Human endogenous retrovirus glycoprotein-mediated induction of redox reactants causes oligodendrocyte death and demyelination - PubMed (original) (raw)
. 2004 Oct;7(10):1088-95.
doi: 10.1038/nn1319. Epub 2004 Sep 26.
Affiliations
- PMID: 15452578
- DOI: 10.1038/nn1319
Human endogenous retrovirus glycoprotein-mediated induction of redox reactants causes oligodendrocyte death and demyelination
Joseph M Antony et al. Nat Neurosci. 2004 Oct.
Abstract
Human endogenous retroviruses (HERVs) constitute 8% of the human genome and have been implicated in both health and disease. Increased HERV gene activity occurs in immunologically activated glia, although the consequences of HERV expression in the nervous system remain uncertain. Here, we report that the HERV-W encoded glycoprotein syncytin is upregulated in glial cells within acute demyelinating lesions of multiple sclerosis patients. Syncytin expression in astrocytes induced the release of redox reactants, which were cytotoxic to oligodendrocytes. Syncytin-mediated neuroinflammation and death of oligodendrocytes, with the ensuing neurobehavioral deficits, were prevented by the antioxidant ferulic acid in a mouse model of multiple sclerosis. Thus, syncytin's proinflammatory properties in the nervous system demonstrate a novel role for an endogenous retrovirus protein, which may be a target for therapeutic intervention.
Comment in
- Ancient viral protein enrages astrocytes in multiple sclerosis.
Mattson MP, Taub DD. Mattson MP, et al. Nat Neurosci. 2004 Oct;7(10):1021-3. doi: 10.1038/nn1004-1021. Nat Neurosci. 2004. PMID: 15452568 No abstract available.
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