Chromium(III) ion and thyroxine cooperate to stabilize the transthyretin tetramer and suppress in vitro amyloid fibril formation

Takashi Sato; Yukio Ando; Seiko Susuki; Fumi Mikami; Shinji Ikemizu; Masaaki Nakamura; Ole Suhr; Makoto Anraku; Toshiya Kai; Mary Ann Suico; Tsuyoshi Shuto; Mineyuki Mizuguchi; Yuriko Yamagata; Hirofumi Kai

doi:10.1016/j.febslet.2005.12.047

Chromium(III) ion and thyroxine cooperate to stabilize the transthyretin tetramer and suppress in vitro amyloid fibril formation

Takashi Sato, Yukio Ando, Seiko Susuki, Fumi Mikami, Shinji Ikemizu, Masaaki Nakamura, Ole Suhr, Makoto Anraku, Toshiya Kai, Mary Ann Suico, Tsuyoshi Shuto, Mineyuki Mizuguchi, Yuriko Yamagata, Hirofumi Kai^*

^*Corresponding author for this work

Structural Biology

Research output: Contribution to journal › Article › peer-review

23 Scopus citations

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.

Original language	English
Pages (from-to)	491-496
Number of pages	6
Journal	FEBS Letters
Volume	580
Issue number	2
DOIs	https://doi.org/10.1016/j.febslet.2005.12.047
State	Published - 2006/01/23

Keywords

Amyloid
Cr
Familial amyloidotic polyneuropathy
Thyroxine
Transthyretin

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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Sato, T., Ando, Y., Susuki, S., Mikami, F., Ikemizu, S., Nakamura, M., Suhr, O., Anraku, M., Kai, T., Suico, M. A., Shuto, T., Mizuguchi, M., Yamagata, Y., & Kai, H. (2006). Chromium(III) ion and thyroxine cooperate to stabilize the transthyretin tetramer and suppress in vitro amyloid fibril formation. FEBS Letters, 580(2), 491-496. https://doi.org/10.1016/j.febslet.2005.12.047

@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.",

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Sato, T, Ando, Y, Susuki, S, Mikami, F, Ikemizu, S, Nakamura, M, Suhr, O, Anraku, M, Kai, T, Suico, MA, Shuto, T, Mizuguchi, M, Yamagata, Y & Kai, H 2006, 'Chromium(III) ion and thyroxine cooperate to stabilize the transthyretin tetramer and suppress in vitro amyloid fibril formation', FEBS Letters, vol. 580, no. 2, pp. 491-496. https://doi.org/10.1016/j.febslet.2005.12.047

TY - JOUR

T1 - Chromium(III) ion and thyroxine cooperate to stabilize the transthyretin tetramer and suppress in vitro amyloid fibril formation

AU - Sato, Takashi

AU - Ando, Yukio

AU - Susuki, Seiko

AU - Mikami, Fumi

AU - Ikemizu, Shinji

AU - Nakamura, Masaaki

AU - Suhr, Ole

AU - Anraku, Makoto

AU - Kai, Toshiya

AU - Suico, Mary Ann

AU - Shuto, Tsuyoshi

AU - Mizuguchi, Mineyuki

AU - Yamagata, Yuriko

AU - Kai, Hirofumi

N1 - Funding Information: The authors’ 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.

PY - 2006/1/23

Y1 - 2006/1/23

N2 - 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.

AB - 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.

KW - Amyloid

KW - Cr

KW - Familial amyloidotic polyneuropathy

KW - Thyroxine

KW - Transthyretin

UR - http://www.scopus.com/inward/record.url?scp=30644472492&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2005.12.047

DO - 10.1016/j.febslet.2005.12.047

M3 - 学術論文

C2 - 16386248

AN - SCOPUS:30644472492

SN - 0014-5793

VL - 580

SP - 491

EP - 496

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

Chromium(III) ion and thyroxine cooperate to stabilize the transthyretin tetramer and suppress in vitro amyloid fibril formation

Abstract

Keywords

ASJC Scopus subject areas

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