Assessment of transthyretin instability in patients with wild-type transthyretin amyloid cardiomyopathy

被引：0
|
作者：
Iino, Takuya [1 ,2 ]
Nagao, Manabu [3 ]
Tanaka, Hidekazu [1 ]
Yoshikawa, Sachiko [1 ]
Asakura, Junko [1 ]
Nishimori, Makoto [4 ]
Shinohara, Masakazu [4 ,5 ]
Harada, Amane [2 ]
Watanabe, Shunsuke [6 ]
Ishida, Tatsuro [1 ,7 ]
Hirata, Ken-ichi [1 ,3 ]
Toh, Ryuji [3 ]
机构：
[1] Kobe Univ, Grad Sch Med, Div Cardiovasc Med, Kobe, Japan
[2] Sysmex Corp, Cent Res Labs, Kobe, Japan
[3] Kobe Univ, Grad Sch Med, Div Evidence Based Lab Med, 7-5-1 Kusunoki Cho,Chuo Ku, Kobe 6500017, Japan
[4] Kobe Univ, Grad Sch Med, Div Mol Epidemiol, Kobe, Japan
[5] Kobe Univ, Grad Sch Med, Integrated Ctr Mass Spectrometry, Kobe, Japan
[6] Sysmex Corp, Biodiagnost Reagent Technol Ctr, Kobe, Japan
[7] Kobe Univ, Grad Sch Hlth Sci, Div Nursing Practice, Kobe, Japan
来源：
SCIENTIFIC REPORTS | 2024年 / 14卷 / 01期
关键词：
Transthyretin; Wild-type transthyretin amyloid cardiomyopathy; Heart failure; Heart failure with preserved ejection fraction; Aging; HEART-FAILURE; CARDIAC AMYLOIDOSIS; PLASMA; QUANTIFICATION; DENATURATION; FIBRIL;
D O I：
10.1038/s41598-024-71446-8
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
The pathophysiology of variant transthyretin (TTR) amyloidosis (ATTRv) is associated with destabilizing mutations in the TTR tetramer. However, why TTR with a wild-type genetic sequence misfolds and aggregates in wild-type transthyretin amyloidosis (ATTRwt) is unknown. Here, we evaluate kinetic TTR stability with a newly developed ELISA system in combination with urea-induced protein denaturation. Compared with that in control patients, endogenous TTR in patients with wild-type transthyretin amyloid cardiomyopathy (ATTRwt-CM) exhibited thermodynamic instability, indicating that circulating TTR instability may be associated with the pathogenesis of ATTRwt as well as ATTRv. Our findings provide new insight into the underlying mechanisms of ATTRwt.
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页数：9
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