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Amyloid fibril composition type is consistent over time in patients with Val30Met (p. Val50Met) transthyretin amyloidosis
Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM). Umeå universitet, Medicinska fakulteten, Institutionen för folkhälsa och klinisk medicin, Avdelningen för medicin.ORCID-id: 0000-0003-2874-7643
Umeå universitet, Medicinska fakulteten, Institutionen för folkhälsa och klinisk medicin, Avdelningen för medicin.ORCID-id: 0000-0002-1175-2369
Department of Medicine, Piteå Hospital, Piteå, Sweden.
Department of Medicine, Piteå Hospital, Piteå, Sweden.
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2022 (engelsk)Inngår i: PLOS ONE, E-ISSN 1932-6203, Vol. 17, nr 3, artikkel-id e0266092Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Background: We have previously shown that transthyretin (TTR) amyloidosis patients have amyloid fibrils of either of two compositions; type A fibrils consisting of large amounts of C-terminal TTR fragments in addition to full-length TTR, or type B fibrils consisting of only full-length TTR. Since type A fibrils are associated with an older age in ATTRVal30Met (p.Val50Met) amyloidosis patients, it has been discussed if the TTR fragments are derived from degradation of the amyloid deposits as the patients are aging. The present study aimed to investigate if the fibril composition type changes over time, especially if type B fibrils can shift to type A fibrils as the disease progresses.

Material and methods: Abdominal adipose tissue biopsies from 29 Swedish ATTRVal30Met amyloidosis patients were investigated. The fibril type in the patients initial biopsy taken for diagnostic purposes was compared to a biopsy taken several years later (ranging between 2 and 13 years). The fibril composition type was determined by western blot.

Results: All 29 patients had the same fibril composition type in both the initial and the follow-up biopsy (8 type A and 21 type B). Even patients with a disease duration of more than 12 years and an age over 75 years at the time of the follow-up biopsy had type B fibrils in both biopsies.

Discussion: The result clearly shows that the amyloid fibril composition containing large amounts of C-terminal fragments (fibril type A) is a consequence of other factors than a slow degradation process occurring over time.

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Public Library of Science , 2022. Vol. 17, nr 3, artikkel-id e0266092
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URN: urn:nbn:se:umu:diva-193805DOI: 10.1371/journal.pone.0266092ISI: 000799828800066PubMedID: 35358243Scopus ID: 2-s2.0-85127435798OAI: oai:DiVA.org:umu-193805DiVA, id: diva2:1656531
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Erik, Karin och Gösta Selanders FoundationTilgjengelig fra: 2022-05-06 Laget: 2022-05-06 Sist oppdatert: 2025-02-10bibliografisk kontrollert

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Anan, IntissarSuhr, Ole B.Pilebro, BjörnWixner, Jonas

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