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Related Concept Videos

B Cell Activation and Differentiation01:24

B Cell Activation and Differentiation

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The adaptive immune response, a sophisticated defense mechanism, relies on the activation and differentiation of B lymphocytes, or B cells. These processes enable our bodies to mount a tailored response against specific pathogens such as bacteria, free virus particles, toxins, and parasites.
When naive B cells encounter a specific antigen that can bind to the B cell receptor (BCR) on their surface, they undergo sensitization to respond to the antigen's presence. Sensitization begins with...
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Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

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Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
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Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

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Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR...
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

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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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ER Retrieval Pathway01:45

ER Retrieval Pathway

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In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
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Related Experiment Videos

UPR-Mediated Membrane Biogenesis in B Cells.

Joseph W Brewer1, Suzanne Jackowski

  • 1Department of Microbiology and Immunology, College of Medicine, University of South Alabama, Mobile, AL 36688, USA.

Biochemistry Research International
|November 24, 2011
PubMed
Summary

The unfolded protein response (UPR) regulates lipid synthesis and membrane biogenesis during B cell differentiation. This process enhances antibody secretion by optimizing the endoplasmic reticulum

Area of Science:

  • Cellular Biology
  • Immunology
  • Biochemistry

Background:

  • The unfolded protein response (UPR) manages endoplasmic reticulum (ER) protein load.
  • UPR is increasingly linked to lipid synthesis and membrane biogenesis.
  • B lymphocyte differentiation into antibody-secreting cells involves significant ER expansion.

Purpose of the Study:

  • To explore the role of UPR in regulating lipid metabolism during B cell differentiation.
  • To investigate the impact of altered lipid metabolism on B cell secretory function.

Main Methods:

  • Analysis of UPR activation in differentiating B cells.
  • Examination of lipid synthesis pathways during B cell activation.
  • Assessment of B cell secretory characteristics under conditions of phospholipid restriction.

Related Experiment Videos

Main Results:

  • Activated B cells show increased UPR transcriptional activator XBP1(S) activity.
  • UPR activation enhances phospholipid precursor supply and secretory machinery.
  • Membrane phospholipid restriction affects B cell secretory characteristics.

Conclusions:

  • UPR plays a crucial role in coordinating lipid metabolism for ER expansion in differentiating B cells.
  • This coordination is essential for efficient antibody synthesis and secretion.
  • Understanding these lipid-metabolism alterations provides insights into B cell function and potential therapeutic targets.