Does the structure of transthyretin amyloid fibrils vary depending on the organ of accumulation?

Mineyuki Mizuguchi

doi:10.1016/j.str.2024.11.002

Does the structure of transthyretin amyloid fibrils vary depending on the organ of accumulation?

Structure. 2024 Dec 5;32(12):2181-2182. doi: 10.1016/j.str.2024.11.002.

Author

Mineyuki Mizuguchi¹

Affiliation

¹ Faculty of Pharmaceutical Sciences, University of Toyama, Toyama, Japan. Electronic address: [email protected].

PMID: 39642847
DOI: 10.1016/j.str.2024.11.002

Abstract

In this issue of Structure, Nguyen et al.¹ reveal that amyloid fibrils of the transthyretin (TTR) V30M variant from the heart and nerves of the same patient exhibit structural homogeneity. This finding is crucial for advancing our understanding of V30M-TTR amyloid deposition, which leads to fatal ATTRv amyloidosis.

MeSH terms

Amyloid Neuropathies, Familial / metabolism
Amyloid Neuropathies, Familial / pathology
Amyloid* / chemistry
Amyloid* / metabolism
Humans
Prealbumin* / chemistry
Prealbumin* / genetics
Prealbumin* / metabolism

Substances

Prealbumin
Amyloid
TTR protein, human

Supplementary concepts

Amyloidosis, Hereditary, Transthyretin-Related