Abstract
Antibodies to myelin oligodendrocyte glycoprotein (MOG) have been implicated in Multiple Sclerosis demyelination through activation of complement and/or macrophage-effector processes. We presented a novel mechanism, whereby MOG on oligodendrocytes, when cross-linked with anti-MOG and secondary antibody resulted in its repartitioning into lipid rafts, and changes in protein phosphorylation and morphology. Here, we show that similar events occur when anti-MOG is cross-linked with Fc receptors (FcRs) present on microglia but not with complement. These results indicate that FcRs are endogenous antigen/antibody cross-linkers in vitro, suggesting that FcRs could be physiologically relevant in vivo and possible targets for therapy in Multiple Sclerosis.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antigens, CD / metabolism
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Cell Death
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Cells, Cultured
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Cross-Linking Reagents / chemistry*
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Cross-Linking Reagents / pharmacology
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Immunoglobulin G / metabolism*
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Immunoglobulin G / pharmacology
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Myelin Basic Protein / metabolism
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Myelin Proteins
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Myelin-Associated Glycoprotein / immunology*
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Myelin-Oligodendrocyte Glycoprotein
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Oligodendroglia / drug effects
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Oligodendroglia / metabolism*
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Rats
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Receptors, Fc / physiology*
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Time Factors
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beta-Cyclodextrins / pharmacology
Substances
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Antigens, CD
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Cross-Linking Reagents
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Immunoglobulin G
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Mog protein, rat
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Myelin Basic Protein
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Myelin Proteins
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Myelin-Associated Glycoprotein
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Myelin-Oligodendrocyte Glycoprotein
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Receptors, Fc
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beta-Cyclodextrins
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methyl-beta-cyclodextrin