@article{3b9c59e34c9947038d61fe1d5983dd23,
title = "Chromium(III) ion and thyroxine cooperate to stabilize the transthyretin tetramer and suppress in vitro amyloid fibril formation",
abstract = "Transthyretin (TTR) amyloid fibril formation, which is triggered by the dissociation of tetrameric TTR, appears to be the causative factor in familial amyloidotic polyneuropathy and senile systemic amyloidosis. Binding of thyroxine (T4), a native ligand of TTR, stabilizes the tetramer, but the bioavailability of T4 for TTR binding is limited due to the preferential binding of T4 to globulin, the major T4 carrier in plasma. Here, we show that Cr3+ increased the T 4-binding capacity of wild-type (WT) and amyloidogenic V30M-TTR. Moreover, we demonstrate that Cr3+ and T4 cooperatively suppressed in vitro fibril formation due to the stabilization of WT-TTR and V30M-TTR.",
keywords = "Amyloid, Cr, Familial amyloidotic polyneuropathy, Thyroxine, Transthyretin",
author = "Takashi Sato and Yukio Ando and Seiko Susuki and Fumi Mikami and Shinji Ikemizu and Masaaki Nakamura and Ole Suhr and Makoto Anraku and Toshiya Kai and Suico, {Mary Ann} and Tsuyoshi Shuto and Mineyuki Mizuguchi and Yuriko Yamagata and Hirofumi Kai",
note = "Funding Information: The authors{\textquoteright} work was supported by grants from the Amyloidosis Research Committee, the Pathogenesis and Therapy of Hereditary Neuropathy Research Committee, Surveys and Research on Specific Diseases, the Ministry of Health and Welfare of Japan, the Charitable Trust Clinical Pathology Research Foundation of Japan, and Grants-in-Aid for Scientific Research from the Ministry of Education, Science, Sports and Culture of Japan.",
year = "2006",
month = jan,
day = "23",
doi = "10.1016/j.febslet.2005.12.047",
language = "英語",
volume = "580",
pages = "491--496",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "John Wiley and Sons Inc.",
number = "2",
}