Abstract
Transthyretin (TTR) is a protein containing 20-40mg/dl in plasma with a half life of 1.9 days. TTR is detected in cerebrospinal fluid with high concentration, and plays important roles in the pathogenesis of brain disorders, such as Alzheimer disease, schizophrenia, and lead intoxication. TTR functions as a tetramerer binding with retinol binding protein (RBP) and T4. Because TTR is a Trp rich protein, it becomes a good maker for evaluating nutritional state in the acute phase of diseases. However, the protein is an antiacute phase protein and plasma concentration is decreased by infection and inflammation. Since TTR is β-sheet rich protein, it is prone to form amyloid fibrils both in vitro and in vivo. It can become the precursor protein of familial amyloidotic polyneuropathy (FAP) and senile systemic amyloidosis (SSA). Because TTR is predominantly synthesized by the liver, liver transplantation is a common therapy for FAP. Recently, it has been well documented that TTR plays important roles in diabetes merits, lipid metabolism disorders as well as cerebral disorders.
