[Transthyretin: it's miracle function and pathogenesis].
Transthyretin (TTR) was previously called prealbumin because the band it formed on agarose gel electrophoresis at pH 8.6 was at the prealbumin position. However, it has been well documented that TTR of rodents does not show a prealbumin position on electrophoresis. Now, its name describes its function, binding to retinol binding protein (RBP) and T4. The serum concentration of the protein is 20-40 mg/dl, and TTR forms a tetramer. The plasma half life of the protein is 1.9 days. TTR is synthesized by the liver, retina, pancreas, and choroid plexus. In cerebro-spinal fluid (CSF), it is the second most abundant protein, and is considered as an important protein in the pathogenesis of Alzheimer's disease, depression, and lead intoxication. In addition, TTR is a tryptophan-rich protein, it is used as one of the nutrition assessment proteins, it acts as an anti acute phase protein, and its plasma concentration decreases during inflammation and bacterial infection. Since TTR is a highly amyloidogenic protein because it contains a beta-sheet structure, it becomes a precursor protein in familial amyloidotic polyneuropathy(FAP). Moreover, TTR plays important roles in various CNS disorders, diabetes melitus, and lipid metabolism.
Department of Diagnostic Medicine, Graduate School of Medical Sciences, Kumamoto University, Kumamoto 860-8556, Japan. andoy709@kumamoto-u.ac.jp
Yukio
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Ando
D000544:Alzheimer Disease / Q000209:etiology*; D028227:Amyloid Neuropathies, Familial / Q000209:etiology*; D000818:Animals; D014408:Biomarkers, Tumor; D002831:Choroid Plexus / Q000378:metabolism; D006801:Humans; D050356:Lipid Metabolism; D011228:Prealbumin / Q000096:biosynthesis / Q000737:chemistry / Q000502:physiology; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012177:Retinol-Binding Proteins; D013974:Thyroxine
D014408:Biomarkers, Tumor; D011228:Prealbumin; D012177:Retinol-Binding Proteins; D013974:Thyroxine