{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T01:14:57Z","timestamp":1760058897698,"version":"build-2065373602"},"reference-count":30,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2025,5,8]],"date-time":"2025-05-08T00:00:00Z","timestamp":1746662400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001691","name":"JSPS KAKENHI","doi-asserted-by":"publisher","award":["JP20K18979"],"award-info":[{"award-number":["JP20K18979"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Amyloid deposition has been reported to localize within thrombi; however, its pathological characteristics, particularly its precursor proteins, remain poorly understood. This study aimed to elucidate the pathological features of thrombus-associated amyloid deposition by immunohistochemistry combined with proteomic analyses using liquid chromatography\u2013tandem mass spectrometry with laser microdissection. Our findings revealed that thrombus-associated amyloid deposits within the thrombus and vessel wall primarily comprised apolipoprotein A-I, with a mixture of amyloid fibrils derived from amyloidogenic proteins, including transthyretin and lactoferrin. Given that these proteins are present in the blood, our results support a previous hypothesis that proteins denatured during thrombus aging are a source of amyloid. Furthermore, phagocytes were infiltrated around the intramural and extravascular deposits rather than around the amyloid deposits within the thrombus. Therefore, amyloid deposits generated within the thrombus may be transported from regions with limited blood flow to the vessel wall and surrounding tissues, where blood flow is present, during thrombus processing. These deposits were primarily removed by phagocytic cells. Our results suggest that a facilitative effect on deposition occurs via a cross-seeding mechanism between amyloid fibrils and that phagocytes can remove amyloid deposits. These findings help elucidate the pathogenesis of localized amyloidosis.<\/jats:p>","DOI":"10.3390\/ijms26104505","type":"journal-article","created":{"date-parts":[[2025,5,8]],"date-time":"2025-05-08T11:37:02Z","timestamp":1746704222000},"page":"4505","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Exploring the Histopathological Features of Thrombus-Associated Localized Amyloid Deposition: Comprehensive Analysis Employing Immunohistochemistry and Proteomics"],"prefix":"10.3390","volume":"26","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7305-8137","authenticated-orcid":false,"given":"Shojiro","family":"Ichimata","sequence":"first","affiliation":[{"name":"Department of Legal Medicine, Faculty of Medicine, University of Toyama, Toyama 930-0194, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4323-0557","authenticated-orcid":false,"given":"Tsuneaki","family":"Yoshinaga","sequence":"additional","affiliation":[{"name":"Department of Medicine (Neurology and Rheumatology), Shinshu University School of Medicine, Matsumoto 390-8621, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mitsuto","family":"Sato","sequence":"additional","affiliation":[{"name":"Department of Medicine (Neurology and Rheumatology), Shinshu University School of Medicine, Matsumoto 390-8621, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nagaaki","family":"Katoh","sequence":"additional","affiliation":[{"name":"Department of Medicine (Neurology and Rheumatology), Shinshu University School of Medicine, Matsumoto 390-8621, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9125-7001","authenticated-orcid":false,"given":"Fuyuki","family":"Kametani","sequence":"additional","affiliation":[{"name":"Department of Brain and Neurosciences, Tokyo Metropolitan Institute of Medical Science, Tokyo 156-8506, Japan"},{"name":"Clinical Laboratory Sciences Division, Shinshu University Graduate School of Medicine, Shinshu University, Matsumoto 390-8621, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5520-6530","authenticated-orcid":false,"given":"Masahide","family":"Yazaki","sequence":"additional","affiliation":[{"name":"Clinical Laboratory Sciences Division, Shinshu University Graduate School of Medicine, Shinshu University, Matsumoto 390-8621, Japan"},{"name":"Institute for Biomedical Sciences, Shinshu University, Matsumoto 390-8621, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yoshiki","family":"Sekijim","sequence":"additional","affiliation":[{"name":"Department of Medicine (Neurology and Rheumatology), Shinshu University School of Medicine, Matsumoto 390-8621, Japan"},{"name":"Institute for Biomedical Sciences, Shinshu University, Matsumoto 390-8621, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yukiko","family":"Hata","sequence":"additional","affiliation":[{"name":"Department of Legal Medicine, Faculty of Medicine, University of Toyama, Toyama 930-0194, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6921-1768","authenticated-orcid":false,"given":"Naoki","family":"Nishida","sequence":"additional","affiliation":[{"name":"Department of Legal Medicine, Faculty of Medicine, University of Toyama, Toyama 930-0194, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2025,5,8]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1080\/13506129.2024.2405948","article-title":"Amyloid nomenclature 2024: Update, novel proteins, and recommendations by the International Society of Amyloidosis (ISA) Nomenclature Committee","volume":"31","author":"Buxbaum","year":"2024","journal-title":"Amyloid"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"3918","DOI":"10.1111\/j.1742-4658.2011.08298.x","article-title":"Localized amyloids important in diseases outside the brain--lessons from the islets of Langerhans and the thoracic aorta","volume":"278","author":"Westermark","year":"2011","journal-title":"FEBS J."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"101484","DOI":"10.1016\/j.arr.2021.101484","article-title":"From corpora amylacea to wasteosomes: History and perspectives","volume":"72","author":"Riba","year":"2021","journal-title":"Ageing Res. 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