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

Autor: Iino T; Division of Cardiovascular Medicine, Kobe University Graduate School of Medicine, Kobe, Japan.; Central Research Laboratories, Sysmex Corporation, Kobe, Japan., Nagao M; Division of Evidence-Based Laboratory Medicine, Kobe University Graduate School of Medicine, 7-5-1 Kusunoki-Cho, Chuo-Ku, Kobe, 650-0017, Japan. mnagao@med.kobe-u.ac.jp., Tanaka H; Division of Cardiovascular Medicine, Kobe University Graduate School of Medicine, Kobe, Japan., Yoshikawa S; Division of Cardiovascular Medicine, Kobe University Graduate School of Medicine, Kobe, Japan., Asakura J; Division of Cardiovascular Medicine, Kobe University Graduate School of Medicine, Kobe, Japan., Nishimori M; Division of Molecular Epidemiology, Kobe University Graduate School of Medicine, Kobe, Japan., Shinohara M; Division of Molecular Epidemiology, Kobe University Graduate School of Medicine, Kobe, Japan.; The Integrated Center for Mass Spectrometry, Kobe University Graduate School of Medicine, Kobe, Japan., Harada A; Central Research Laboratories, Sysmex Corporation, Kobe, Japan., Watanabe S; Bio-Diagnostic Reagent Technology Center, Sysmex Corporation, Kobe, Japan., Ishida T; Division of Cardiovascular Medicine, Kobe University Graduate School of Medicine, Kobe, Japan.; Division of Nursing Practice, Kobe University Graduate School of Health Sciences, Kobe, Japan., Hirata KI; Division of Cardiovascular Medicine, Kobe University Graduate School of Medicine, Kobe, Japan.; Division of Evidence-Based Laboratory Medicine, Kobe University Graduate School of Medicine, 7-5-1 Kusunoki-Cho, Chuo-Ku, Kobe, 650-0017, Japan., Toh R; Division of Evidence-Based Laboratory Medicine, Kobe University Graduate School of Medicine, 7-5-1 Kusunoki-Cho, Chuo-Ku, Kobe, 650-0017, Japan.
Jazyk: angličtina
Zdroj: Scientific reports [Sci Rep] 2024 Sep 03; Vol. 14 (1), pp. 20508. Date of Electronic Publication: 2024 Sep 03.
DOI: 10.1038/s41598-024-71446-8
Abstrakt: 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.
(© 2024. The Author(s).)
Databáze: MEDLINE
Externí odkaz:
Nepřihlášeným uživatelům se plný text nezobrazuje