DJ‐1 is present in a large molecular complex in human brain tissue and interacts with α‐synuclein
DJ‐1 is a ubiquitously expressed protein involved in various cellular processes including cell proliferation, RNA‐binding, and oxidative stress. Mutations that result in loss of DJ‐1 function lead to early onset parkinsonism in humans, and DJ‐1 protein is present in pathological lesions of several t...
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| Veröffentlicht in: | Journal of neurochemistry 2005-06, Vol.93 (6), p.1524-1532 |
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| container_title | Journal of neurochemistry |
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| creator | Meulener, Marc C. Graves, Charles L. Sampathu, Deepak M. Armstrong‐Gold, Cecilia E. Bonini, Nancy M. Giasson, Benoit I. |
| description | DJ‐1 is a ubiquitously expressed protein involved in various cellular processes including cell proliferation, RNA‐binding, and oxidative stress. Mutations that result in loss of DJ‐1 function lead to early onset parkinsonism in humans, and DJ‐1 protein is present in pathological lesions of several tauopathies and synucleinopathies. In order to further investigate the role of DJ‐1 in human neurodegenerative disease, we have generated novel polyclonal and monoclonal antibodies to human DJ‐1 protein. We have characterized these antibodies and confirmed the pathological co‐localization of DJ‐1 with other neurodegenerative disease‐associated proteins, as well as the decrease in DJ‐1 solubility in disease tissue. In addition, we report the presence of DJ‐1 in a large molecular complex (> 2000 kDa), and provide evidence for an interaction between endogenous DJ‐1 and α‐synuclein in normal and diseased tissue. These findings provide new avenues towards the study of DJ‐1 function and how loss of its activity may lead to parkinsonism. Furthermore, our results provide further evidence for the interplay between neurodegenerative disease‐associated proteins. |
| doi_str_mv | 10.1111/j.1471-4159.2005.03145.x |
| format | Article |
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Mutations that result in loss of DJ‐1 function lead to early onset parkinsonism in humans, and DJ‐1 protein is present in pathological lesions of several tauopathies and synucleinopathies. In order to further investigate the role of DJ‐1 in human neurodegenerative disease, we have generated novel polyclonal and monoclonal antibodies to human DJ‐1 protein. We have characterized these antibodies and confirmed the pathological co‐localization of DJ‐1 with other neurodegenerative disease‐associated proteins, as well as the decrease in DJ‐1 solubility in disease tissue. In addition, we report the presence of DJ‐1 in a large molecular complex (> 2000 kDa), and provide evidence for an interaction between endogenous DJ‐1 and α‐synuclein in normal and diseased tissue. These findings provide new avenues towards the study of DJ‐1 function and how loss of its activity may lead to parkinsonism. Furthermore, our results provide further evidence for the interplay between neurodegenerative disease‐associated proteins.</description><identifier>ISSN: 0022-3042</identifier><identifier>EISSN: 1471-4159</identifier><identifier>DOI: 10.1111/j.1471-4159.2005.03145.x</identifier><identifier>PMID: 15935068</identifier><identifier>CODEN: JONRA9</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>alpha-Synuclein ; Animals ; Antibodies - immunology ; Antibody Specificity ; Biological and medical sciences ; Brain - metabolism ; Brain - physiopathology ; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases ; DJ‐1 ; Drosophila ; Humans ; Inclusion Bodies - immunology ; Inclusion Bodies - metabolism ; Intracellular Signaling Peptides and Proteins ; Macromolecular Substances - metabolism ; Medical sciences ; Mice ; Molecular Sequence Data ; Molecular Weight ; Nerve Degeneration - metabolism ; Nerve Degeneration - physiopathology ; Nerve Tissue Proteins - metabolism ; Nervous system (semeiology, syndromes) ; Nervous system as a whole ; Neurology ; Oncogene Proteins - immunology ; Oncogene Proteins - metabolism ; Parkinson Disease - metabolism ; Parkinson Disease - physiopathology ; Parkinson's disease ; Protein Deglycase DJ-1 ; Sequence Homology, Amino Acid ; Solubility ; Synucleins ; tau Proteins - metabolism ; α‐synuclein</subject><ispartof>Journal of neurochemistry, 2005-06, Vol.93 (6), p.1524-1532</ispartof><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3975-959d8ee3da141ccd21d9a7d73beffe0e395052792808a7613801b8f1534e30153</citedby><cites>FETCH-LOGICAL-c3975-959d8ee3da141ccd21d9a7d73beffe0e395052792808a7613801b8f1534e30153</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1471-4159.2005.03145.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1471-4159.2005.03145.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,1427,27903,27904,45553,45554,46387,46811</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16821026$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15935068$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Meulener, Marc C.</creatorcontrib><creatorcontrib>Graves, Charles L.</creatorcontrib><creatorcontrib>Sampathu, Deepak M.</creatorcontrib><creatorcontrib>Armstrong‐Gold, Cecilia E.</creatorcontrib><creatorcontrib>Bonini, Nancy M.</creatorcontrib><creatorcontrib>Giasson, Benoit I.</creatorcontrib><title>DJ‐1 is present in a large molecular complex in human brain tissue and interacts with α‐synuclein</title><title>Journal of neurochemistry</title><addtitle>J Neurochem</addtitle><description>DJ‐1 is a ubiquitously expressed protein involved in various cellular processes including cell proliferation, RNA‐binding, and oxidative stress. Mutations that result in loss of DJ‐1 function lead to early onset parkinsonism in humans, and DJ‐1 protein is present in pathological lesions of several tauopathies and synucleinopathies. In order to further investigate the role of DJ‐1 in human neurodegenerative disease, we have generated novel polyclonal and monoclonal antibodies to human DJ‐1 protein. We have characterized these antibodies and confirmed the pathological co‐localization of DJ‐1 with other neurodegenerative disease‐associated proteins, as well as the decrease in DJ‐1 solubility in disease tissue. In addition, we report the presence of DJ‐1 in a large molecular complex (> 2000 kDa), and provide evidence for an interaction between endogenous DJ‐1 and α‐synuclein in normal and diseased tissue. These findings provide new avenues towards the study of DJ‐1 function and how loss of its activity may lead to parkinsonism. Furthermore, our results provide further evidence for the interplay between neurodegenerative disease‐associated proteins.</description><subject>alpha-Synuclein</subject><subject>Animals</subject><subject>Antibodies - immunology</subject><subject>Antibody Specificity</subject><subject>Biological and medical sciences</subject><subject>Brain - metabolism</subject><subject>Brain - physiopathology</subject><subject>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</subject><subject>DJ‐1</subject><subject>Drosophila</subject><subject>Humans</subject><subject>Inclusion Bodies - immunology</subject><subject>Inclusion Bodies - metabolism</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>Macromolecular Substances - metabolism</subject><subject>Medical sciences</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Nerve Degeneration - metabolism</subject><subject>Nerve Degeneration - physiopathology</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Nervous system (semeiology, syndromes)</subject><subject>Nervous system as a whole</subject><subject>Neurology</subject><subject>Oncogene Proteins - immunology</subject><subject>Oncogene Proteins - metabolism</subject><subject>Parkinson Disease - metabolism</subject><subject>Parkinson Disease - physiopathology</subject><subject>Parkinson's disease</subject><subject>Protein Deglycase DJ-1</subject><subject>Sequence Homology, Amino Acid</subject><subject>Solubility</subject><subject>Synucleins</subject><subject>tau Proteins - metabolism</subject><subject>α‐synuclein</subject><issn>0022-3042</issn><issn>1471-4159</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkM9u1DAQhy1ERZfCKyBf4JYwtuPEPnBAy9-qKhc4W15nQr1yksVO1N0bj8Cr8CI8RJ-kDruiV3yZkX7fzFgfIZRByfJ7vS1Z1bCiYlKXHECWIFgly_0jsvoXPCYrAM4LARU_J09T2gKwuqrZE3KeYyGhVivSvbu8-_mLUZ_oLmLCYaJ-oJYGG78j7ceAbs49dWO_C7hfwpu5twPdRJv7yac0I7VDm5MJo3VTord-uqF_fue96TDMLqAfnpGzzoaEz0_1gnz78P7r-lNx9eXj5_Xbq8IJ3chCS90qRNFaVjHnWs5abZu2ERvsOgQUWoLkjeYKlG1qJhSwjeqYFBUKyOWCvDru3cXxx4xpMr1PDkOwA45zMnWjQVRKZ1AdQRfHlCJ2Zhd9b-PBMDCLY7M1i0qzqDSLY_PXsdnn0RenG_Omx_Zh8CQ1Ay9PgE3Ohi7awfn0wNWKM-B15t4cuVsf8PDfHzCX1-ulE_ec25l0</recordid><startdate>200506</startdate><enddate>200506</enddate><creator>Meulener, Marc C.</creator><creator>Graves, Charles L.</creator><creator>Sampathu, Deepak M.</creator><creator>Armstrong‐Gold, Cecilia E.</creator><creator>Bonini, Nancy M.</creator><creator>Giasson, Benoit I.</creator><general>Blackwell Science Ltd</general><general>Blackwell</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>7X8</scope></search><sort><creationdate>200506</creationdate><title>DJ‐1 is present in a large molecular complex in human brain tissue and interacts with α‐synuclein</title><author>Meulener, Marc C. ; Graves, Charles L. ; Sampathu, Deepak M. ; Armstrong‐Gold, Cecilia E. ; Bonini, Nancy M. ; Giasson, Benoit I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3975-959d8ee3da141ccd21d9a7d73beffe0e395052792808a7613801b8f1534e30153</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>alpha-Synuclein</topic><topic>Animals</topic><topic>Antibodies - immunology</topic><topic>Antibody Specificity</topic><topic>Biological and medical sciences</topic><topic>Brain - metabolism</topic><topic>Brain - physiopathology</topic><topic>Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases</topic><topic>DJ‐1</topic><topic>Drosophila</topic><topic>Humans</topic><topic>Inclusion Bodies - immunology</topic><topic>Inclusion Bodies - metabolism</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>Macromolecular Substances - metabolism</topic><topic>Medical sciences</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Nerve Degeneration - metabolism</topic><topic>Nerve Degeneration - physiopathology</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Nervous system (semeiology, syndromes)</topic><topic>Nervous system as a whole</topic><topic>Neurology</topic><topic>Oncogene Proteins - immunology</topic><topic>Oncogene Proteins - metabolism</topic><topic>Parkinson Disease - metabolism</topic><topic>Parkinson Disease - physiopathology</topic><topic>Parkinson's disease</topic><topic>Protein Deglycase DJ-1</topic><topic>Sequence Homology, Amino Acid</topic><topic>Solubility</topic><topic>Synucleins</topic><topic>tau Proteins - metabolism</topic><topic>α‐synuclein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Meulener, Marc C.</creatorcontrib><creatorcontrib>Graves, Charles L.</creatorcontrib><creatorcontrib>Sampathu, Deepak M.</creatorcontrib><creatorcontrib>Armstrong‐Gold, Cecilia E.</creatorcontrib><creatorcontrib>Bonini, Nancy M.</creatorcontrib><creatorcontrib>Giasson, Benoit I.</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>MEDLINE - Academic</collection><jtitle>Journal of neurochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Meulener, Marc C.</au><au>Graves, Charles L.</au><au>Sampathu, Deepak M.</au><au>Armstrong‐Gold, Cecilia E.</au><au>Bonini, Nancy M.</au><au>Giasson, Benoit I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>DJ‐1 is present in a large molecular complex in human brain tissue and interacts with α‐synuclein</atitle><jtitle>Journal of neurochemistry</jtitle><addtitle>J Neurochem</addtitle><date>2005-06</date><risdate>2005</risdate><volume>93</volume><issue>6</issue><spage>1524</spage><epage>1532</epage><pages>1524-1532</pages><issn>0022-3042</issn><eissn>1471-4159</eissn><coden>JONRA9</coden><abstract>DJ‐1 is a ubiquitously expressed protein involved in various cellular processes including cell proliferation, RNA‐binding, and oxidative stress. Mutations that result in loss of DJ‐1 function lead to early onset parkinsonism in humans, and DJ‐1 protein is present in pathological lesions of several tauopathies and synucleinopathies. In order to further investigate the role of DJ‐1 in human neurodegenerative disease, we have generated novel polyclonal and monoclonal antibodies to human DJ‐1 protein. We have characterized these antibodies and confirmed the pathological co‐localization of DJ‐1 with other neurodegenerative disease‐associated proteins, as well as the decrease in DJ‐1 solubility in disease tissue. In addition, we report the presence of DJ‐1 in a large molecular complex (> 2000 kDa), and provide evidence for an interaction between endogenous DJ‐1 and α‐synuclein in normal and diseased tissue. These findings provide new avenues towards the study of DJ‐1 function and how loss of its activity may lead to parkinsonism. Furthermore, our results provide further evidence for the interplay between neurodegenerative disease‐associated proteins.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>15935068</pmid><doi>10.1111/j.1471-4159.2005.03145.x</doi><tpages>9</tpages></addata></record> |
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| ispartof | Journal of neurochemistry, 2005-06, Vol.93 (6), p.1524-1532 |
| issn | 0022-3042 1471-4159 |
| language | eng |
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| source | MEDLINE; Wiley Online Library; Wiley Online Library Journals Frontfile Complete; IngentaConnect Free/Open Access Journals; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | alpha-Synuclein Animals Antibodies - immunology Antibody Specificity Biological and medical sciences Brain - metabolism Brain - physiopathology Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases DJ‐1 Drosophila Humans Inclusion Bodies - immunology Inclusion Bodies - metabolism Intracellular Signaling Peptides and Proteins Macromolecular Substances - metabolism Medical sciences Mice Molecular Sequence Data Molecular Weight Nerve Degeneration - metabolism Nerve Degeneration - physiopathology Nerve Tissue Proteins - metabolism Nervous system (semeiology, syndromes) Nervous system as a whole Neurology Oncogene Proteins - immunology Oncogene Proteins - metabolism Parkinson Disease - metabolism Parkinson Disease - physiopathology Parkinson's disease Protein Deglycase DJ-1 Sequence Homology, Amino Acid Solubility Synucleins tau Proteins - metabolism α‐synuclein |
| title | DJ‐1 is present in a large molecular complex in human brain tissue and interacts with α‐synuclein |
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