Decreased cell surface prion protein in mouse models of prion disease
Transmissible spongiform encephalopathies are infectious neurodegenerative diseases caused by prions, composed of ordered aggregates of misfolded cellular prion protein. Neural antigen density of prion protein, Thy-1 and glial fibrillary acidic protein was analyzed using flow cytometry of dissociate...
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| Veröffentlicht in: | Neuroreport 2007-01, Vol.18 (1), p.1-6 |
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| creator | Griffin, Jennifer K Terry, Linda A Jackman, Roy Yousefi, Masoud Cashman, Neil R |
| description | Transmissible spongiform encephalopathies are infectious neurodegenerative diseases caused by prions, composed of ordered aggregates of misfolded cellular prion protein. Neural antigen density of prion protein, Thy-1 and glial fibrillary acidic protein was analyzed using flow cytometry of dissociated mouse brain cells after inoculation with mouse-adapted transmissible spongiform encephalopathy agents. Transmissible spongiform encephalopathy gliosis was demonstrated by increased intracellular immunoreactivity for glial fibrillary acidic protein compared with controls. Immunoreactivity for cell surface prion protein was reduced 2.8–3.8-fold compared with control brain cells, whereas surface Thy-1 protein was reduced 1.5–4-fold. Double-staining protocols revealed loss of brain cells highly immunoreactive for prion protein and Thy-1, with a preferential reduction of prion protein, suggesting that prion protein expression, trafficking or consumption may be affected early in disease. |
| doi_str_mv | 10.1097/01.wnr.0000239967.06438.21 |
| format | Article |
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Neural antigen density of prion protein, Thy-1 and glial fibrillary acidic protein was analyzed using flow cytometry of dissociated mouse brain cells after inoculation with mouse-adapted transmissible spongiform encephalopathy agents. Transmissible spongiform encephalopathy gliosis was demonstrated by increased intracellular immunoreactivity for glial fibrillary acidic protein compared with controls. Immunoreactivity for cell surface prion protein was reduced 2.8–3.8-fold compared with control brain cells, whereas surface Thy-1 protein was reduced 1.5–4-fold. 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Neural antigen density of prion protein, Thy-1 and glial fibrillary acidic protein was analyzed using flow cytometry of dissociated mouse brain cells after inoculation with mouse-adapted transmissible spongiform encephalopathy agents. Transmissible spongiform encephalopathy gliosis was demonstrated by increased intracellular immunoreactivity for glial fibrillary acidic protein compared with controls. Immunoreactivity for cell surface prion protein was reduced 2.8–3.8-fold compared with control brain cells, whereas surface Thy-1 protein was reduced 1.5–4-fold. Double-staining protocols revealed loss of brain cells highly immunoreactive for prion protein and Thy-1, with a preferential reduction of prion protein, suggesting that prion protein expression, trafficking or consumption may be affected early in disease.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Degenerative and inherited degenerative diseases of the nervous system. 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Prion diseases</subject><subject>Disease Models, Animal</subject><subject>Gene Expression Regulation</subject><subject>Human viral diseases</subject><subject>Infectious diseases</subject><subject>Medical sciences</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Neurology</subject><subject>Neurons - pathology</subject><subject>Prion Diseases - metabolism</subject><subject>Prion Diseases - pathology</subject><subject>Prion Proteins</subject><subject>Prions - metabolism</subject><subject>Protein Transport</subject><subject>Thy-1 Antigens - metabolism</subject><subject>Viral diseases</subject><subject>Viral diseases of the nervous system</subject><issn>0959-4965</issn><issn>1473-558X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LxDAQhoMouq7-BSmC3lon34038RsELx68hTSdYrXbarJl8d-b3S3s0RAmEJ535p2XkHMKBQWjr4AWqz4UkA7jxihdgBK8LBjdIzMqNM-lLN_3yQyMNLkwSh6R4xg_E2-AlofkiGomTSnpjNzfoQ_oItaZx67L4hga5zH7Du3Qpzosse2zdBfDGDHVGruYDc0E1G1ci0_IQeO6iKfTOydvD_dvt0_5y-vj8-3NS-4F4zSnyviqclwCNlp5dEy4unTgvUCha684Q0a55Dot4AxyyYzHqnG8qqU3fE4ut22Tr58R49Iu2ri27XpM9qwqTdJS8S_IQGotzRq83oI-DDEGbGzaa-HCr6Vg12FboDaFbXdh203YNvmck7NpylgtsN5Jp3QTcDEBLnrXNcH1vo07rhTKpKaJE1tuNXRLDPGrG1cY7Ae6bvmxGU21VDkD0EChhHzzxf8AcFGYlw</recordid><startdate>20070108</startdate><enddate>20070108</enddate><creator>Griffin, Jennifer K</creator><creator>Terry, Linda A</creator><creator>Jackman, Roy</creator><creator>Yousefi, Masoud</creator><creator>Cashman, Neil R</creator><general>Lippincott Williams & Wilkins, Inc</general><general>Lippincott Williams and Wilkins</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>7TK</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20070108</creationdate><title>Decreased cell surface prion protein in mouse models of prion disease</title><author>Griffin, Jennifer K ; Terry, Linda A ; Jackman, Roy ; Yousefi, Masoud ; Cashman, Neil R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4231-169cbba350ef76cea24ad8a0cc4e47dc632e213537558a9e3529cebfa3bd5c93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Degenerative and inherited degenerative diseases of the nervous system. 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Prion diseases</topic><topic>Disease Models, Animal</topic><topic>Gene Expression Regulation</topic><topic>Human viral diseases</topic><topic>Infectious diseases</topic><topic>Medical sciences</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Neurology</topic><topic>Neurons - pathology</topic><topic>Prion Diseases - metabolism</topic><topic>Prion Diseases - pathology</topic><topic>Prion Proteins</topic><topic>Prions - metabolism</topic><topic>Protein Transport</topic><topic>Thy-1 Antigens - metabolism</topic><topic>Viral diseases</topic><topic>Viral diseases of the nervous system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Griffin, Jennifer K</creatorcontrib><creatorcontrib>Terry, Linda A</creatorcontrib><creatorcontrib>Jackman, Roy</creatorcontrib><creatorcontrib>Yousefi, Masoud</creatorcontrib><creatorcontrib>Cashman, Neil R</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>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Neuroreport</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Griffin, Jennifer K</au><au>Terry, Linda A</au><au>Jackman, Roy</au><au>Yousefi, Masoud</au><au>Cashman, Neil R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Decreased cell surface prion protein in mouse models of prion disease</atitle><jtitle>Neuroreport</jtitle><addtitle>Neuroreport</addtitle><date>2007-01-08</date><risdate>2007</risdate><volume>18</volume><issue>1</issue><spage>1</spage><epage>6</epage><pages>1-6</pages><issn>0959-4965</issn><eissn>1473-558X</eissn><abstract>Transmissible spongiform encephalopathies are infectious neurodegenerative diseases caused by prions, composed of ordered aggregates of misfolded cellular prion protein. Neural antigen density of prion protein, Thy-1 and glial fibrillary acidic protein was analyzed using flow cytometry of dissociated mouse brain cells after inoculation with mouse-adapted transmissible spongiform encephalopathy agents. Transmissible spongiform encephalopathy gliosis was demonstrated by increased intracellular immunoreactivity for glial fibrillary acidic protein compared with controls. Immunoreactivity for cell surface prion protein was reduced 2.8–3.8-fold compared with control brain cells, whereas surface Thy-1 protein was reduced 1.5–4-fold. 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| subjects | Animals Biological and medical sciences Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases Disease Models, Animal Gene Expression Regulation Human viral diseases Infectious diseases Medical sciences Mice Mice, Inbred C57BL Neurology Neurons - pathology Prion Diseases - metabolism Prion Diseases - pathology Prion Proteins Prions - metabolism Protein Transport Thy-1 Antigens - metabolism Viral diseases Viral diseases of the nervous system |
| title | Decreased cell surface prion protein in mouse models of prion disease |
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