Proteomic Analysis of Demyelinated and Remyelinating Brain Tissue following Dietary Cuprizone Administration
Cuprizone intoxication is a commonly used model of demyelination that allows the temporal separation of demyelination and remyelination. The underlying biochemical alterations leading to demyelination, using this model, remain unclear and may be multifold. Analysis of proteomic changes within the br...
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| Veröffentlicht in: | Journal of molecular neuroscience 2010-10, Vol.42 (2), p.210-225 |
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| creator | Werner, Sean R. Saha, Joy K. Broderick, Carol L. Zhen, Eugene Y. Higgs, Richard E. Duffin, Kevin L. Smith, Rosamund C. |
| description | Cuprizone intoxication is a commonly used model of demyelination that allows the temporal separation of demyelination and remyelination. The underlying biochemical alterations leading to demyelination, using this model, remain unclear and may be multifold. Analysis of proteomic changes within the brains of cuprizone-exposed animals may help elucidate key cellular processes. In the current study, we report the results of the liquid chromatography tandem mass spectrometry analysis of total protein from the brain hemispheres of control and toxin-exposed mice at 6 weeks of exposure and after 3 and 6 weeks of recovery to identify protein changes during the remyelination phase. We found that at 6 weeks of cuprizone exposure, myelin proteins were reduced compared to controls and increased throughout the course of recovery, as expected. In contrast, other protein groups, such as proteins related to mitochondrial function, were increased at 6 weeks of treatment compared to untreated controls and returned toward control levels following withdrawal of toxin. These results suggest that a global proteomic analysis of the brain tissue of cuprizone-treated mice can identify changes related to the demyelination/remyelination process. |
| doi_str_mv | 10.1007/s12031-010-9354-9 |
| format | Article |
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The underlying biochemical alterations leading to demyelination, using this model, remain unclear and may be multifold. Analysis of proteomic changes within the brains of cuprizone-exposed animals may help elucidate key cellular processes. In the current study, we report the results of the liquid chromatography tandem mass spectrometry analysis of total protein from the brain hemispheres of control and toxin-exposed mice at 6 weeks of exposure and after 3 and 6 weeks of recovery to identify protein changes during the remyelination phase. We found that at 6 weeks of cuprizone exposure, myelin proteins were reduced compared to controls and increased throughout the course of recovery, as expected. In contrast, other protein groups, such as proteins related to mitochondrial function, were increased at 6 weeks of treatment compared to untreated controls and returned toward control levels following withdrawal of toxin. These results suggest that a global proteomic analysis of the brain tissue of cuprizone-treated mice can identify changes related to the demyelination/remyelination process.</description><identifier>ISSN: 0895-8696</identifier><identifier>EISSN: 1559-1166</identifier><identifier>DOI: 10.1007/s12031-010-9354-9</identifier><identifier>PMID: 20401640</identifier><language>eng</language><publisher>New York: Humana Press Inc</publisher><subject>Administration, Oral ; Animals ; Behavior, Animal - drug effects ; Behavior, Animal - physiology ; Biomedical and Life Sciences ; Biomedicine ; Brain - drug effects ; Brain - pathology ; Brain - physiology ; Brain research ; Cell Biology ; Cerebral hemispheres ; Chromatography ; cuprizone ; Cuprizone - toxicity ; Demyelinating Diseases - chemically induced ; Demyelinating Diseases - metabolism ; Demyelinating Diseases - pathology ; Demyelination ; Diet ; Disease Models, Animal ; Food, Formulated - adverse effects ; Gene expression ; Intoxication ; Laboratories ; Liquid chromatography ; Male ; Mass spectrometry ; Mass spectroscopy ; Mice ; Mice, Inbred C57BL ; Mitochondria ; Monoamine Oxidase Inhibitors - toxicity ; Multiple sclerosis ; Myelin ; Myelination ; Nerve Fibers, Myelinated - drug effects ; Nerve Fibers, Myelinated - pathology ; Nerve Fibers, Myelinated - physiology ; Nerve Regeneration - drug effects ; Nerve Regeneration - physiology ; Nervous system ; Neurochemistry ; Neurology ; Neurosciences ; Neurotoxins - toxicity ; Proteins ; Proteomics ; Proteomics - methods ; Recovery of Function - physiology ; Scientific imaging ; Toxins</subject><ispartof>Journal of molecular neuroscience, 2010-10, Vol.42 (2), p.210-225</ispartof><rights>Springer Science+Business Media, LLC 2010</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c468t-b12680f61c3cf4b7a222560a5458227f6ead63e9442a849de36e6e2344373a8c3</citedby><cites>FETCH-LOGICAL-c468t-b12680f61c3cf4b7a222560a5458227f6ead63e9442a849de36e6e2344373a8c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12031-010-9354-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12031-010-9354-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20401640$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Werner, Sean R.</creatorcontrib><creatorcontrib>Saha, Joy K.</creatorcontrib><creatorcontrib>Broderick, Carol L.</creatorcontrib><creatorcontrib>Zhen, Eugene Y.</creatorcontrib><creatorcontrib>Higgs, Richard E.</creatorcontrib><creatorcontrib>Duffin, Kevin L.</creatorcontrib><creatorcontrib>Smith, Rosamund C.</creatorcontrib><title>Proteomic Analysis of Demyelinated and Remyelinating Brain Tissue following Dietary Cuprizone Administration</title><title>Journal of molecular neuroscience</title><addtitle>J Mol Neurosci</addtitle><addtitle>J Mol Neurosci</addtitle><description>Cuprizone intoxication is a commonly used model of demyelination that allows the temporal separation of demyelination and remyelination. The underlying biochemical alterations leading to demyelination, using this model, remain unclear and may be multifold. Analysis of proteomic changes within the brains of cuprizone-exposed animals may help elucidate key cellular processes. In the current study, we report the results of the liquid chromatography tandem mass spectrometry analysis of total protein from the brain hemispheres of control and toxin-exposed mice at 6 weeks of exposure and after 3 and 6 weeks of recovery to identify protein changes during the remyelination phase. We found that at 6 weeks of cuprizone exposure, myelin proteins were reduced compared to controls and increased throughout the course of recovery, as expected. In contrast, other protein groups, such as proteins related to mitochondrial function, were increased at 6 weeks of treatment compared to untreated controls and returned toward control levels following withdrawal of toxin. These results suggest that a global proteomic analysis of the brain tissue of cuprizone-treated mice can identify changes related to the demyelination/remyelination process.</description><subject>Administration, Oral</subject><subject>Animals</subject><subject>Behavior, Animal - drug effects</subject><subject>Behavior, Animal - physiology</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Brain - drug effects</subject><subject>Brain - pathology</subject><subject>Brain - physiology</subject><subject>Brain research</subject><subject>Cell Biology</subject><subject>Cerebral hemispheres</subject><subject>Chromatography</subject><subject>cuprizone</subject><subject>Cuprizone - toxicity</subject><subject>Demyelinating Diseases - chemically induced</subject><subject>Demyelinating Diseases - metabolism</subject><subject>Demyelinating Diseases - pathology</subject><subject>Demyelination</subject><subject>Diet</subject><subject>Disease Models, Animal</subject><subject>Food, Formulated - adverse effects</subject><subject>Gene expression</subject><subject>Intoxication</subject><subject>Laboratories</subject><subject>Liquid chromatography</subject><subject>Male</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Mitochondria</subject><subject>Monoamine Oxidase Inhibitors - toxicity</subject><subject>Multiple sclerosis</subject><subject>Myelin</subject><subject>Myelination</subject><subject>Nerve Fibers, Myelinated - drug effects</subject><subject>Nerve Fibers, Myelinated - pathology</subject><subject>Nerve Fibers, Myelinated - physiology</subject><subject>Nerve Regeneration - drug effects</subject><subject>Nerve Regeneration - physiology</subject><subject>Nervous system</subject><subject>Neurochemistry</subject><subject>Neurology</subject><subject>Neurosciences</subject><subject>Neurotoxins - toxicity</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Proteomics - 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The underlying biochemical alterations leading to demyelination, using this model, remain unclear and may be multifold. Analysis of proteomic changes within the brains of cuprizone-exposed animals may help elucidate key cellular processes. In the current study, we report the results of the liquid chromatography tandem mass spectrometry analysis of total protein from the brain hemispheres of control and toxin-exposed mice at 6 weeks of exposure and after 3 and 6 weeks of recovery to identify protein changes during the remyelination phase. We found that at 6 weeks of cuprizone exposure, myelin proteins were reduced compared to controls and increased throughout the course of recovery, as expected. In contrast, other protein groups, such as proteins related to mitochondrial function, were increased at 6 weeks of treatment compared to untreated controls and returned toward control levels following withdrawal of toxin. These results suggest that a global proteomic analysis of the brain tissue of cuprizone-treated mice can identify changes related to the demyelination/remyelination process.</abstract><cop>New York</cop><pub>Humana Press Inc</pub><pmid>20401640</pmid><doi>10.1007/s12031-010-9354-9</doi><tpages>16</tpages></addata></record> |
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| subjects | Administration, Oral Animals Behavior, Animal - drug effects Behavior, Animal - physiology Biomedical and Life Sciences Biomedicine Brain - drug effects Brain - pathology Brain - physiology Brain research Cell Biology Cerebral hemispheres Chromatography cuprizone Cuprizone - toxicity Demyelinating Diseases - chemically induced Demyelinating Diseases - metabolism Demyelinating Diseases - pathology Demyelination Diet Disease Models, Animal Food, Formulated - adverse effects Gene expression Intoxication Laboratories Liquid chromatography Male Mass spectrometry Mass spectroscopy Mice Mice, Inbred C57BL Mitochondria Monoamine Oxidase Inhibitors - toxicity Multiple sclerosis Myelin Myelination Nerve Fibers, Myelinated - drug effects Nerve Fibers, Myelinated - pathology Nerve Fibers, Myelinated - physiology Nerve Regeneration - drug effects Nerve Regeneration - physiology Nervous system Neurochemistry Neurology Neurosciences Neurotoxins - toxicity Proteins Proteomics Proteomics - methods Recovery of Function - physiology Scientific imaging Toxins |
| title | Proteomic Analysis of Demyelinated and Remyelinating Brain Tissue following Dietary Cuprizone Administration |
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