Purification and Partial Structural and Functional Characterization of Mouse Myelin/Oligodendrocyte Glycoprotein

Amiguet, Patrick; Gardinier, Minnetta V.; Zanetta, Jean‐Pierre; Matthieu, Jean‐Marie

doi:10.1111/j.1471-4159.1992.tb10040.x

Cited by 82 publications

(62 citation statements)

References 37 publications

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“…It has been reported that it is involved in the formation of the intraperiod line of myelin [25], and the results from the knockout and transgenic mice also suggest an important role of PLP in the interaction of oligodendrocyte and axon [25,26]. On the other hand, MOG is a quantitatively minor component of the CNS myelin that represents only ~0.05% of the total protein content of myelin [27]. It is located at the extracellular surface of myelin sheaths and oligodendrocyte processes and is believed to regulate oligodendrocyte microtubule stability and mediate interactions between the myelin and the immune system [28].…”

Section: Discussionmentioning

confidence: 99%

Redox regulation of cytokine-mediated inhibition of myelin gene expression in human primary oligodendrocytes

Jana

Pahan

2005

Free Radical Biology and Medicine

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Multiple sclerosis (MS) is a chronic autoimmune demyelinating disorder of the central nervous system (CNS) of unknown etiology. Several studies have shown that demyelination in MS is caused by proinflammatory mediators which are released by perivascular infiltrates and/or activated glial cells. To understand if proinflammatory mediators such as IL (interleukin)-1β and TNF (tumor necrosis factor)-α are capable of modulating the expression of myelin-specific genes, we investigated the effect of these cytokines on the expression of myelin basic protein (MBP), 2′,3′-cyclic nucleotide 3′-phosphodiesterase (CNPase), myelin oligodendrocyte glycoprotein (MOG), and proteolipid protein (PLP) in human primary oligodendrocytes. Interestingly, both IL-1β and TNF-α markedly inhibited the expression of MOG, CNPase, and PLP but not MBP, the effect that was blocked by antioxidants such as N-acetylcysteine (NAC) and pyrrolidine dithiocarbamate (PDTC). Consistently, oxidants and prooxidants like H 2 O 2 and diamide also markedly inhibited the expression of MOG, CNPase, and PLP. Furthermore, both IL-1β and TNF-α induced the production of H 2 O 2 . Taken together, these studies suggest that proinflammatory cytokines inhibit the expression of myelin genes in human primary oligodendrocytes through the alteration of cellular redox.

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Section: Discussionmentioning

confidence: 99%

Redox regulation of cytokine-mediated inhibition of myelin gene expression in human primary oligodendrocytes

Jana

Pahan

2005

Free Radical Biology and Medicine

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“…That this actually occurs in vivo has recently been shown for MBPp84 -102 in the context of HLA-DR2 (38). However, MBP is an abundant Ag in the CNS, whereas MOG comprises only 0.01-0.05% of the myelin mass (39). Therefore, it is not known whether it is processed and presented in the CNS, and by which type of APCs.…”

Section: Discussionmentioning

confidence: 99%

T Cell Epitopes of Human Myelin Oligodendrocyte Glycoprotein Identified in HLA-DR4 (DRB1*0401) Transgenic Mice Are Encephalitogenic and Are Presented by Human B Cells

Forsthuber

Shive

Wienhold

et al. 2001

The Journal of Immunology

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Myelin oligodendrocyte glycoprotein (MOG) is an Ag present in the myelin sheath of the CNS thought to be targeted by the autoimmune T cell response in multiple sclerosis (MS). In this study, we have for the first time characterized the T cell epitopes of human MOG restricted by HLA-DR4 (DRB1*0401), an MHC class II allele associated with MS in a subpopulation of patients. Using MHC binding algorithms, we have predicted MOG peptide binding to HLA-DR4 (DRB1*0401) and subsequently defined the in vivo T cell reactivity to overlapping MOG peptides by testing HLA-DR4 (DRB1*0401) transgenic mice immunized with recombinant human (rh)MOG. The data indicated that MOG peptide 97–108 (core 99–107, FFRDHSYQE) was the immunodominant HLA-DR4-restricted T cell epitope in vivo. This peptide has a high in vitro binding affinity for HLA-DR4 (DRB1*0401) and upon immunization induced severe experimental autoimmune encephalomyelitis in the HLA-DR4 transgenic mice. Interestingly, the same peptide was presented by human B cells expressing HLA-DR4 (DRB1*0401), suggesting a role for the identified MOG epitopes in the pathogenesis of human MS.

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“…It is exclusively localized on the outer surface of the myelin sheath, where it can be readily attacked by specific Ab mediating demyelination (5,6). In addition, the expression of MOG is restricted to the CNS, and it appears late during development of myelin (7)(8)(9)(10)(11).…”

mentioning

confidence: 99%

Development of Myelin Oligodendrocyte Glycoprotein Autoreactive Transgenic B Lymphocytes: Receptor Editing In Vivo After Encounter of a Self-Antigen Distinct from Myelin Oligodendrocyte Glycoprotein

Litzenburger

Blüthmann

Morales

et al. 2000

The Journal of Immunology

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We explored mechanisms involved in B cell self-tolerance against brain autoantigens in a double-transgenic mouse model carrying the Ig H-chain (introduced by gene replacement) and/or the L-chain κ (conventional transgenic) of the mAb 8.18C5, specific for the myelin oligodendrocyte glycoprotein (MOG). Previously, we demonstrated that B cells expressing solely the MOG-specific Ig H-chain differentiate without tolerogenic censure. We show now that double-transgenic (THκmog) B cells expressing transgenic Ig H- and L-chains are subjected to receptor editing. We show that in adult mice carrying both MOG-specific Ig H- and L-chains, the frequency of MOG-binding B cells is not higher than in mice expressing solely the transgenic Ig H-chain. In fact, in THκmog double-transgenic mice, the transgenic κmog L-chain was commonly replaced by endogenous L-chains, i.e., by receptor editing. In rearrangement-deficient RAG-2− mice, differentiation of THκmog B cells is blocked at an immature stage (defined by the B220lowIgMlowIgD− phenotype), reflecting interaction of the autoreactive B cells with a local self-determinant. The tolerogenic structure in the bone marrow is not classical MOG, because back-crossing THκmog mice into a MOG-deficient genetic background does not lead to an increase in the proportion of MOG-binding B cells. We propose that an as yet undefined self-Ag distinct from MOG cross-reacts with the THκmog B cell receptor and induces editing of the transgenic κmog L-chain in early immature B cells without affecting the pathogenic potential of the remaining MOG-specific B cells. This phenomenon represents a particular form of chain-specific split tolerance.

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Purification and Partial Structural and Functional Characterization of Mouse Myelin/Oligodendrocyte Glycoprotein

Cited by 82 publications

References 37 publications

Redox regulation of cytokine-mediated inhibition of myelin gene expression in human primary oligodendrocytes

Redox regulation of cytokine-mediated inhibition of myelin gene expression in human primary oligodendrocytes

T Cell Epitopes of Human Myelin Oligodendrocyte Glycoprotein Identified in HLA-DR4 (DRB1*0401) Transgenic Mice Are Encephalitogenic and Are Presented by Human B Cells

Development of Myelin Oligodendrocyte Glycoprotein Autoreactive Transgenic B Lymphocytes: Receptor Editing In Vivo After Encounter of a Self-Antigen Distinct from Myelin Oligodendrocyte Glycoprotein

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