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N-terminal peptide fragment constitutes core of amyloid deposition of serum amyloid A: An imaging mass spectrometry study
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 re...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9565386/ https://www.ncbi.nlm.nih.gov/pubmed/36240260 http://dx.doi.org/10.1371/journal.pone.0275993 |
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author | Shintani-Domoto, Yukako Sugiura, Yuki Ogawa, Makiko Sugiyama, Eiji Abe, Hiroyuki Sakatani, Takashi Ohashi, Ryuji Ushiku, Tetsuo Fukayama, Masashi |
author_facet | Shintani-Domoto, Yukako Sugiura, Yuki Ogawa, Makiko Sugiyama, Eiji Abe, Hiroyuki Sakatani, Takashi Ohashi, Ryuji Ushiku, Tetsuo Fukayama, Masashi |
author_sort | Shintani-Domoto, Yukako |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-9565386 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-95653862022-10-15 N-terminal peptide fragment constitutes core of amyloid deposition of serum amyloid A: An imaging mass spectrometry study Shintani-Domoto, Yukako Sugiura, Yuki Ogawa, Makiko Sugiyama, Eiji Abe, Hiroyuki Sakatani, Takashi Ohashi, Ryuji Ushiku, Tetsuo Fukayama, Masashi PLoS One Research Article 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. Public Library of Science 2022-10-14 /pmc/articles/PMC9565386/ /pubmed/36240260 http://dx.doi.org/10.1371/journal.pone.0275993 Text en © 2022 Shintani-Domoto et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Shintani-Domoto, Yukako Sugiura, Yuki Ogawa, Makiko Sugiyama, Eiji Abe, Hiroyuki Sakatani, Takashi Ohashi, Ryuji Ushiku, Tetsuo Fukayama, Masashi N-terminal peptide fragment constitutes core of amyloid deposition of serum amyloid A: An imaging mass spectrometry study |
title | N-terminal peptide fragment constitutes core of amyloid deposition of serum amyloid A: An imaging mass spectrometry study |
title_full | N-terminal peptide fragment constitutes core of amyloid deposition of serum amyloid A: An imaging mass spectrometry study |
title_fullStr | N-terminal peptide fragment constitutes core of amyloid deposition of serum amyloid A: An imaging mass spectrometry study |
title_full_unstemmed | N-terminal peptide fragment constitutes core of amyloid deposition of serum amyloid A: An imaging mass spectrometry study |
title_short | N-terminal peptide fragment constitutes core of amyloid deposition of serum amyloid A: An imaging mass spectrometry study |
title_sort | n-terminal peptide fragment constitutes core of amyloid deposition of serum amyloid a: an imaging mass spectrometry study |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9565386/ https://www.ncbi.nlm.nih.gov/pubmed/36240260 http://dx.doi.org/10.1371/journal.pone.0275993 |
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