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Global longitudinal strain in pre-symptomatic patients with mutation for transthyretin amyloidosis.
Orphanet J Rare Dis
December 2024
Department of Advanced Biomedical Sciences, University Federico II of Naples, Naples, Italy.
Background: Hereditary transthyretin (ATTRv) amyloidosis is rare, autosomal dominant disease with a fatal outcome if left untreated. Early stages detection is crucial for intervention. We aimed identifying early indexes of cardiac involvement and their eventual correlation with neurological indexes, in pre-symptomatic subjects with TTR gene mutation.
View Article and Find Full Text PDFA phenotypic comparison of the Romanian and French ATTRv cohorts: Glu54Gln founder pathogenic variant vs the most common variants in Western Europe.
Int J Cardiol
January 2025
French Referral Centre for Cardiac Amyloidosis, GRC Amyloid Research Institute, Amyloidosis Mondor Network, Henri-Mondor Teaching Hospital, AP-HP, Creteil, France; Cardiology Department, Henri-Mondor Teaching Hospital, Creteil, France; Clinical Epidemiology and Ageing (CEpiA) Geriatrics, Primary Care and Public Health, Creteil, France; Université Paris Est Creteil, INSERM, IMRB, Creteil, France.
Aim And Methods: We conducted a retrospective observational study of the ATTRv heterozygous mutation frequency, phenotype, and all-cause mortality at two cardiac amyloidosis centers in Romania and France.
Results: 291 patients were included: 26 Glu54Gln (all Romanian), 200 Val122Ile, 47 Val30Met and 18 Ser77Tyr. On diagnosis, Gu54Gln patients were younger than Val122Ile or late-onset Val30Met (median age: 46 [42-50], 76 [71-80] and 70 [61-76], respectively; p < 0.
Arginine: A potential prophylactic supplement for transthyretin amyloidosis.
Biochem Biophys Res Commun
December 2024
Department of Amyloidosis Research, Faculty of Pharmaceutical Sciences, Nagasaki International University, Huis Ten Bosch, Sasebo, Nagasaki, Japan; Department of Amyloidosis Supporting Center, Sugimura Hospital, Honjo, Chuo-ku, Kumamoto, Japan. Electronic address:
Transthyretin (TTR) is an amyloidogenic protein associated with TTR amyloidosis (ATTR). Dissociation of TTR tetramers into TTR monomers causes TTR misfolding, resulting in amyloid fibril formation and triggering the onset of ATTR. Low-molecular-weight tetrameric TTR stabilizers are potential therapeutic agents to delay ATTR progression.
View Article and Find Full Text PDFHereditary Transthyretin Amyloidosis (hATTR) with Polyneuropathy Clusters Are Located in Ancient Mining Districts: A Possible Geochemical Origin of the Disease.
Biomolecules
June 2024
Chemistry Section, Stockholm University, 10691 Stockholm, Sweden.
Hereditary transthyretin amyloidosis (hATTR) with polyneuropathy (formerly known as Familial Amyloid Polyneuropathy (FAP)) is an endemic amyloidosis involving the harmful aggregation of proteins, most commonly transthyretin (TTR) but sometimes also apolipoprotein A-1 or gelsolin. hATTR appears to be transmitted as an autosomal dominant trait. Over 100 point mutations have been identified, with the Val30Met substitution being the most common.
View Article and Find Full Text PDFAmyloid Neuropathy: From Pathophysiology to Treatment in Light-Chain Amyloidosis and Hereditary Transthyretin Amyloidosis.
Ann Neurol
September 2024
Department of Medicine, Division of Cardiology, Vanderbilt University Medical Center, Nashville, TN, USA.
Amyloid neuropathy is caused by deposition of insoluble β-pleated amyloid sheets in the peripheral nervous system. It is most common in: (1) light-chain amyloidosis, a clonal non-proliferative plasma cell disorder in which fragments of immunoglobulin, light or heavy chain, deposit in tissues, and (2) hereditary transthyretin (ATTRv) amyloidosis, a disorder caused by autosomal dominant mutations in the TTR gene resulting in mutated protein that has a higher tendency to misfold. Amyloid fibrils deposit in the endoneurium of peripheral nerves, often extensive in the dorsal root ganglia and sympathetic ganglia, leading to atrophy of Schwann cells in proximity to amyloid fibrils and blood-nerve barrier disruption.
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