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 (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.
authors.affiliation: Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto 862-0973, Japan.
authors.forename: Takashi
authors.initials: T
authors.lastname: Sato
authors.forename: Yukio
authors.initials: Y
authors.lastname: Ando
authors.forename: Seiko
authors.initials: S
authors.lastname: Susuki
authors.forename: Fumi
authors.initials: F
authors.lastname: Mikami
authors.forename: Shinji
authors.initials: S
authors.lastname: Ikemizu
authors.forename: Masaaki
authors.initials: M
authors.lastname: Nakamura
authors.forename: Ole
authors.initials: O
authors.lastname: Suhr
authors.forename: Makoto
authors.initials: M
authors.lastname: Anraku
authors.forename: Toshiya
authors.initials: T
authors.lastname: Kai
authors.forename: Mary Ann
authors.initials: MA
authors.lastname: Suico
authors.forename: Tsuyoshi
authors.initials: T
authors.lastname: Shuto
authors.forename: Mineyuki
authors.initials: M
authors.lastname: Mizuguchi
authors.forename: Yuriko
authors.initials: Y
authors.lastname: Yamagata
authors.forename: Hirofumi
authors.initials: H
authors.lastname: Kai
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000378:metabolism*; D002857:Chromium / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D017354:Point Mutation; D011228:Prealbumin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D013974:Thyroxine / Q000378:metabolism*
chemical_list: D000682:Amyloid; D011228:Prealbumin; D002857:Chromium; D013974:Thyroxine