Human amygdala involvement in Alzheimer's disease revealed by stereological and dia‐PASEF analysis
Alzheimer's disease (AD) is characterized by the accumulation of pathological amyloid‐β (Aβ) and Tau proteins. According to the prion‐like hypothesis, both proteins can seed and disseminate through brain regions through neural connections and glial cells. The amygdaloid complex (AC) is involved...
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| Veröffentlicht in: | Brain pathology (Zurich, Switzerland) Switzerland), 2023-09, Vol.33 (5), p.e13180-n/a |
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| creator | Gonzalez‐Rodriguez, Melania Villar‐Conde, Sandra Astillero‐Lopez, Veronica Villanueva‐Anguita, Patricia Ubeda‐Banon, Isabel Flores‐Cuadrado, Alicia Martinez‐Marcos, Alino Saiz‐Sanchez, Daniel |
| description | Alzheimer's disease (AD) is characterized by the accumulation of pathological amyloid‐β (Aβ) and Tau proteins. According to the prion‐like hypothesis, both proteins can seed and disseminate through brain regions through neural connections and glial cells. The amygdaloid complex (AC) is involved early in the disease, and its widespread connections with other brain regions indicate that it is a hub for propagating pathology. To characterize changes in the AC as well as the involvement of neuronal and glial cells in AD, a combined stereological and proteomic analysis was performed in non‐Alzheimer's disease and AD human samples. The synaptic alterations identified by proteomic data analysis could be related to the volume reduction observed in AD by the Cavalieri probe without neuronal loss. The pathological markers appeared in a gradient pattern with the medial region (cortical nucleus, Co) being more affected than lateral regions, suggesting the relevance of connections in the distribution of the pathology among different brain regions. Generalized astrogliosis was observed in every AC nucleus, likely related to deposits of pathological proteins. Astrocytes might mediate phagocytic microglial activation, whereas microglia might play a dual role since protective and toxic phenotypes have been described. These results highlight the potential participation of the amygdala in the disease spreading from/to olfactory areas, the temporal lobe and beyond. Proteomic data are available via ProteomeXchange with identifier PXD038322.
A combined stereological and proteomic analysis revealed amygdala volume reduction linked to synaptic dysfunction in Alzheimer''s disease samples. The pathological markers gradient suggested the relevance of connections in the distribution of the pathology among different brain regions. Extended astrogliosis, likely as response to pathologic deposits, could mediate phagocytic microglial activation. Microglia might play a dual role since protective and toxic phenotypes have been described. In conclusion, amygdala might promote the spreading of pathology from/to olfactory areas, the temporal lobe and beyond. |
| doi_str_mv | 10.1111/bpa.13180 |
| format | Article |
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A combined stereological and proteomic analysis revealed amygdala volume reduction linked to synaptic dysfunction in Alzheimer''s disease samples. The pathological markers gradient suggested the relevance of connections in the distribution of the pathology among different brain regions. Extended astrogliosis, likely as response to pathologic deposits, could mediate phagocytic microglial activation. Microglia might play a dual role since protective and toxic phenotypes have been described. In conclusion, amygdala might promote the spreading of pathology from/to olfactory areas, the temporal lobe and beyond.</description><identifier>ISSN: 1015-6305</identifier><identifier>EISSN: 1750-3639</identifier><identifier>DOI: 10.1111/bpa.13180</identifier><identifier>PMID: 37331354</identifier><language>eng</language><publisher>Switzerland: John Wiley & Sons, Inc</publisher><subject>Alzheimer's disease ; Amygdala ; antioxidant protein 2 (AOP2) ; Astrocytes ; BM88 antigen (BM88) ; Brain ; calpactin II ; calpactin‐1 heavy chain (CAL1H) ; centaurin‐alpha‐1 (CENTA1) ; Data analysis ; endonexin II (ENX2) ; Glial cells ; Gliosis ; Microglia ; Neurodegenerative diseases ; Neuroglia ; Neuronal-glial interactions ; nuclear chloride ion channel 27 (NCC27) ; Pathology ; Phagocytes ; Phenotypes ; Proteins ; Proteomics ; Tau protein ; Temporal lobe ; β-Amyloid</subject><ispartof>Brain pathology (Zurich, Switzerland), 2023-09, Vol.33 (5), p.e13180-n/a</ispartof><rights>2023 The Authors. published by John Wiley & Sons Ltd on behalf of International Society of Neuropathology.</rights><rights>2023 The Authors. Brain Pathology published by John Wiley & Sons Ltd on behalf of International Society of Neuropathology.</rights><rights>2023. This work is published under http://creativecommons.org/licenses/by/4.0/ (the "License"). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4440-d6e80171d443257eecb6dced41980546343992297dfc1a2bfcd5cee496b773c23</citedby><cites>FETCH-LOGICAL-c4440-d6e80171d443257eecb6dced41980546343992297dfc1a2bfcd5cee496b773c23</cites><orcidid>0000-0002-3768-5483 ; 0000-0003-3691-3605 ; 0000-0001-7002-8031 ; 0000-0003-0564-3630 ; 0000-0002-4199-6313 ; 0000-0003-1753-5469 ; 0000-0002-5351-3008 ; 0000-0002-3290-902X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10467039/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10467039/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,865,886,1418,11567,27929,27930,45579,45580,46057,46481,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37331354$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gonzalez‐Rodriguez, Melania</creatorcontrib><creatorcontrib>Villar‐Conde, Sandra</creatorcontrib><creatorcontrib>Astillero‐Lopez, Veronica</creatorcontrib><creatorcontrib>Villanueva‐Anguita, Patricia</creatorcontrib><creatorcontrib>Ubeda‐Banon, Isabel</creatorcontrib><creatorcontrib>Flores‐Cuadrado, Alicia</creatorcontrib><creatorcontrib>Martinez‐Marcos, Alino</creatorcontrib><creatorcontrib>Saiz‐Sanchez, Daniel</creatorcontrib><title>Human amygdala involvement in Alzheimer's disease revealed by stereological and dia‐PASEF analysis</title><title>Brain pathology (Zurich, Switzerland)</title><addtitle>Brain Pathol</addtitle><description>Alzheimer's disease (AD) is characterized by the accumulation of pathological amyloid‐β (Aβ) and Tau proteins. According to the prion‐like hypothesis, both proteins can seed and disseminate through brain regions through neural connections and glial cells. The amygdaloid complex (AC) is involved early in the disease, and its widespread connections with other brain regions indicate that it is a hub for propagating pathology. To characterize changes in the AC as well as the involvement of neuronal and glial cells in AD, a combined stereological and proteomic analysis was performed in non‐Alzheimer's disease and AD human samples. The synaptic alterations identified by proteomic data analysis could be related to the volume reduction observed in AD by the Cavalieri probe without neuronal loss. The pathological markers appeared in a gradient pattern with the medial region (cortical nucleus, Co) being more affected than lateral regions, suggesting the relevance of connections in the distribution of the pathology among different brain regions. Generalized astrogliosis was observed in every AC nucleus, likely related to deposits of pathological proteins. Astrocytes might mediate phagocytic microglial activation, whereas microglia might play a dual role since protective and toxic phenotypes have been described. These results highlight the potential participation of the amygdala in the disease spreading from/to olfactory areas, the temporal lobe and beyond. Proteomic data are available via ProteomeXchange with identifier PXD038322.
A combined stereological and proteomic analysis revealed amygdala volume reduction linked to synaptic dysfunction in Alzheimer''s disease samples. The pathological markers gradient suggested the relevance of connections in the distribution of the pathology among different brain regions. Extended astrogliosis, likely as response to pathologic deposits, could mediate phagocytic microglial activation. Microglia might play a dual role since protective and toxic phenotypes have been described. In conclusion, amygdala might promote the spreading of pathology from/to olfactory areas, the temporal lobe and beyond.</description><subject>Alzheimer's disease</subject><subject>Amygdala</subject><subject>antioxidant protein 2 (AOP2)</subject><subject>Astrocytes</subject><subject>BM88 antigen (BM88)</subject><subject>Brain</subject><subject>calpactin II</subject><subject>calpactin‐1 heavy chain (CAL1H)</subject><subject>centaurin‐alpha‐1 (CENTA1)</subject><subject>Data analysis</subject><subject>endonexin II (ENX2)</subject><subject>Glial cells</subject><subject>Gliosis</subject><subject>Microglia</subject><subject>Neurodegenerative diseases</subject><subject>Neuroglia</subject><subject>Neuronal-glial interactions</subject><subject>nuclear chloride ion channel 27 (NCC27)</subject><subject>Pathology</subject><subject>Phagocytes</subject><subject>Phenotypes</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Tau protein</subject><subject>Temporal 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amygdala involvement in Alzheimer's disease revealed by stereological and dia‐PASEF analysis</title><author>Gonzalez‐Rodriguez, Melania ; Villar‐Conde, Sandra ; Astillero‐Lopez, Veronica ; Villanueva‐Anguita, Patricia ; Ubeda‐Banon, Isabel ; Flores‐Cuadrado, Alicia ; Martinez‐Marcos, Alino ; Saiz‐Sanchez, Daniel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4440-d6e80171d443257eecb6dced41980546343992297dfc1a2bfcd5cee496b773c23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Alzheimer's disease</topic><topic>Amygdala</topic><topic>antioxidant protein 2 (AOP2)</topic><topic>Astrocytes</topic><topic>BM88 antigen (BM88)</topic><topic>Brain</topic><topic>calpactin II</topic><topic>calpactin‐1 heavy chain (CAL1H)</topic><topic>centaurin‐alpha‐1 (CENTA1)</topic><topic>Data analysis</topic><topic>endonexin II (ENX2)</topic><topic>Glial 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Daniel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human amygdala involvement in Alzheimer's disease revealed by stereological and dia‐PASEF analysis</atitle><jtitle>Brain pathology (Zurich, Switzerland)</jtitle><addtitle>Brain Pathol</addtitle><date>2023-09</date><risdate>2023</risdate><volume>33</volume><issue>5</issue><spage>e13180</spage><epage>n/a</epage><pages>e13180-n/a</pages><issn>1015-6305</issn><eissn>1750-3639</eissn><abstract>Alzheimer's disease (AD) is characterized by the accumulation of pathological amyloid‐β (Aβ) and Tau proteins. According to the prion‐like hypothesis, both proteins can seed and disseminate through brain regions through neural connections and glial cells. The amygdaloid complex (AC) is involved early in the disease, and its widespread connections with other brain regions indicate that it is a hub for propagating pathology. To characterize changes in the AC as well as the involvement of neuronal and glial cells in AD, a combined stereological and proteomic analysis was performed in non‐Alzheimer's disease and AD human samples. The synaptic alterations identified by proteomic data analysis could be related to the volume reduction observed in AD by the Cavalieri probe without neuronal loss. The pathological markers appeared in a gradient pattern with the medial region (cortical nucleus, Co) being more affected than lateral regions, suggesting the relevance of connections in the distribution of the pathology among different brain regions. Generalized astrogliosis was observed in every AC nucleus, likely related to deposits of pathological proteins. Astrocytes might mediate phagocytic microglial activation, whereas microglia might play a dual role since protective and toxic phenotypes have been described. These results highlight the potential participation of the amygdala in the disease spreading from/to olfactory areas, the temporal lobe and beyond. Proteomic data are available via ProteomeXchange with identifier PXD038322.
A combined stereological and proteomic analysis revealed amygdala volume reduction linked to synaptic dysfunction in Alzheimer''s disease samples. The pathological markers gradient suggested the relevance of connections in the distribution of the pathology among different brain regions. Extended astrogliosis, likely as response to pathologic deposits, could mediate phagocytic microglial activation. Microglia might play a dual role since protective and toxic phenotypes have been described. In conclusion, amygdala might promote the spreading of pathology from/to olfactory areas, the temporal lobe and beyond.</abstract><cop>Switzerland</cop><pub>John Wiley & Sons, Inc</pub><pmid>37331354</pmid><doi>10.1111/bpa.13180</doi><tpages>22</tpages><orcidid>https://orcid.org/0000-0002-3768-5483</orcidid><orcidid>https://orcid.org/0000-0003-3691-3605</orcidid><orcidid>https://orcid.org/0000-0001-7002-8031</orcidid><orcidid>https://orcid.org/0000-0003-0564-3630</orcidid><orcidid>https://orcid.org/0000-0002-4199-6313</orcidid><orcidid>https://orcid.org/0000-0003-1753-5469</orcidid><orcidid>https://orcid.org/0000-0002-5351-3008</orcidid><orcidid>https://orcid.org/0000-0002-3290-902X</orcidid><oa>free_for_read</oa></addata></record> |
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| source | Open Access: PubMed Central; Wiley Online Library Journals; DOAJ Directory of Open Access Journals; Wiley Open Access; EZB Electronic Journals Library |
| subjects | Alzheimer's disease Amygdala antioxidant protein 2 (AOP2) Astrocytes BM88 antigen (BM88) Brain calpactin II calpactin‐1 heavy chain (CAL1H) centaurin‐alpha‐1 (CENTA1) Data analysis endonexin II (ENX2) Glial cells Gliosis Microglia Neurodegenerative diseases Neuroglia Neuronal-glial interactions nuclear chloride ion channel 27 (NCC27) Pathology Phagocytes Phenotypes Proteins Proteomics Tau protein Temporal lobe β-Amyloid |
| title | Human amygdala involvement in Alzheimer's disease revealed by stereological and dia‐PASEF analysis |
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