Transmissible α-synuclein seeding activity in brain and stomach of patients with Parkinson’s disease
Cerebral deposition of abnormally aggregated α-synuclein (αSyn) is a neuropathological hallmark of Parkinson’s disease (PD). PD-associated αSyn (αSyn PD ) aggregates can act as proteinaceous nuclei (“seeds”) able of self-templated propagation. Since this is strikingly reminiscent to properties of pr...
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| Veröffentlicht in: | Acta neuropathologica 2021-06, Vol.141 (6), p.861-879 |
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| creator | Thomzig, Achim Wagenführ, Katja Pinder, Phillip Joncic, Marion Schulz-Schaeffer, Walter J. Beekes, Michael |
| description | Cerebral deposition of abnormally aggregated α-synuclein (αSyn) is a neuropathological hallmark of Parkinson’s disease (PD). PD-associated αSyn (αSyn
PD
) aggregates can act as proteinaceous nuclei (“seeds”) able of self-templated propagation. Since this is strikingly reminiscent to properties of proteinaceous infectious particles (prions), lessons learned from prion diseases suggest to test whether transferred αSyn
PD
can propagate and induce neurological impairments or disease in a new host. Two studies that addressed this question provided divergent results. Intracerebral (i.c.) injection of Lewy body extracts from PD patients caused cerebral αSyn pathology, as well as nigrostriatal neurodegeneration, of wild-type mice and macaques, with the mice also showing motor impairments (Recasens et al. 2014, Ann Neurol 75:351–362). In contrast, i.c. transmission of homogenates from PD brains did not stimulate, after “> 360” days post-injection (dpi), pathological αSyn conversion or clinical symptoms in transgenic TgM83
+/−
mice hemizygously expressing mutated (A53T) human αSyn (Prusiner et al. 2015, PNAS 112:E5308–E5317). To advance the assessment of possible αSyn
PD
hazards by providing further data, we examined neuropathological and clinical effects upon i.c. transmission of brain, stomach wall and muscle tissue as well as blood from PD patients in TgM83
+/−
mice up to 612 dpi. This revealed a subtle, yet distinctive stimulation of localized αSyn aggregation in the somatodendritic compartment and dystrophic neurites of individual or focally clustered cerebral neurons after challenge with brain and stomach wall homogenates. No such effect was observed with transmitted blood or homogenized muscle tissue. The detected stimulation of αSyn aggregation was not accompanied by apparent motor impairments or overt neurological disease in TgM83
+/−
mice. Our study substantiated that transmitted αSyn
PD
seeds, including those from the stomach wall, are able to propagate in new mammalian hosts. The consequences of such propagation and potential safeguards need to be further investigated. |
| doi_str_mv | 10.1007/s00401-021-02312-4 |
| format | Article |
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PD
) aggregates can act as proteinaceous nuclei (“seeds”) able of self-templated propagation. Since this is strikingly reminiscent to properties of proteinaceous infectious particles (prions), lessons learned from prion diseases suggest to test whether transferred αSyn
PD
can propagate and induce neurological impairments or disease in a new host. Two studies that addressed this question provided divergent results. Intracerebral (i.c.) injection of Lewy body extracts from PD patients caused cerebral αSyn pathology, as well as nigrostriatal neurodegeneration, of wild-type mice and macaques, with the mice also showing motor impairments (Recasens et al. 2014, Ann Neurol 75:351–362). In contrast, i.c. transmission of homogenates from PD brains did not stimulate, after “> 360” days post-injection (dpi), pathological αSyn conversion or clinical symptoms in transgenic TgM83
+/−
mice hemizygously expressing mutated (A53T) human αSyn (Prusiner et al. 2015, PNAS 112:E5308–E5317). To advance the assessment of possible αSyn
PD
hazards by providing further data, we examined neuropathological and clinical effects upon i.c. transmission of brain, stomach wall and muscle tissue as well as blood from PD patients in TgM83
+/−
mice up to 612 dpi. This revealed a subtle, yet distinctive stimulation of localized αSyn aggregation in the somatodendritic compartment and dystrophic neurites of individual or focally clustered cerebral neurons after challenge with brain and stomach wall homogenates. No such effect was observed with transmitted blood or homogenized muscle tissue. The detected stimulation of αSyn aggregation was not accompanied by apparent motor impairments or overt neurological disease in TgM83
+/−
mice. Our study substantiated that transmitted αSyn
PD
seeds, including those from the stomach wall, are able to propagate in new mammalian hosts. The consequences of such propagation and potential safeguards need to be further investigated.</description><identifier>ISSN: 0001-6322</identifier><identifier>EISSN: 1432-0533</identifier><identifier>DOI: 10.1007/s00401-021-02312-4</identifier><identifier>PMID: 33895878</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>alpha-Synuclein - administration & dosage ; alpha-Synuclein - blood ; alpha-Synuclein - isolation & purification ; alpha-Synuclein - metabolism ; Animals ; Axons ; Brain ; Brain - pathology ; Enteric Nervous System - pathology ; Humans ; Injection ; Lewy bodies ; Lewy Bodies - pathology ; Medicine ; Medicine & Public Health ; Mice ; Movement disorders ; Muscle, Skeletal - pathology ; Neurodegeneration ; Neurodegenerative diseases ; Neurological diseases ; Neurons - pathology ; Neuropathology ; Neurosciences ; Original Paper ; Parkinson Disease - metabolism ; Parkinson Disease - pathology ; Parkinson's disease ; Pathology ; Prion protein ; Prions ; Protein seeding ; Seeds ; Stomach ; Stomach - pathology ; Synuclein ; Transgenic mice</subject><ispartof>Acta neuropathologica, 2021-06, Vol.141 (6), p.861-879</ispartof><rights>The Author(s) 2021</rights><rights>The Author(s) 2021. 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-c474t-dd5630119a0699f11cff920ac38adc37f877179a01b3cdd2dde871585a0eaa8f3</citedby><cites>FETCH-LOGICAL-c474t-dd5630119a0699f11cff920ac38adc37f877179a01b3cdd2dde871585a0eaa8f3</cites><orcidid>0000-0002-6454-6657</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00401-021-02312-4$$EPDF$$P50$$Gspringer$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00401-021-02312-4$$EHTML$$P50$$Gspringer$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33895878$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Thomzig, Achim</creatorcontrib><creatorcontrib>Wagenführ, Katja</creatorcontrib><creatorcontrib>Pinder, Phillip</creatorcontrib><creatorcontrib>Joncic, Marion</creatorcontrib><creatorcontrib>Schulz-Schaeffer, Walter J.</creatorcontrib><creatorcontrib>Beekes, Michael</creatorcontrib><title>Transmissible α-synuclein seeding activity in brain and stomach of patients with Parkinson’s disease</title><title>Acta neuropathologica</title><addtitle>Acta Neuropathol</addtitle><addtitle>Acta Neuropathol</addtitle><description>Cerebral deposition of abnormally aggregated α-synuclein (αSyn) is a neuropathological hallmark of Parkinson’s disease (PD). PD-associated αSyn (αSyn
PD
) aggregates can act as proteinaceous nuclei (“seeds”) able of self-templated propagation. Since this is strikingly reminiscent to properties of proteinaceous infectious particles (prions), lessons learned from prion diseases suggest to test whether transferred αSyn
PD
can propagate and induce neurological impairments or disease in a new host. Two studies that addressed this question provided divergent results. Intracerebral (i.c.) injection of Lewy body extracts from PD patients caused cerebral αSyn pathology, as well as nigrostriatal neurodegeneration, of wild-type mice and macaques, with the mice also showing motor impairments (Recasens et al. 2014, Ann Neurol 75:351–362). In contrast, i.c. transmission of homogenates from PD brains did not stimulate, after “> 360” days post-injection (dpi), pathological αSyn conversion or clinical symptoms in transgenic TgM83
+/−
mice hemizygously expressing mutated (A53T) human αSyn (Prusiner et al. 2015, PNAS 112:E5308–E5317). To advance the assessment of possible αSyn
PD
hazards by providing further data, we examined neuropathological and clinical effects upon i.c. transmission of brain, stomach wall and muscle tissue as well as blood from PD patients in TgM83
+/−
mice up to 612 dpi. This revealed a subtle, yet distinctive stimulation of localized αSyn aggregation in the somatodendritic compartment and dystrophic neurites of individual or focally clustered cerebral neurons after challenge with brain and stomach wall homogenates. No such effect was observed with transmitted blood or homogenized muscle tissue. The detected stimulation of αSyn aggregation was not accompanied by apparent motor impairments or overt neurological disease in TgM83
+/−
mice. Our study substantiated that transmitted αSyn
PD
seeds, including those from the stomach wall, are able to propagate in new mammalian hosts. The consequences of such propagation and potential safeguards need to be further investigated.</description><subject>alpha-Synuclein - administration & dosage</subject><subject>alpha-Synuclein - blood</subject><subject>alpha-Synuclein - isolation & purification</subject><subject>alpha-Synuclein - metabolism</subject><subject>Animals</subject><subject>Axons</subject><subject>Brain</subject><subject>Brain - pathology</subject><subject>Enteric Nervous System - pathology</subject><subject>Humans</subject><subject>Injection</subject><subject>Lewy bodies</subject><subject>Lewy Bodies - pathology</subject><subject>Medicine</subject><subject>Medicine & Public Health</subject><subject>Mice</subject><subject>Movement disorders</subject><subject>Muscle, Skeletal - pathology</subject><subject>Neurodegeneration</subject><subject>Neurodegenerative diseases</subject><subject>Neurological diseases</subject><subject>Neurons - pathology</subject><subject>Neuropathology</subject><subject>Neurosciences</subject><subject>Original Paper</subject><subject>Parkinson Disease - metabolism</subject><subject>Parkinson Disease - pathology</subject><subject>Parkinson's disease</subject><subject>Pathology</subject><subject>Prion protein</subject><subject>Prions</subject><subject>Protein seeding</subject><subject>Seeds</subject><subject>Stomach</subject><subject>Stomach - pathology</subject><subject>Synuclein</subject><subject>Transgenic mice</subject><issn>0001-6322</issn><issn>1432-0533</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kUtuFDEQhi0EIkPgAiyQJTZsGvzqtnuDhCJeUiRYhLVVY7tnHHrswdWdaHa5Ro7BRTgEJ8HDhPBYIMu27Prqd5V_Qh5z9pwzpl8gY4rxhon9lFw06g5ZcCVFw1op75IFYzXcSSGOyAPE83oSWrX3yZGUpm-NNguyOiuQcBMR43IM9NvXBndpdmOIiWIIPqYVBTfFizjtaL1bFqgrJE9xyhtwa5oHuoUphjQhvYzTmn6E8jkmzOn71TVSHzEAhofk3gAjhkc3-zH59Ob12cm75vTD2_cnr04bp7SaGu_bTjLOe2Bd3w-cu2HoBQMnDXgn9WC05rpG-VI674X3wWjemhZYADCDPCYvD7rbebkJ3tWyCox2W-IGys5miPbvSIpru8oX1rDOqLavAs9uBEr-MgecbP0cF8YRUsgzWtFyoxXv9B59-g96nueSanuVqkO1nKlKiQPlSkYsYbgthjO799EefLTVR_vTR7tPevJnG7cpv4yrgDwAWENpFcrvt_8j-wOrtKxo</recordid><startdate>20210601</startdate><enddate>20210601</enddate><creator>Thomzig, Achim</creator><creator>Wagenführ, Katja</creator><creator>Pinder, Phillip</creator><creator>Joncic, Marion</creator><creator>Schulz-Schaeffer, Walter J.</creator><creator>Beekes, Michael</creator><general>Springer Berlin Heidelberg</general><general>Springer Nature B.V</general><scope>C6C</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7TK</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88G</scope><scope>8AO</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-6454-6657</orcidid></search><sort><creationdate>20210601</creationdate><title>Transmissible α-synuclein seeding activity in brain and stomach of patients with Parkinson’s disease</title><author>Thomzig, Achim ; Wagenführ, Katja ; Pinder, Phillip ; Joncic, Marion ; Schulz-Schaeffer, Walter J. ; Beekes, Michael</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c474t-dd5630119a0699f11cff920ac38adc37f877179a01b3cdd2dde871585a0eaa8f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>alpha-Synuclein - administration & dosage</topic><topic>alpha-Synuclein - blood</topic><topic>alpha-Synuclein - isolation & purification</topic><topic>alpha-Synuclein - metabolism</topic><topic>Animals</topic><topic>Axons</topic><topic>Brain</topic><topic>Brain - pathology</topic><topic>Enteric Nervous System - pathology</topic><topic>Humans</topic><topic>Injection</topic><topic>Lewy bodies</topic><topic>Lewy Bodies - pathology</topic><topic>Medicine</topic><topic>Medicine & Public Health</topic><topic>Mice</topic><topic>Movement disorders</topic><topic>Muscle, Skeletal - pathology</topic><topic>Neurodegeneration</topic><topic>Neurodegenerative diseases</topic><topic>Neurological diseases</topic><topic>Neurons - pathology</topic><topic>Neuropathology</topic><topic>Neurosciences</topic><topic>Original Paper</topic><topic>Parkinson Disease - metabolism</topic><topic>Parkinson Disease - pathology</topic><topic>Parkinson's disease</topic><topic>Pathology</topic><topic>Prion protein</topic><topic>Prions</topic><topic>Protein seeding</topic><topic>Seeds</topic><topic>Stomach</topic><topic>Stomach - pathology</topic><topic>Synuclein</topic><topic>Transgenic mice</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Thomzig, Achim</creatorcontrib><creatorcontrib>Wagenführ, Katja</creatorcontrib><creatorcontrib>Pinder, Phillip</creatorcontrib><creatorcontrib>Joncic, Marion</creatorcontrib><creatorcontrib>Schulz-Schaeffer, Walter J.</creatorcontrib><creatorcontrib>Beekes, Michael</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Psychology Database (Alumni)</collection><collection>ProQuest Pharma Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Psychology Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest One Psychology</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Acta neuropathologica</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Thomzig, Achim</au><au>Wagenführ, Katja</au><au>Pinder, Phillip</au><au>Joncic, Marion</au><au>Schulz-Schaeffer, Walter J.</au><au>Beekes, Michael</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Transmissible α-synuclein seeding activity in brain and stomach of patients with Parkinson’s disease</atitle><jtitle>Acta neuropathologica</jtitle><stitle>Acta Neuropathol</stitle><addtitle>Acta Neuropathol</addtitle><date>2021-06-01</date><risdate>2021</risdate><volume>141</volume><issue>6</issue><spage>861</spage><epage>879</epage><pages>861-879</pages><issn>0001-6322</issn><eissn>1432-0533</eissn><abstract>Cerebral deposition of abnormally aggregated α-synuclein (αSyn) is a neuropathological hallmark of Parkinson’s disease (PD). PD-associated αSyn (αSyn
PD
) aggregates can act as proteinaceous nuclei (“seeds”) able of self-templated propagation. Since this is strikingly reminiscent to properties of proteinaceous infectious particles (prions), lessons learned from prion diseases suggest to test whether transferred αSyn
PD
can propagate and induce neurological impairments or disease in a new host. Two studies that addressed this question provided divergent results. Intracerebral (i.c.) injection of Lewy body extracts from PD patients caused cerebral αSyn pathology, as well as nigrostriatal neurodegeneration, of wild-type mice and macaques, with the mice also showing motor impairments (Recasens et al. 2014, Ann Neurol 75:351–362). In contrast, i.c. transmission of homogenates from PD brains did not stimulate, after “> 360” days post-injection (dpi), pathological αSyn conversion or clinical symptoms in transgenic TgM83
+/−
mice hemizygously expressing mutated (A53T) human αSyn (Prusiner et al. 2015, PNAS 112:E5308–E5317). To advance the assessment of possible αSyn
PD
hazards by providing further data, we examined neuropathological and clinical effects upon i.c. transmission of brain, stomach wall and muscle tissue as well as blood from PD patients in TgM83
+/−
mice up to 612 dpi. This revealed a subtle, yet distinctive stimulation of localized αSyn aggregation in the somatodendritic compartment and dystrophic neurites of individual or focally clustered cerebral neurons after challenge with brain and stomach wall homogenates. No such effect was observed with transmitted blood or homogenized muscle tissue. The detected stimulation of αSyn aggregation was not accompanied by apparent motor impairments or overt neurological disease in TgM83
+/−
mice. Our study substantiated that transmitted αSyn
PD
seeds, including those from the stomach wall, are able to propagate in new mammalian hosts. The consequences of such propagation and potential safeguards need to be further investigated.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>33895878</pmid><doi>10.1007/s00401-021-02312-4</doi><tpages>19</tpages><orcidid>https://orcid.org/0000-0002-6454-6657</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | alpha-Synuclein - administration & dosage alpha-Synuclein - blood alpha-Synuclein - isolation & purification alpha-Synuclein - metabolism Animals Axons Brain Brain - pathology Enteric Nervous System - pathology Humans Injection Lewy bodies Lewy Bodies - pathology Medicine Medicine & Public Health Mice Movement disorders Muscle, Skeletal - pathology Neurodegeneration Neurodegenerative diseases Neurological diseases Neurons - pathology Neuropathology Neurosciences Original Paper Parkinson Disease - metabolism Parkinson Disease - pathology Parkinson's disease Pathology Prion protein Prions Protein seeding Seeds Stomach Stomach - pathology Synuclein Transgenic mice |
| title | Transmissible α-synuclein seeding activity in brain and stomach of patients with Parkinson’s disease |
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