ArticlePloS one2022
N-terminal peptide fragment constitutes core of amyloid deposition of serum amyloid A: An imaging mass spectrometry study.
Article in PloS one, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- In situ, antibody-independent, and multiplexed characterization of amyloid plaques by MALDI MS/MS imaging using iprm-PASEF.Analytical and bioanalytical chemistry · 2026Article
- Elucidation of the mechanism of amyloid A and transthyretin formation using mass spectrometry-based absolute quantification.Virchows Archiv : an international journal of pathology · 2024Article
- Integrated Spatial Multi-Omics Study of Postmortem Brains of Alzheimer's Disease.Acta histochemica et cytochemica · 2024Article
- Investigation of serum amyloid a within animal species focusing on the 1-25 amino acid region.The veterinary quarterly · 2023Article
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Authors and funding
9 authors at 6 institutions in 2 countries.
Funding
Abstract
Serum amyloid A (SAA) is an acute phase protein, which undergoes structural changes and deposits in the extracellular matrix, causing organ damage. Systemic AA amyloidosis is a relatively common amyloid subtype among the more than 30 amyloid subtypes, but the mechanism of amyloid fibril formation remains unclear. In this study, we investigated the tissue distribution of SAA derived peptides in formalin-fixed paraffin embedded (FFPE) specimens of human myocardium with amyloidosis using matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI-IMS). In the whole SAA protein, four trypsin-digested peptides in the range of SAA2-67 were visualized and the N-terminal peptide; SAA2-15, was selectively localized in the Congo red-positive region. The C-terminal peptides; SAA47-62, SAA48-62, and SAA63-67 were detected not only in the Congo red-positive region but also in the surrounding negative region. Our results demonstrate that the N-terminal SAA2-15 plays a critical role in the formation of AA amyloid fibril, as previously reported. Roles of the C-terminal peptides require further investigation.
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Registered trials
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