{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T01:27:06Z","timestamp":1789694826772,"version":"4.0.1"},"reference-count":92,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2021,9,9]],"date-time":"2021-09-09T00:00:00Z","timestamp":1631145600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2021,9,9]],"date-time":"2021-09-09T00:00:00Z","timestamp":1631145600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/100000049","name":"National Institute on Aging","doi-asserted-by":"crossref","award":["P50AG047266"],"award-info":[{"award-number":["P50AG047266"]}],"id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"crossref","award":["R01NS089022"],"award-info":[{"award-number":["R01NS089022"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"crossref","award":["R01NS100876"],"award-info":[{"award-number":["R01NS100876"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Neurodegeneration"],"abstract":"<jats:title>Abstract<\/jats:title><jats:sec>\n                <jats:title>Background<\/jats:title>\n                <jats:p>The misfolding of host-encoded proteins into pathological prion conformations is a defining characteristic of many neurodegenerative disorders, including Alzheimer\u2019s disease, Parkinson\u2019s disease, and Lewy body dementia. A current area of intense study is the way in which the pathological deposition of these proteins might influence each other, as various combinations of co-pathology between prion-capable proteins are associated with exacerbation of disease. A spectrum of pathological, genetic and biochemical evidence provides credence to the notion that amyloid \u03b2 (A\u03b2) accumulation can induce and promote \u03b1-synuclein pathology, driving neurodegeneration.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Methods<\/jats:title>\n                <jats:p>To assess the interplay between \u03b1-synuclein and A\u03b2 on protein aggregation kinetics, we crossed mice expressing human \u03b1-synuclein (M20) with APPswe\/PS1dE9 transgenic mice (L85) to generate M20\/L85 mice. We then injected \u03b1-synuclein preformed fibrils (PFFs) unilaterally into the hippocampus of 6-month-old mice, harvesting 2 or 4\u2009months later.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Results<\/jats:title>\n                <jats:p>Immunohistochemical analysis of M20\/L85 mice revealed that pre-existing A\u03b2 plaques exacerbate the spread and deposition of induced \u03b1-synuclein pathology. This process was associated with increased neuroinflammation. Unexpectedly, the injection of \u03b1-synuclein PFFs in L85 mice enhanced the deposition of A\u03b2; whereas the level of A\u03b2 deposition in M20\/L85 bigenic mice, injected with \u03b1-synuclein PFFs, did not differ from that of mice injected with PBS.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Conclusions<\/jats:title>\n                <jats:p>These studies reveal novel and unexpected interplays between \u03b1-synuclein pathology, A\u03b2 and neuroinflammation in mice that recapitulate the pathology of Alzheimer\u2019s disease and Lewy body dementia.<\/jats:p>\n              <\/jats:sec>","DOI":"10.1186\/s13024-021-00486-9","type":"journal-article","created":{"date-parts":[[2021,9,9]],"date-time":"2021-09-09T09:02:47Z","timestamp":1631178167000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":27,"title":["Collusion of \u03b1-Synuclein and A\u03b2 aggravating co-morbidities in a novel prion-type mouse model"],"prefix":"10.1186","volume":"16","author":[{"given":"Grace M.","family":"Lloyd","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jess-Karan S.","family":"Dhillon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kimberly-Marie M.","family":"Gorion","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cara","family":"Riffe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susan E.","family":"Fromholt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuxing","family":"Xia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2992-4234","authenticated-orcid":false,"given":"Benoit I.","family":"Giasson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David R.","family":"Borchelt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2021,9,9]]},"reference":[{"issue":"6","key":"486_CR1","doi-asserted-by":"publisher","first-page":"1188","DOI":"10.1016\/j.cell.2012.02.022","volume":"148","author":"D Eisenberg","year":"2012","unstructured":"Eisenberg D, Jucker M. 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