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Hereditäre Transthyretin-Amyloidosen
Der Nervenarzt, 2014Hereditary amyloidosis is an autosomal dominant fatal multisystem disease caused by extracellular deposition of misfolded proteins and, therefore represents a hereditary protein folding or deposition disease that leads to progressive organ damage and eventually death.
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Transthyretin Mass Determination for Detection of Transthyretin Familial Amyloid
2009The concentration range of plasma proteins exceeds the dynamic range of any single analytical method. It has been estimated that the concentration range of serum proteins exceeds ten orders of magnitude (1). Because of this, prior immunoselection of even abundant proteins facilitates the relative nonquantitative observations required to show structural
John F. O'Brien, H. Robert Bergen
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Transthyretin and the Transthyretin Amyloidoses
2007Transthyretin is a normal serum protein that carries the secondary thyroid hormone thyroxine and retinol binding protein when it is loaded with retinol. It is synthesized primarily in the liver but there is also significant production in the choroid plexus and the retina. Both message and protein are found in the kidney but that site does not appear to
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Monoclonal antibodies to transthyretin
Scandinavian Journal of Clinical and Laboratory Investigation, 1986Monoclonal antibodies (mabs) have been raised against human transthyretin (hTTR). The protein was isolated by an affinity chromatography procedure using Sepharose-hRBP and BALB/c mice were immunized. Following fusion with SP 2/0 myeloma cells, 26 single cell clones producing antibodies against hTTR were isolated.
Tom Pettersson +3 more
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Cardiac transthyretin amyloidosis
Heart, 2012Cardiac amyloidosis of transthyretin fibril protein (ATTR) type is an infiltrative cardiomyopathy characterised by ventricular wall thickening and diastolic heart failure. Increased access to cardiovascular magnetic resonance imaging has led to a marked increase in referrals to our centre of Caucasian patients with wild-type ATTR (senile systemic ...
Jason Dungu +3 more
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Pathogenesis of transthyretin amyloidosis
Amyloid, 2012Current dogma for transthyretin (TTR) pathogenesis is that mutations in TTR alter its structure such that the tetramer becomes unstable and prone to release of monomer which then becomes the putative building block of the fibril. This hypothesis is supported by thermodynamic data showing decreased stability of mutant TTR tetrameric proteins and ...
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Tafamidis: A First-in-Class Transthyretin Stabilizer for Transthyretin Amyloid Cardiomyopathy
Annals of Pharmacotherapy, 2019Objective: To review the pharmacology, efficacy, and safety of the selective transthyretin inhibitor tafamidis for transthyretin amyloid cardiomyopathy (ATTR-CM). Data Sources: A PubMed (1966 to October 2019) and ClinicalTrials. gov search was conducted using the keywords tafamidis, Fx-1006A, Vyndaqel, and Vyndamax.
Jonathan Park +5 more
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Localization of transthyretin-mRNA and of immunoreactive transthyretin in the human fetus
Virchows Archiv A Pathological Anatomy and Histopathology, 1989Five human fetuses at mid-term (16-20 weeks) and one with a gestational age of 8 weeks were investigated. The cellular localization of transthyretin (TTR)-mRNA in different organs was demonstrated by in situ hybridization with a 35S-labelled, single-stranded RNA probe. Immunoreactive TTR (TTR-IR) was localized with a monoclonal antibody to TTR.
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Tafamidis for transthyretin amyloidosis
Drugs of Today, 2012Tafamidis meglumine (Vyndaqel®, Pfizer) is a novel, first-in-class drug for the treatment of transthyretin familial amyloid polyneuropathy (TTR-FAP), a rare neurodegenerative disorder characterized by progressive sensory, motor and autonomic impairment that is ultimately fatal.
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