with sufficient space for the fibrils inside.