期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1993
卷号：90
期号：6
页码：2375-2379
DOI：10.1073/pnas.90.6.2375
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Transthyretin (TTR) is thought to play a major role in vitamin A metabolism and thyroid hormone transport in mammals. To investigate the physiological role of the TTR protein in development of the embryo and in the adult, we used gene targeting techniques to generate a null mutation at the mouse ttr locus. The resultant mutant animals are phenotypically normal, viable, and fertile. However, levels of serum retinol, retinol-binding protein, and thyroid hormone are significantly depressed in the mutant animals. These observations demonstrate that the TTR protein maintains normal levels of these metabolites in the circulating plasma.
