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Chromium(III) ion and thyroxine cooperate to stabilize the transthyretin tetramer and suppress in vitro amyloid fibril formation
Author(s) -
Sato Takashi,
Ando Yukio,
Susuki Seiko,
Mikami Fumi,
Ikemizu Shinji,
Nakamura Masaaki,
Suhr Ole,
Anraku Makoto,
Kai Toshiya,
Suico Mary Ann,
Shuto Tsuyoshi,
Mizuguchi Mineyuki,
Yamagata Yuriko,
Kai Hirofumi
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.12.047
Subject(s) - transthyretin , tetramer , chemistry , amyloidosis , in vitro , amyloid (mycology) , fibril , amyloid fibril , ligand (biochemistry) , biophysics , biochemistry , endocrinology , medicine , amyloid β , receptor , biology , inorganic chemistry , disease , enzyme
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 (T 4 ), a native ligand of TTR, stabilizes the tetramer, but the bioavailability of T 4 for TTR binding is limited due to the preferential binding of T 4 to globulin, the major T 4 carrier in plasma. Here, we show that Cr 3+ increased the T 4 ‐binding capacity of wild‐type (WT) and amyloidogenic V30M‐TTR. Moreover, we demonstrate that Cr 3+ and T 4 cooperatively suppressed in vitro fibril formation due to the stabilization of WT‐TTR and V30M‐TTR.