{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,31]],"date-time":"2025-12-31T00:27:20Z","timestamp":1767140840036,"version":"build-2238731810"},"reference-count":9,"publisher":"Springer Science and Business Media LLC","issue":"5","license":[{"start":{"date-parts":[[2023,7,15]],"date-time":"2023-07-15T00:00:00Z","timestamp":1689379200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2023,7,15]],"date-time":"2023-07-15T00:00:00Z","timestamp":1689379200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100001691","name":"KAKENHI","doi-asserted-by":"crossref","award":["17K08717"],"award-info":[{"award-number":["17K08717"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100001691","name":"KAKENHI","doi-asserted-by":"crossref","award":["20K07389"],"award-info":[{"award-number":["20K07389"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Virchows Arch"],"published-print":{"date-parts":[[2024,11]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>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.\u00a0Liquid 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 ATTR to a 'mature ATTR amyloid fibril' with a truncated low-amyloidogenic segment has been mathematically revealed. The amount of full-length ATTR was nine times higher than in mature fibers. Large cohort studies using MS-QBIC may shed light on the clinical significance of amyloid fibrils.<\/jats:p>","DOI":"10.1007\/s00428-023-03591-w","type":"journal-article","created":{"date-parts":[[2023,7,15]],"date-time":"2023-07-15T02:01:32Z","timestamp":1689386492000},"page":"943-946","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Elucidation of the mechanism of amyloid A and transthyretin formation using mass spectrometry-based absolute quantification"],"prefix":"10.1007","volume":"485","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8061-6176","authenticated-orcid":false,"given":"Yukako","family":"Shintani-Domoto","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Koji L.","family":"Ode","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Seitaro","family":"Nomura","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hiroyuki","family":"Abe","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hiroki R.","family":"Ueda","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Takashi","family":"Sakatani","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ryuji","family":"Ohashi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2023,7,15]]},"reference":[{"key":"3591_CR1","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1080\/13506129.2022.2147636","volume":"29","author":"JN Buxbaum","year":"2022","unstructured":"Buxbaum JN, Dispenzieri A, Eisenberg DS et al (2022) Amyloid nomenclature 2022: update, novel proteins, and recommendations by the International Society of Amyloidosis (ISA) Nomenclature Committee. 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Amyloid 26:164\u2013170. https:\/\/doi.org\/10.1080\/13506129.2019.1628015","journal-title":"Amyloid"},{"key":"3591_CR6","doi-asserted-by":"publisher","first-page":"e0275993","DOI":"10.1371\/journal.pone.0275993","volume":"17","author":"Y Shintani-Domoto","year":"2022","unstructured":"Shintani-Domoto Y, Sugiura Y, Ogawa M et al (2022) N-terminal peptide fragment constitutes core of amyloid deposition of serum amyloid A: An imaging mass spectrometry study. PLoS One 17:e0275993. https:\/\/doi.org\/10.1371\/journal.pone.0275993","journal-title":"PLoS One"},{"key":"3591_CR7","doi-asserted-by":"publisher","first-page":"5008","DOI":"10.1038\/s41467-019-13038-z","volume":"10","author":"M Schmidt","year":"2019","unstructured":"Schmidt M, Wiese S, Adak V et al (2019) Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis. 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Informed consent for the use of patient specimens for.the research was obtained from the responsible parties.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Informed consent"}},{"value":"H.R.U conducted a collaborative research project with Thermo Fisher Scientific Inc. The authors have no conflicts of interest to declare.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}}]}}