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A strong phenotypic heterogeneity was demonstrated across coding mutations causing TTR amyloidosis. Non-coding variants affect TTR expression and, consequently, phenotypic presentation in carriers of amyloidogenic mutations.
Serum prealbumin was significantly lower in patients with versus those without post-stroke depression, and was a significant predictor of post-stroke depression after adjusting for confounding risk factors.
TTR induced apoptosis of retinal microvascular endothelial cells in an environment that simulated hypoxia.
Data suggest that transthyretin exhibits site-specific solvation of the indole ring of tryptophans W41 and W79; these studies involved incorporation of tryptophan labeled with fluorine at 5 or 6 positions (5-fluorotryptophan/5FW or 6-fluorotryptophan/6FW) into recombinant TTR; replacement of fluorine at 5-position of a tryptophan with one at adjacent 6-position emphasizes delicate balance of stability in TTR tetramer.
This study shows that highly destabilized, aggregation-prone TTR variants are secreted as both native tetramers and non-native conformations that accumulate as high-molecular-weight oligomers.
The role of transthyretin in normal pregnancy is reviewed.
the role of H88 and the hydrogen bond network in the stability of TTR
we identify a somatic mosaicism, in several subjects affected by familial amyloidotic polyneuropathy, involving the dominant c.325G>C mutation of the TTR gene
The role of Transthyretin in the regulation of Ubc9 (zeige UBE2I Proteine) SUMOylation
Gene sequencing revealed a phenylalanine-->isoleucine mutation in the 33rd position of exon 2 of TTR in 1 patient of 1 pedigree, confirming the diagnosis of FAP. Two patients subsequently were found to have sensorimotor autonomic neuropathy, whereas 2 others had subclinical autonomic dysfunction.
New insights into ghrelin (zeige GHRL Proteine) cell physiology, and given the known functions of RBP4 (zeige RBP4 Proteine) and TTR, support an emerging role for the ghrelin (zeige GHRL Proteine) cell in blood glucose handling and metabolism.
Transthyretin (TTR) deposition in the peripheral nervous system is the hallmark of familial amyloidotic polyneuropathy (FAP (zeige FAP Proteine)).
TTR mediated transport of thyroxine represents a survival mechanism necessary for the myogenic program.
provide evidence of a new role of Transthyretin as a transcription inducer of insulin (zeige INS Proteine)-like growth factor receptor (zeige RYK Proteine) I in central nervous system, unveiling a new role in neuroprotection
data also indicate that it is unlikely that the behaviors seen in Ttr(-/-) mice are related to its function
Native transthyretin inhibits all preeclampsia-like features in the humanized mouse model.
Transthyretin silencing (TTRkd) significantly reduced myogenin (zeige MYOG Proteine) expression.
Amyloid fibrils formed by a mutant form of TTR, A25T, activate microglia, leading to the secretion of tumor necrosis factor-alpha (TNF-alpha (zeige TNF Proteine)), interleukin-6 (IL-6 (zeige IL6 Proteine)) and nitric oxide.
Hsf-1 (zeige HSF1 Proteine) affects podocyte markers NPHS1 (zeige NPHS1 Proteine), NPHS2 and WT1 (zeige WT1 Proteine) in a transgenic mouse model of TTRVal30Met-related amyloidosis.
Fibroblasts endocytose and degrade transthyretin aggregates in transthyretin-related amyloidosis.
The rank order potency of the chemicals tested for the displacement of [125I]TIP from TTR was TIP > ioxynil > pentachlorophenol, T4, and retinoic acid > tetrabromobisphenol A, diethylstilbestrol, and T3.
This study suggested closer links between the release of haptoglobin (zeige HP Proteine), Pig-MAP and monocytes compared to the release of AGP, SAA (zeige SAA1 Proteine) and transthyretin.
Study determined the genomic structure of the Xenopus laevis TTR gene including 5'-flanking regions, and examined TTR expression patterns in several tissues; coding regions of xTTR gene was separated into 4 exons by 3 introns and these numbers were in agreement with those determined for the human, mouse, and rat genes
This gene encodes transthyretin, one of the three prealbumins including alpha-1-antitrypsin, transthyretin and orosomucoid. Transthyretin is a carrier protein\; it transports thyroid hormones in the plasma and cerebrospinal fluid, and also transports retinol (vitamin A) in the plasma. The protein consists of a tetramer of identical subunits. More than 80 different mutations in this gene have been reported\; most mutations are related to amyloid deposition, affecting predominantly peripheral nerve and/or the heart, and a small portion of the gene mutations is non-amyloidogenic. The diseases caused by mutations include amyloidotic polyneuropathy, euthyroid hyperthyroxinaemia, amyloidotic vitreous opacities, cardiomyopathy, oculoleptomeningeal amyloidosis, meningocerebrovascular amyloidosis, carpal tunnel syndrome, etc.
, transthyretin (prealbumin, amyloidosis type I)
, transthyretin (prealbumin, amyloidosis type 1)
, carpal tunnel syndrome 1
, prealbumin, amyloidosis type I
, thyroxine-binding prealbumin