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Observations of amyloid breakdown by proteases over time using scanning acoustic microscopy
Amyloid consists of insoluble beta-fibrillar proteins with stable structures. The Congo red staining method for histologically detecting amyloid is unsuitable for quantitatively assessing amyloid fibers. Scanning acoustic microscopy (SAM) detects the attenuation of sound (AOS) through sections. This...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10673902/ https://www.ncbi.nlm.nih.gov/pubmed/38001251 http://dx.doi.org/10.1038/s41598-023-48033-4 |
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author | Miura, Katsutoshi Iwashita, Toshihide |
author_facet | Miura, Katsutoshi Iwashita, Toshihide |
author_sort | Miura, Katsutoshi |
collection | PubMed |
description | Amyloid consists of insoluble beta-fibrillar proteins with stable structures. The Congo red staining method for histologically detecting amyloid is unsuitable for quantitatively assessing amyloid fibers. Scanning acoustic microscopy (SAM) detects the attenuation of sound (AOS) through sections. This study aimed to clarify whether AOS values reflected the amount of amyloid fibril degradation in tissues. Formalin-fixed paraffin-embedded unstained sections of various types of amyloidosis were digested with different endopeptidases. The AOS images after digestion were observed over time via SAM. The corresponding Congo red-stained images were followed to identify the amyloid. The amyloid and nonamyloid portions were statistically examined over time to determine the changes in the AOS values. Most of the amyloid areas showed significantly different AOS values from nonamyloid portions before digestion and significantly decreased after digestion; these findings corresponded with the disappearance and waning of the Congo red staining in the light microscopic images. Some nonamyloid areas with high AOS masked the reduction in AOS in the amyloid areas. The method used in this study may help detect the amyloid quantity and determine the appropriate treatment method for removing amyloid deposits from tissues. |
format | Online Article Text |
id | pubmed-10673902 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-106739022023-11-24 Observations of amyloid breakdown by proteases over time using scanning acoustic microscopy Miura, Katsutoshi Iwashita, Toshihide Sci Rep Article Amyloid consists of insoluble beta-fibrillar proteins with stable structures. The Congo red staining method for histologically detecting amyloid is unsuitable for quantitatively assessing amyloid fibers. Scanning acoustic microscopy (SAM) detects the attenuation of sound (AOS) through sections. This study aimed to clarify whether AOS values reflected the amount of amyloid fibril degradation in tissues. Formalin-fixed paraffin-embedded unstained sections of various types of amyloidosis were digested with different endopeptidases. The AOS images after digestion were observed over time via SAM. The corresponding Congo red-stained images were followed to identify the amyloid. The amyloid and nonamyloid portions were statistically examined over time to determine the changes in the AOS values. Most of the amyloid areas showed significantly different AOS values from nonamyloid portions before digestion and significantly decreased after digestion; these findings corresponded with the disappearance and waning of the Congo red staining in the light microscopic images. Some nonamyloid areas with high AOS masked the reduction in AOS in the amyloid areas. The method used in this study may help detect the amyloid quantity and determine the appropriate treatment method for removing amyloid deposits from tissues. Nature Publishing Group UK 2023-11-24 /pmc/articles/PMC10673902/ /pubmed/38001251 http://dx.doi.org/10.1038/s41598-023-48033-4 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Miura, Katsutoshi Iwashita, Toshihide Observations of amyloid breakdown by proteases over time using scanning acoustic microscopy |
title | Observations of amyloid breakdown by proteases over time using scanning acoustic microscopy |
title_full | Observations of amyloid breakdown by proteases over time using scanning acoustic microscopy |
title_fullStr | Observations of amyloid breakdown by proteases over time using scanning acoustic microscopy |
title_full_unstemmed | Observations of amyloid breakdown by proteases over time using scanning acoustic microscopy |
title_short | Observations of amyloid breakdown by proteases over time using scanning acoustic microscopy |
title_sort | observations of amyloid breakdown by proteases over time using scanning acoustic microscopy |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10673902/ https://www.ncbi.nlm.nih.gov/pubmed/38001251 http://dx.doi.org/10.1038/s41598-023-48033-4 |
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