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Cited by 77Multiple Sclerosis Research StudiesNeuroinflammation and Neurodegeneration MechanismsNeurogenesis and neuroplasticity mechanisms

MHC class II exacerbates demyelination in vivo independently of T cells

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Hiremath, Meenaxi M., Chen, Vivian S., Suzuki, Kinuko, Ting, Jenny P.-Y., Matsushima, Glenn K.·2008·Journal of Neuroimmunology
DOI 10.1016/j.jneuroim.2008.06.034PMC PMC2913406
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Abstract

We have shown previously the importance of MHC class II for central nervous system remyelination; however, the function of MHC class II during cuprizone-induced demyelination has not been examined. Here, we show that I-A(beta)-/- mice exhibit significantly reduced inflammation and demyelination. RAG-1(1/1) mice are indistinguishable from controls, indicating T cells may not play a role. The role of MHC class II depends on an intact cytoplasmic tail that leads to the production of IL-1beta, TNF-alpha, and nitric oxide, and oligodendrocyte apoptosis. Thus, the function of MHC class II cytoplasmic tail appears to increase microglial proliferation and activation that exacerbates demyelination.

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  • The increased severity in EAE may be because of T-cell immune mechanisms that are not induced by cuprizone intoxication.

    “The increased severity in EAE may be because of T‐cell immune mechanisms that are not induced by cuprizone intoxication 2, 24.”

    From SJL Mice Exposed to Cuprizone Intoxication Reveal Strain and Gender Pattern Differences in Demyelination (2009) · cites this paper as [24]

    The Discussion (page not available) contrasts T-cell-mediated demyelination in EAE with the lack of T-cell infiltrates in the cuprizone model. The Results section, “T cells are not required for activating MHC II” (page not available), also finds that T cells do not play a significant role in cuprizone-induced demyelination. The paper does not report greater severity in EAE or attribute a severity difference to those immune mechanisms. (LLM, conf=0.83)

    Experimental — accuracy not yet measured

  • Historically, T-cells are not linked to demyelination following cuprizone treatment because loss of RAG-1 does not alter demyelination and T-cell accumulation in the corpus callosum.

    “Historically these cells are not linked to demyelination following cuprizone treatment because the loss of the V(D)J recombination activation gene-1 (RAG-1), which is critical for B- and T- lymphocyte generation [269], does not alter demyelination and T-cell accumulation in the corpus callosum [46, 270].”

    From Oligodendrocyte death and myelin loss in the cuprizone model: an updated overview of the intrinsic and extrinsic causes of cuprizone demyelination (2022) · cites this paper as [270]

    The Results section (‘T cells are not required for activating MHC II’; page unavailable) reports similar demyelination in cuprizone-treated RAG-1−/− and wild-type mice and concludes that T cells do not play a significant role. It does not report that RAG-1 loss leaves T-cell accumulation unchanged: the corpus callosum T-cell counts given are for wild-type and I-Aβ−/− mice, not a RAG-1 comparison. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • Remyelination is very robust in the cuprizone model and starts directly after demyelination is complete, irrespective of whether cuprizone is further fed or not.

    “Remyelination is very robust in the cuprizone model and starts directly after demyelination is complete, irrespective if cuprizone is further fed or not (Matsushima and Morell, 2001; Hiremath et al., 2008; Gudi et al., 2009).”

    From Glial response during cuprizone-induced de- and remyelination in the CNS: lessons learned (2014) · cites this paper as Hiremath et al., 2008

    The Materials and Methods section says total demyelination is usually observed after six weeks of cuprizone treatment, and the Discussion refers to remyelination at weeks 7 and 8. The paper does not establish that remyelination starts directly after demyelination, is very robust, or occurs irrespective of whether cuprizone feeding continues. Page numbers are unavailable in our copy. (LLM, conf=0.82)

    Experimental — accuracy not yet measured

  • Cuprizone-induced de- and remyelination are not mediated by B or T cells.

    “Overall, cuprizone-induced de- and remyelination are not mediated by B or T cells, as shown by the use of RAG −/− mice that lack lymphocytes (Arnett et al., 2001; Hiremath et al., 2008).”

    From Glial response during cuprizone-induced de- and remyelination in the CNS: lessons learned (2014) · cites this paper as Hiremath et al., 2008

    The Results section (‘T cells are not required for activating MHC II’; page unavailable) reports that cuprizone-treated RAG-1−/− mice, which lack B and T cells, had demyelination similar to wild-type mice. The Discussion says T cells do not play a role in remyelination, citing Arnett et al. (2001), but this paper does not report a RAG-1−/− remyelination comparison or establish the same conclusion for B cells during remyelination. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

  • The presence of T cells in the brains of progressive MS patients is clear, whereas their presence in the cuprizone model is controversial.

    “Although the presence of T cells in the brains of progressive MS patients is clear, this aspect is controversial in the cuprizone model.”

    From Cuprizone‐induced demyelination triggers a <scp>CD8</scp>‐pronounced T cell recruitment (2021) · cites this paper as Hiremath et al., 2008

    The Results (‘T cells are not required for activating MHC II’; page unavailable) say T cells are rarely detected in cuprizone-treated lesions, supporting the sentence’s focus on their presence in that model. The paper does not describe their presence as controversial; its Discussion instead emphasizes a lack of T-cell infiltrates. The Introduction also notes MS lesions without significant T-cell infiltration, but does not address progressive MS patients specifically. (LLM, conf=0.83)

    Experimental — accuracy not yet measured

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Cited by

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Authors
Hiremath, M. M., Chen, V. S., Suzuki, K., Ting, J. P.-Y., & Matsushima, G. K.
Affiliations
University of North Carolina at Chapel Hill (US)
Corresponding author
Matsushima, Glenn K.
ORCID
Venue
Journal of Neuroimmunology
Publisher
Elsevier BV
Published
2008-10
Volume
203
Issue
1
Pages
23-32
ISSN
0165-5728 (ISSN-L)
DOI
10.1016/j.jneuroim.2008.06.034
PMC
PMC2913406
OpenAlex
W2018226150
Cited by
77
References
7
Citations by year
2026: 1 · 2025: 1 · 2024: 3 · 2023: 7 · 2022: 6 · 2021: 5 · 2020: 4 · 2019: 9 · 2018: 5 · 2017: 6 · 2016: 2 · 2015: 5 · 2014: 3 · 2013: 2 · 2012: 4
FWCI
3.32
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Neuroimmunology (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
  • UNC Libraries
Funders
  • National Multiple Sclerosis Society
  • National Institutes of Health (5r29ns035372-05, RG7295, RG3898A)
  • National Institute of Allergy and Infectious Diseases (AI51770, R01AI051770, T32AI007273, R01AI050736, AI 07273, T32 AI07273)
  • National Institute of Neurological Disorders and Stroke (NS 24453, R01NS024453, NS-35372)
  • Eunice Kennedy Shriver National Institute of Child Health and Human Development (#HD03110, P30HD003110)
Topics
  • Health Sciences › Medicine › Pathology and Forensic Medicine › Multiple Sclerosis Research Studies
  • Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
  • Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
Keywords
MHC class II, demyelination, cuprizone, T cells, microglia, oligodendrocyte apoptosis, IL-1β, TNF-α, nitric oxide, neuroinflammation, remyelination
MeSH terms
Animals, Histocompatibility Antigens Class II, Chelating Agents, Cuprizone, Cytoplasm, Demyelinating Diseases, Male, Mice, Inbred C57BL, Mice, Mutant Strains, T-Lymphocytes, Tumor Necrosis Factor-alpha, Reactive Oxygen Species, Protein Structure, Tertiary, Microglia, Homeodomain Proteins, Mice, Interleukin-1beta

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