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Related Concept Videos

The Unfolded Protein Response01:37

The Unfolded Protein Response

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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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T Cell Types and Functions

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When T cells with CD4 markers are activated, they give rise to two types of effector cells: helper T cells and regulatory T cells. Meanwhile, T cells with CD8 markers differentiate into effector cytotoxic T cells. The differentiation of CD4 T cells into helper T cell subsets, such as Th1, Th2, and Th17 cells, is dependent on the antigen type, antigen-presenting cell, and regulatory cytokines.
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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Author Spotlight: Novel Assay for Studying B-Cell Responses in Multiple Sclerosis Research
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The unfolded protein response in multiple sclerosis.

Sarrabeth Stone1, Wensheng Lin1

  • 1Department of Neuroscience, University of Minnesota Minneapolis, MN, USA ; Institute for Translational Neuroscience, University of Minnesota Minneapolis, MN, USA.

Frontiers in Neuroscience
|August 19, 2015
PubMed
Summary

The unfolded protein response (UPR) is activated by endoplasmic reticulum (ER) stress and plays a role in multiple sclerosis (MS). UPR activation in oligodendrocytes is implicated in MS development.

Keywords:
demyelinationendoplasmic reticulum stressexperimental autoimmune encephalomyelitismultiple sclerosisoligodendrocytespancreatic endoplasmic reticulum kinaseremyelinationunfolded protein response

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Area of Science:

  • Cellular Biology
  • Neuroscience
  • Immunology

Background:

  • The unfolded protein response (UPR) is a cellular stress response pathway.
  • UPR activation is linked to endoplasmic reticulum (ER) stress.
  • UPR can lead to cell survival or apoptosis.

Purpose of the Study:

  • To review the current literature on the UPR.
  • To examine the evidence for UPR's role in multiple sclerosis (MS).

Main Methods:

  • Literature review of UPR and MS.
  • Analysis of studies on UPR components in MS lesions.
  • Examination of data from EAE and cuprizone models.

Main Results:

  • UPR components are upregulated in various cell types within MS lesions.
  • Oligodendrocytes show UPR activation in MS.
  • Animal models suggest UPR in oligodendrocytes contributes to MS pathogenesis.

Conclusions:

  • The UPR is implicated in the development of multiple sclerosis.
  • Targeting UPR pathways may offer therapeutic strategies for MS.