Protein Aggregation in the Aging Retina
The age-related altered expression of neuron-related proteins as seen in other regions of the central nervous system is expected in the aging retina. Using immunohistochemical techniques, we characterized the distribution and aggregation of tau, βA4-amyloid, α-synuclein, and ubiquitin in human retin...
Gespeichert in:
| Veröffentlicht in: | Journal of neuropathology and experimental neurology 2011-01, Vol.70 (1), p.63-68 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 68 |
|---|---|
| container_issue | 1 |
| container_start_page | 63 |
| container_title | Journal of neuropathology and experimental neurology |
| container_volume | 70 |
| creator | Leger, François Fernagut, Pierre-Olivier Canron, Marie-Hélène Léoni, Sandy Vital, Claude Tison, François Bezard, Erwan Vital, Anne |
| description | The age-related altered expression of neuron-related proteins as seen in other regions of the central nervous system is expected in the aging retina. Using immunohistochemical techniques, we characterized the distribution and aggregation of tau, βA4-amyloid, α-synuclein, and ubiquitin in human retina obtained from 19 enucleated eyes of patients aged 49 to 87 years and correlated the findings with the ages. Using a phosphorylation-independent antibody, tau aggregates were observed within the cytoplasm of several photoreceptor cells, and there was a positive correlation between age and the number of tau-positive ganglionic cells. Tau deposits were immunonegative with a phosphorylation-dependent antibody. We did not observe βA4-amyloid in subretinal pigment epithelium deposits or in neuroepithelial layers. α-Synuclein and ubiquitin inclusions were found in the inner nuclear layer, and there was colocalization of these proteins. The proportion of patients displaying such α-synuclein and/or ubiquitin intracytoplasmic inclusions was significantly higher with aging. The presence of ubiquitin deposits within drusen was remarkable, but diffuse ubiquitin aggregates between the retinal pigment epithelium and Bruch membrane were also noticed. These results indicate that protein aggregation in the retina increases with aging and that tau, α-synuclein, and ubiquitin should be the subjects of future investigations. |
| doi_str_mv | 10.1097/NEN.0b013e31820376cc |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_853679137</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>853679137</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4546-54f952fd29d979ba3eac6ecb4770a63246485b3a824f116b7c9f4b9305f041b13</originalsourceid><addsrcrecordid>eNpdkVtLAzEQhYMoWqv_QKQI4tPWyXU2j1LqBaSK6HPIptl2dburyS7Ff2_EasGnYQ7fmRnOEHJCYUxB4-VsOhtDAZR7TnMGHJVzO2RApRSZkpjvkgEAYxkHpQ_IYYyvAKBBi31ywCiVyBEH5OIxtJ2vmtHVYhH8wnZV24xS2y19kqpmMXryXdXYI7JX2jr6400dkpfr6fPkNrt_uLmbXN1nTkihMilKLVk5Z3quUReWe-uUd4VABKs4E0rksuA2Z6KkVBXodCkKzUGWIGhB-ZBc_Mx9D-1H72NnVlV0vq5t49s-mlxyhZpyTOTZP_K17UOTjjO5QMbyHHmCxA_kQhtj8KV5D9XKhk9DwXzHaFKM5n-MyXa6md0XKz__M_3mloDzDWCjs3UZbOOquOU4CkCtt_vXbd35EN_qfu2DWXpbd0uTHgISkGUMKAWauuxbUvwL5dqH3A</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>847228873</pqid></control><display><type>article</type><title>Protein Aggregation in the Aging Retina</title><source>MEDLINE</source><source>Journals@Ovid Complete</source><source>Oxford University Press Journals All Titles (1996-Current)</source><source>EZB-FREE-00999 freely available EZB journals</source><creator>Leger, François ; Fernagut, Pierre-Olivier ; Canron, Marie-Hélène ; Léoni, Sandy ; Vital, Claude ; Tison, François ; Bezard, Erwan ; Vital, Anne</creator><creatorcontrib>Leger, François ; Fernagut, Pierre-Olivier ; Canron, Marie-Hélène ; Léoni, Sandy ; Vital, Claude ; Tison, François ; Bezard, Erwan ; Vital, Anne</creatorcontrib><description>The age-related altered expression of neuron-related proteins as seen in other regions of the central nervous system is expected in the aging retina. Using immunohistochemical techniques, we characterized the distribution and aggregation of tau, βA4-amyloid, α-synuclein, and ubiquitin in human retina obtained from 19 enucleated eyes of patients aged 49 to 87 years and correlated the findings with the ages. Using a phosphorylation-independent antibody, tau aggregates were observed within the cytoplasm of several photoreceptor cells, and there was a positive correlation between age and the number of tau-positive ganglionic cells. Tau deposits were immunonegative with a phosphorylation-dependent antibody. We did not observe βA4-amyloid in subretinal pigment epithelium deposits or in neuroepithelial layers. α-Synuclein and ubiquitin inclusions were found in the inner nuclear layer, and there was colocalization of these proteins. The proportion of patients displaying such α-synuclein and/or ubiquitin intracytoplasmic inclusions was significantly higher with aging. The presence of ubiquitin deposits within drusen was remarkable, but diffuse ubiquitin aggregates between the retinal pigment epithelium and Bruch membrane were also noticed. These results indicate that protein aggregation in the retina increases with aging and that tau, α-synuclein, and ubiquitin should be the subjects of future investigations.</description><identifier>ISSN: 0022-3069</identifier><identifier>EISSN: 1554-6578</identifier><identifier>DOI: 10.1097/NEN.0b013e31820376cc</identifier><identifier>PMID: 21157377</identifier><identifier>CODEN: JNENAD</identifier><language>eng</language><publisher>Hagerstown, MD: American Association of Neuropathologists, Inc</publisher><subject>Aged ; Aged, 80 and over ; Aging - metabolism ; Aging - pathology ; alpha-Synuclein - chemistry ; alpha-Synuclein - metabolism ; Biological and medical sciences ; Eye Proteins - chemistry ; Eye Proteins - metabolism ; Female ; Humans ; Injuries of the nervous system and the skull. Diseases due to physical agents ; Male ; Medical sciences ; Middle Aged ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - metabolism ; Neurology ; Retina - chemistry ; Retina - metabolism ; Retina - pathology ; tau Proteins - chemistry ; tau Proteins - metabolism ; Traumas. Diseases due to physical agents ; Ubiquitin - chemistry ; Ubiquitin - metabolism</subject><ispartof>Journal of neuropathology and experimental neurology, 2011-01, Vol.70 (1), p.63-68</ispartof><rights>2011 American Association of Neuropathologists, Inc</rights><rights>2015 INIST-CNRS</rights><rights>Copyright Lippincott Williams & Wilkins Jan 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4546-54f952fd29d979ba3eac6ecb4770a63246485b3a824f116b7c9f4b9305f041b13</citedby><cites>FETCH-LOGICAL-c4546-54f952fd29d979ba3eac6ecb4770a63246485b3a824f116b7c9f4b9305f041b13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4024,27923,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23740799$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21157377$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Leger, François</creatorcontrib><creatorcontrib>Fernagut, Pierre-Olivier</creatorcontrib><creatorcontrib>Canron, Marie-Hélène</creatorcontrib><creatorcontrib>Léoni, Sandy</creatorcontrib><creatorcontrib>Vital, Claude</creatorcontrib><creatorcontrib>Tison, François</creatorcontrib><creatorcontrib>Bezard, Erwan</creatorcontrib><creatorcontrib>Vital, Anne</creatorcontrib><title>Protein Aggregation in the Aging Retina</title><title>Journal of neuropathology and experimental neurology</title><addtitle>J Neuropathol Exp Neurol</addtitle><description>The age-related altered expression of neuron-related proteins as seen in other regions of the central nervous system is expected in the aging retina. Using immunohistochemical techniques, we characterized the distribution and aggregation of tau, βA4-amyloid, α-synuclein, and ubiquitin in human retina obtained from 19 enucleated eyes of patients aged 49 to 87 years and correlated the findings with the ages. Using a phosphorylation-independent antibody, tau aggregates were observed within the cytoplasm of several photoreceptor cells, and there was a positive correlation between age and the number of tau-positive ganglionic cells. Tau deposits were immunonegative with a phosphorylation-dependent antibody. We did not observe βA4-amyloid in subretinal pigment epithelium deposits or in neuroepithelial layers. α-Synuclein and ubiquitin inclusions were found in the inner nuclear layer, and there was colocalization of these proteins. The proportion of patients displaying such α-synuclein and/or ubiquitin intracytoplasmic inclusions was significantly higher with aging. The presence of ubiquitin deposits within drusen was remarkable, but diffuse ubiquitin aggregates between the retinal pigment epithelium and Bruch membrane were also noticed. These results indicate that protein aggregation in the retina increases with aging and that tau, α-synuclein, and ubiquitin should be the subjects of future investigations.</description><subject>Aged</subject><subject>Aged, 80 and over</subject><subject>Aging - metabolism</subject><subject>Aging - pathology</subject><subject>alpha-Synuclein - chemistry</subject><subject>alpha-Synuclein - metabolism</subject><subject>Biological and medical sciences</subject><subject>Eye Proteins - chemistry</subject><subject>Eye Proteins - metabolism</subject><subject>Female</subject><subject>Humans</subject><subject>Injuries of the nervous system and the skull. Diseases due to physical agents</subject><subject>Male</subject><subject>Medical sciences</subject><subject>Middle Aged</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurology</subject><subject>Retina - chemistry</subject><subject>Retina - metabolism</subject><subject>Retina - pathology</subject><subject>tau Proteins - chemistry</subject><subject>tau Proteins - metabolism</subject><subject>Traumas. Diseases due to physical agents</subject><subject>Ubiquitin - chemistry</subject><subject>Ubiquitin - metabolism</subject><issn>0022-3069</issn><issn>1554-6578</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><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>eNpdkVtLAzEQhYMoWqv_QKQI4tPWyXU2j1LqBaSK6HPIptl2dburyS7Ff2_EasGnYQ7fmRnOEHJCYUxB4-VsOhtDAZR7TnMGHJVzO2RApRSZkpjvkgEAYxkHpQ_IYYyvAKBBi31ywCiVyBEH5OIxtJ2vmtHVYhH8wnZV24xS2y19kqpmMXryXdXYI7JX2jr6400dkpfr6fPkNrt_uLmbXN1nTkihMilKLVk5Z3quUReWe-uUd4VABKs4E0rksuA2Z6KkVBXodCkKzUGWIGhB-ZBc_Mx9D-1H72NnVlV0vq5t49s-mlxyhZpyTOTZP_K17UOTjjO5QMbyHHmCxA_kQhtj8KV5D9XKhk9DwXzHaFKM5n-MyXa6md0XKz__M_3mloDzDWCjs3UZbOOquOU4CkCtt_vXbd35EN_qfu2DWXpbd0uTHgISkGUMKAWauuxbUvwL5dqH3A</recordid><startdate>201101</startdate><enddate>201101</enddate><creator>Leger, François</creator><creator>Fernagut, Pierre-Olivier</creator><creator>Canron, Marie-Hélène</creator><creator>Léoni, Sandy</creator><creator>Vital, Claude</creator><creator>Tison, François</creator><creator>Bezard, Erwan</creator><creator>Vital, Anne</creator><general>American Association of Neuropathologists, Inc</general><general>Lippincott Williams & Wilkins</general><general>Oxford University Press</general><scope>IQODW</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>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88G</scope><scope>88I</scope><scope>8AF</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>HCIFZ</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>S0X</scope><scope>7X8</scope></search><sort><creationdate>201101</creationdate><title>Protein Aggregation in the Aging Retina</title><author>Leger, François ; Fernagut, Pierre-Olivier ; Canron, Marie-Hélène ; Léoni, Sandy ; Vital, Claude ; Tison, François ; Bezard, Erwan ; Vital, Anne</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4546-54f952fd29d979ba3eac6ecb4770a63246485b3a824f116b7c9f4b9305f041b13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Aged</topic><topic>Aged, 80 and over</topic><topic>Aging - metabolism</topic><topic>Aging - pathology</topic><topic>alpha-Synuclein - chemistry</topic><topic>alpha-Synuclein - metabolism</topic><topic>Biological and medical sciences</topic><topic>Eye Proteins - chemistry</topic><topic>Eye Proteins - metabolism</topic><topic>Female</topic><topic>Humans</topic><topic>Injuries of the nervous system and the skull. Diseases due to physical agents</topic><topic>Male</topic><topic>Medical sciences</topic><topic>Middle Aged</topic><topic>Nerve Tissue Proteins - chemistry</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neurology</topic><topic>Retina - chemistry</topic><topic>Retina - metabolism</topic><topic>Retina - pathology</topic><topic>tau Proteins - chemistry</topic><topic>tau Proteins - metabolism</topic><topic>Traumas. Diseases due to physical agents</topic><topic>Ubiquitin - chemistry</topic><topic>Ubiquitin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Leger, François</creatorcontrib><creatorcontrib>Fernagut, Pierre-Olivier</creatorcontrib><creatorcontrib>Canron, Marie-Hélène</creatorcontrib><creatorcontrib>Léoni, Sandy</creatorcontrib><creatorcontrib>Vital, Claude</creatorcontrib><creatorcontrib>Tison, François</creatorcontrib><creatorcontrib>Bezard, Erwan</creatorcontrib><creatorcontrib>Vital, Anne</creatorcontrib><collection>Pascal-Francis</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>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Psychology Database (Alumni)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</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>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science 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 Central China</collection><collection>ProQuest Central Basic</collection><collection>SIRS Editorial</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of neuropathology and experimental neurology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Leger, François</au><au>Fernagut, Pierre-Olivier</au><au>Canron, Marie-Hélène</au><au>Léoni, Sandy</au><au>Vital, Claude</au><au>Tison, François</au><au>Bezard, Erwan</au><au>Vital, Anne</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein Aggregation in the Aging Retina</atitle><jtitle>Journal of neuropathology and experimental neurology</jtitle><addtitle>J Neuropathol Exp Neurol</addtitle><date>2011-01</date><risdate>2011</risdate><volume>70</volume><issue>1</issue><spage>63</spage><epage>68</epage><pages>63-68</pages><issn>0022-3069</issn><eissn>1554-6578</eissn><coden>JNENAD</coden><abstract>The age-related altered expression of neuron-related proteins as seen in other regions of the central nervous system is expected in the aging retina. Using immunohistochemical techniques, we characterized the distribution and aggregation of tau, βA4-amyloid, α-synuclein, and ubiquitin in human retina obtained from 19 enucleated eyes of patients aged 49 to 87 years and correlated the findings with the ages. Using a phosphorylation-independent antibody, tau aggregates were observed within the cytoplasm of several photoreceptor cells, and there was a positive correlation between age and the number of tau-positive ganglionic cells. Tau deposits were immunonegative with a phosphorylation-dependent antibody. We did not observe βA4-amyloid in subretinal pigment epithelium deposits or in neuroepithelial layers. α-Synuclein and ubiquitin inclusions were found in the inner nuclear layer, and there was colocalization of these proteins. The proportion of patients displaying such α-synuclein and/or ubiquitin intracytoplasmic inclusions was significantly higher with aging. The presence of ubiquitin deposits within drusen was remarkable, but diffuse ubiquitin aggregates between the retinal pigment epithelium and Bruch membrane were also noticed. These results indicate that protein aggregation in the retina increases with aging and that tau, α-synuclein, and ubiquitin should be the subjects of future investigations.</abstract><cop>Hagerstown, MD</cop><pub>American Association of Neuropathologists, Inc</pub><pmid>21157377</pmid><doi>10.1097/NEN.0b013e31820376cc</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-3069 |
| ispartof | Journal of neuropathology and experimental neurology, 2011-01, Vol.70 (1), p.63-68 |
| issn | 0022-3069 1554-6578 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_853679137 |
| source | MEDLINE; Journals@Ovid Complete; Oxford University Press Journals All Titles (1996-Current); EZB-FREE-00999 freely available EZB journals |
| subjects | Aged Aged, 80 and over Aging - metabolism Aging - pathology alpha-Synuclein - chemistry alpha-Synuclein - metabolism Biological and medical sciences Eye Proteins - chemistry Eye Proteins - metabolism Female Humans Injuries of the nervous system and the skull. Diseases due to physical agents Male Medical sciences Middle Aged Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - metabolism Neurology Retina - chemistry Retina - metabolism Retina - pathology tau Proteins - chemistry tau Proteins - metabolism Traumas. Diseases due to physical agents Ubiquitin - chemistry Ubiquitin - metabolism |
| title | Protein Aggregation in the Aging Retina |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-23T19%3A35%3A59IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Protein%20Aggregation%20in%20the%20Aging%20Retina&rft.jtitle=Journal%20of%20neuropathology%20and%20experimental%20neurology&rft.au=Leger,%20Fran%C3%A7ois&rft.date=2011-01&rft.volume=70&rft.issue=1&rft.spage=63&rft.epage=68&rft.pages=63-68&rft.issn=0022-3069&rft.eissn=1554-6578&rft.coden=JNENAD&rft_id=info:doi/10.1097/NEN.0b013e31820376cc&rft_dat=%3Cproquest_cross%3E853679137%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=847228873&rft_id=info:pmid/21157377&rfr_iscdi=true |