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Human Palatine Tonsils Are Linked to Alzheimer’s Disease through Function of Reservoir of Amyloid Beta Protein Associated with Bacterial Infection
Amyloid-β (Aβ)-peptide production or deposition in the neuropathology of Alzheimer’s disease (AD) was shown to be caused by chronic inflammation that may be induced by infection, but the role of pathogenic-bacteria-related AD-associated Aβ is not yet clearly understood. In this study, we validated t...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9330135/ https://www.ncbi.nlm.nih.gov/pubmed/35892582 http://dx.doi.org/10.3390/cells11152285 |
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author | Lim, Jung Yeon Lee, Jung Eun Kim, Han Kyung Park, Yeon-Joon Jeon, Jung Ho Park, Soon-A. Lee, Naeun Lee, Il Hwan Kim, Do Hyun Yang, Seung Ho Yoo, Jongman Kim, Sung Won |
author_facet | Lim, Jung Yeon Lee, Jung Eun Kim, Han Kyung Park, Yeon-Joon Jeon, Jung Ho Park, Soon-A. Lee, Naeun Lee, Il Hwan Kim, Do Hyun Yang, Seung Ho Yoo, Jongman Kim, Sung Won |
author_sort | Lim, Jung Yeon |
collection | PubMed |
description | Amyloid-β (Aβ)-peptide production or deposition in the neuropathology of Alzheimer’s disease (AD) was shown to be caused by chronic inflammation that may be induced by infection, but the role of pathogenic-bacteria-related AD-associated Aβ is not yet clearly understood. In this study, we validated the hypothesis that there is a correlation between the Aβ-protein load and bacterial infection and that there are effects of bacteria, Staphylococcus aureus (S. aureus), on the Aβ load in the inflammatory environment of human tonsils. Here, we detected Aβ-peptide deposits in human tonsil tissue as well as tissue similar to tonsilloliths found in the olfactory cleft. Interestingly, we demonstrated for the first time the presence of Staphylococcus aureus (S. aureus) clustered around or embedded in the Aβ deposits. Notably, we showed that treatment with S. aureus upregulated the Aβ-protein load in cultures of human tonsil organoids and brain organoids, showing the new role of S. aureus in Aβ-protein aggregation. These findings suggest that a reservoir of Aβ and pathogenic bacteria may be a possible therapeutic target in human tonsils, supporting the treatment of antibiotics to prevent the deposition of Aβ peptides via the removal of pathogens in the intervention of AD pathogenesis. |
format | Online Article Text |
id | pubmed-9330135 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-93301352022-07-29 Human Palatine Tonsils Are Linked to Alzheimer’s Disease through Function of Reservoir of Amyloid Beta Protein Associated with Bacterial Infection Lim, Jung Yeon Lee, Jung Eun Kim, Han Kyung Park, Yeon-Joon Jeon, Jung Ho Park, Soon-A. Lee, Naeun Lee, Il Hwan Kim, Do Hyun Yang, Seung Ho Yoo, Jongman Kim, Sung Won Cells Article Amyloid-β (Aβ)-peptide production or deposition in the neuropathology of Alzheimer’s disease (AD) was shown to be caused by chronic inflammation that may be induced by infection, but the role of pathogenic-bacteria-related AD-associated Aβ is not yet clearly understood. In this study, we validated the hypothesis that there is a correlation between the Aβ-protein load and bacterial infection and that there are effects of bacteria, Staphylococcus aureus (S. aureus), on the Aβ load in the inflammatory environment of human tonsils. Here, we detected Aβ-peptide deposits in human tonsil tissue as well as tissue similar to tonsilloliths found in the olfactory cleft. Interestingly, we demonstrated for the first time the presence of Staphylococcus aureus (S. aureus) clustered around or embedded in the Aβ deposits. Notably, we showed that treatment with S. aureus upregulated the Aβ-protein load in cultures of human tonsil organoids and brain organoids, showing the new role of S. aureus in Aβ-protein aggregation. These findings suggest that a reservoir of Aβ and pathogenic bacteria may be a possible therapeutic target in human tonsils, supporting the treatment of antibiotics to prevent the deposition of Aβ peptides via the removal of pathogens in the intervention of AD pathogenesis. MDPI 2022-07-24 /pmc/articles/PMC9330135/ /pubmed/35892582 http://dx.doi.org/10.3390/cells11152285 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Lim, Jung Yeon Lee, Jung Eun Kim, Han Kyung Park, Yeon-Joon Jeon, Jung Ho Park, Soon-A. Lee, Naeun Lee, Il Hwan Kim, Do Hyun Yang, Seung Ho Yoo, Jongman Kim, Sung Won Human Palatine Tonsils Are Linked to Alzheimer’s Disease through Function of Reservoir of Amyloid Beta Protein Associated with Bacterial Infection |
title | Human Palatine Tonsils Are Linked to Alzheimer’s Disease through Function of Reservoir of Amyloid Beta Protein Associated with Bacterial Infection |
title_full | Human Palatine Tonsils Are Linked to Alzheimer’s Disease through Function of Reservoir of Amyloid Beta Protein Associated with Bacterial Infection |
title_fullStr | Human Palatine Tonsils Are Linked to Alzheimer’s Disease through Function of Reservoir of Amyloid Beta Protein Associated with Bacterial Infection |
title_full_unstemmed | Human Palatine Tonsils Are Linked to Alzheimer’s Disease through Function of Reservoir of Amyloid Beta Protein Associated with Bacterial Infection |
title_short | Human Palatine Tonsils Are Linked to Alzheimer’s Disease through Function of Reservoir of Amyloid Beta Protein Associated with Bacterial Infection |
title_sort | human palatine tonsils are linked to alzheimer’s disease through function of reservoir of amyloid beta protein associated with bacterial infection |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9330135/ https://www.ncbi.nlm.nih.gov/pubmed/35892582 http://dx.doi.org/10.3390/cells11152285 |
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