Buxbaum Joel N, Reixach Natàlia
Molecular and Experimental Medicine Department, The Scripps Research Institute, La Jolla, CA 92037, USA.
Cell Mol Life Sci. 2009 Oct;66(19):3095-101. doi: 10.1007/s00018-009-0109-0. Epub 2009 Jul 31.
Transthyretin (TTR) (formerly, thyroxine binding prealbumin) is an evolutionarily conserved serum and cerebrospinal fluid protein that transports holo-retinol-binding protein and thyroxine. Its serum concentration has been widely used to assess clinical nutritional status. It is also well known that wild-type transthyretin and approximately 100 different mutants give rise to a variety of forms of systemic amyloid deposition. It has been suspected and recently established that TTR can suppress the Alzheimer's disease phenotype in transgenic animal models of cerebral Abeta deposition. Thus, while TTR is a systemic amyloid precursor, in the brain it seems to have an anti-amyloidogenic effect. TTR is found in other organs as a result of local synthesis or transport, suggesting that it may have other, as yet undiscovered, functions. It is possible that its capacity to bind many classes of compounds allows it to serve as an endogenous detoxifier of molecules with potential pathologic effects.
转甲状腺素蛋白（TTR）（以前称为甲状腺素结合前白蛋白）是一种在进化上保守的血清和脑脊液蛋白，可转运全反式视黄醇结合蛋白和甲状腺素。其血清浓度已被广泛用于评估临床营养状况。众所周知，野生型转甲状腺素蛋白和大约100种不同的突变体可导致多种形式的系统性淀粉样蛋白沉积。有人怀疑并最近证实，在脑β淀粉样蛋白沉积的转基因动物模型中，TTR可以抑制阿尔茨海默病表型。因此，虽然TTR是一种系统性淀粉样蛋白前体，但在大脑中它似乎具有抗淀粉样蛋白生成的作用。由于局部合成或转运，TTR在其他器官中也有发现，这表明它可能还有其他尚未被发现的功能。它结合多种化合物的能力可能使其能够作为具有潜在病理作用的分子的内源性解毒剂。
