Cellular and Molecular Mechanism of Neuroimmunological Diseases

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cells of the Nervous System".

Deadline for manuscript submissions: closed (15 June 2023) | Viewed by 2269

Special Issue Editor


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Guest Editor
School of Medicine and Health Sciences, The George Washington University, Washington, DC, USA
Interests: neural development/stem cells; myelin repair; spinal cord injury

Special Issue Information

Dear Colleagues, 

The impact of the immune system on the development of neurological diseases such as Multiple Sclerosis and Myasthenia Gravis has long been known. What has more recently become clear is the critical role of the immune system in disease progression in a wide range of neurological diseases that are not identified as classical neuroimmunological diseases. For example, conditions such as Alzheimer’s disease, Parkinson’s disease, ALS, stroke and neuropathic pain all have a significant engagement of the immune system. In most conditions the impact of the immune system is considered to be detrimental to recovery, however in certain circumstances such as where cellular debris inhibits recovery, removal of debris by cells of the immune system may actually enhance recovery. Understanding such interplay between the systemic and innate immune systems with cells of the nervous system is critical for harnessing the positive and mitigating the negative effects of such interactions.

The aim of this special issue is to highlight the similarities and differences in how neuroimmune interactions contribute to the pathogenesis of a range of neurological conditions with the hope that such knowledge will trigger new therapeutic directions. 

Prof. Dr. Robert H. Miller
Guest Editor

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Keywords

  • neurodegenerative diseases
  • neuro-immune interactions
  • CNS injury
  • neural repair

Published Papers (1 paper)

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Research

24 pages, 19238 KiB  
Article
TMEM106B Puncta Is Increased in Multiple Sclerosis Plaques, and Reduced Protein in Mice Results in Delayed Lipid Clearance Following CNS Injury
by Bridget Shafit-Zagardo, Simone Sidoli, James E. Goldman, Juwen C. DuBois, John R. Corboy, Stephen M. Strittmatter, Hillary Guzik, Ukuemi Edema, Anita G. Arackal, Yair M. Botbol, Emilio Merheb, Rashed M. Nagra and Sarah Graff
Cells 2023, 12(13), 1734; https://doi.org/10.3390/cells12131734 - 27 Jun 2023
Cited by 2 | Viewed by 1853
Abstract
During inflammatory, demyelinating diseases such as multiple sclerosis (MS), inflammation and axonal damage are prevalent early in the course. Axonal damage includes swelling, defects in transport, and failure to clear damaged intracellular proteins, all of which affect recovery and compromise neuronal integrity. The [...] Read more.
During inflammatory, demyelinating diseases such as multiple sclerosis (MS), inflammation and axonal damage are prevalent early in the course. Axonal damage includes swelling, defects in transport, and failure to clear damaged intracellular proteins, all of which affect recovery and compromise neuronal integrity. The clearance of damaged cell components is important to maintain normal turnover and restore homeostasis. In this study, we used mass spectrometry to identify insoluble proteins within high-speed/mercaptoethanol/sarcosyl-insoluble pellets from purified white matter plaques isolated from the brains of individuals with relapsing–remitting MS (RRMS). We determined that the transmembrane protein 106B (TMEM106B), normally lysosome-associated, is insoluble in RRMS plaques relative to normal-appearing white matter from individuals with Alzheimer’s disease and non-neurologic controls. Relative to wild-type mice, hypomorphic mice with a reduction in TMEM106B have increased axonal damage and lipid droplet accumulation in the spinal cord following myelin-oligodendrocyte-glycoprotein-induced experimental autoimmune encephalomyelitis. Additionally, the corpora callosa from cuprizone-challenged hypomorphic mice fail to clear lipid droplets efficiently during remyelination, suggesting that when TMEM106B is compromised, protein and lipid clearance by the lysosome is delayed. As TMEM106B contains putative lipid- and LC3-binding sites, further exploration of these sites is warranted. Full article
(This article belongs to the Special Issue Cellular and Molecular Mechanism of Neuroimmunological Diseases)
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