Elucidation of the mechanism of amyloid A and transthyretin formation using mass spectrometry-based absolute quantification.

ABSTRACT: Amyloidosis is triggered by the truncation of amyloid precursor proteins, causing organ damages. While previous studies found the truncation of amyloid A (AA) and amyloid transthyretin (ATTR) occurs in C- and N-terminal, respectively, the detailed mechanism of the fibril formation remains unclear. Liquid chromatography mass spectrometry is usually applied for a qualitative purpose, and thus quantification of tryptic peptide residue is difficult. We therefore employed a mass spectrometry-based quantification by isotope-labeled cell-free (MS-QBIC) to analyze the truncation processes in amyloid fibrillogenesis of AA and ATTR using the formalin-fixed paraffin-embedded tissues of autopsy cases. In this study, the process of transthyretin from an 'early fibril state' consisting of full-length AT

SUBMITTER: Shintani-Domoto Y 

PROVIDER: S-EPMC11564350 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature