Amyloid fibril composition type is consistent over time in patients with Val30Met (p.Val50Met) transthyretin amyloidosis.

ABSTRACT:

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 amyloidos

SUBMITTER: Anan I 

PROVIDER: S-EPMC8970372 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature