Full metadata record
DC Field | Value | Language |
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dc.creator | Lalive, P.H. (Patrice H.) | - |
dc.creator | Menge, T. (Til) | - |
dc.creator | Delarasse, C. (Cecile) | - |
dc.creator | Gaspera, B.D. (Bruno Della) | - |
dc.creator | Pham-Dinh, D. (Danielle) | - |
dc.creator | Villoslada, P. (Pablo) | - |
dc.creator | Budingen, H.C. (H.C.) von | - |
dc.creator | Genain, C.P. (Claude P.) | - |
dc.date.accessioned | 2014-08-30T17:12:30Z | - |
dc.date.available | 2014-08-30T17:12:30Z | - |
dc.date.issued | 2006 | - |
dc.identifier.citation | Lalive P H, Menge T, Delarasse C, Gaspera B D, Pham-Dinh D, Villoslada P, Büdingen H C, Genain C P. Antibodies to native myelin oligodendrocyte glycoprotein are serologic markers of early inflammation in multiple sclerosis. Proc Natl Acad Sci U S A. 2006 February 14; 103(7): 2280–2285 | es_ES |
dc.identifier.issn | 1091-6490 | - |
dc.identifier.uri | https://hdl.handle.net/10171/36416 | - |
dc.description.abstract | Myelin oligodendrocyte glycoprotein (MOG) is an integral membrane protein expressed in CNS oligodendrocytes and outermost myelin lamellae. Anti-MOG Abs cause myelin destruction (demyelination) in animal models of multiple sclerosis (MS); however, such pathogenic Abs have not yet been characterized in humans. Here, a method that specifically detects IgG binding to human MOG in its native, membrane-embedded conformation on MOG-transfected mammalian cells was used to evaluate the significance of these auto Abs. Compared with healthy controls, native MOG-specific IgGs were most frequently found in serum of clinically isolated syndromes (P < 0.001) and relapsing-remitting MS (P < 0.01), only marginally in secondary progressive MS (P < 0.05), and not at all in primary progressive MS. We demonstrate that epitopes exposed in this cell-based assay are different from those exposed on the refolded, extracellular domain of human recombinant MOG tested by solid-phase ELISA. In marmoset monkeys induced to develop MS-like CNS inflammatory demyelination, IgG reactivity against the native membrane-bound MOG is always detected before clinical onset of disease (P < 0.0001), unlike that against other myelin constituents. We conclude that (i) epitopes displayed on native, glycosylated MOG expressed in vivo are early targets for pathogenic Abs; (ii) these Abs, which are not detected in solid-phase assays, might be the ones to play a pathogenic role in early MS with predominant inflammatory activity; and (iii) the cell-based assay provides a practical serologic marker for early detection of CNS autoimmune demyelination including its preclinical stage at least in the primate MS model | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | National Academy of Science | es_ES |
dc.rights | info:eu-repo/semantics/openAccess | es_ES |
dc.subject | Antibodies | es_ES |
dc.subject | Multiple sclerosis | es_ES |
dc.subject | Oligodendrocyte glycoprotein | es_ES |
dc.title | Antibodies to native myelin oligodendrocyte glycoprotein are serologic markers of early inflammation in multiple sclerosis | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.identifier.doi | http://dx.doi.org/10.1073/pnas.0510672103 | es_ES |
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