Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Role Of Notch Signalling In Intestinal Stem Cell Renewal01:12

Role Of Notch Signalling In Intestinal Stem Cell Renewal

Notch signaling was first discovered in Drosophila melanogaster, where it is involved in cell lineage differentiation. Notch signaling regulates the maintenance and differentiation of intestinal stem cells or ISCs by controlling the expression of atonal homolog 1 or Atoh1. Atoh1 directs cells to differentiate into secretory cells.
Direct cell-to-cell contact is needed for the activation of Notch signaling. The signal is initiated when a notch ligand binds to a receptor on an adjacent cell, also...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...
Insulin: The Receptor and Signaling Pathways01:28

Insulin: The Receptor and Signaling Pathways

Insulin action is mediated through a receptor tyrosine kinase, akin to the IGF-1 receptor. The number of receptors per cell varies significantly, from 40 on erythrocytes to 300,000 on adipocytes and hepatocytes. The insulin receptor consists of linked α/β subunit dimers, forming a heterotetramer glycoprotein with two extracellular α subunits and two β subunits spanning the membrane. The α subunits inhibit the inherent tyrosine kinase activity of the β subunits, but this inhibition is released...
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
Two...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Comparative analysis of salmonid non-classical MHC class I U lineage genes: Promoter architecture and transcriptional responses with a focus on Atlantic salmon.

Developmental and comparative immunology·2026
Same author

Pneumococcal H₂O₂ reshapes mitochondrial function and reprograms host cell metabolism.

mBio·2025
Same author

Impacts of real microplastic leachates on the development and behavior of developing zebrafish (<i>Danio rerio</i>).

Environmental science. Processes & impacts·2025
Same author

Diagnosis and Management of Alzheimer's Disease in Primary Care: A Real-World Study in Ontario, Canada.

Journal of primary care & community health·2025
Same author

Comparative analysis of salmonid non-classical MHC class I L lineage genes.

Developmental and comparative immunology·2025
Same author

Pneumococcal H<sub>2</sub>O<sub>2</sub> Reshapes Mitochondrial Function and Reprograms Host Cell Metabolism.

bioRxiv : the preprint server for biology·2025

Related Experiment Video

Updated: Jun 3, 2026

Intravital Imaging of Intraepithelial Lymphocytes in Murine Small Intestine
08:00

Intravital Imaging of Intraepithelial Lymphocytes in Murine Small Intestine

Published on: June 24, 2019

Insights into the function of IgD.

Eva-Stina Edholm1, Eva Bengten, Melanie Wilson

  • 1University of Mississippi Medical Center, Jackson, MS 39216, USA.

Developmental and Comparative Immunology
|March 19, 2011
PubMed
Summary
This summary is machine-generated.

Immunoglobulin D (IgD) is an ancient molecule with a unique role in vertebrate immunity, not just a co-receptor on naive B cells. Recent studies reveal its ancient origins and potential functions across diverse species.

More Related Videos

Dioscin Mediated IgA Nephropathy Alleviation by Inhibiting B Cell Activation In Vivo and Decreasing Galactose-Deficient IgA1 Production In Vitro
14:18

Dioscin Mediated IgA Nephropathy Alleviation by Inhibiting B Cell Activation In Vivo and Decreasing Galactose-Deficient IgA1 Production In Vitro

Published on: October 13, 2023

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Related Experiment Videos

Last Updated: Jun 3, 2026

Intravital Imaging of Intraepithelial Lymphocytes in Murine Small Intestine
08:00

Intravital Imaging of Intraepithelial Lymphocytes in Murine Small Intestine

Published on: June 24, 2019

Dioscin Mediated IgA Nephropathy Alleviation by Inhibiting B Cell Activation In Vivo and Decreasing Galactose-Deficient IgA1 Production In Vitro
14:18

Dioscin Mediated IgA Nephropathy Alleviation by Inhibiting B Cell Activation In Vivo and Decreasing Galactose-Deficient IgA1 Production In Vitro

Published on: October 13, 2023

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Area of Science:

  • Immunology
  • Evolutionary Biology
  • Genomics

Background:

  • Immunoglobulin D (IgD) was historically considered a recent evolutionary addition with an unclear function beyond its co-expression with IgM on naive B cells.
  • Debate existed regarding IgD's specific role in mammalian immunity.

Purpose of the Study:

  • To summarize IgD gene organization and structural data, highlighting its ancient evolutionary origins.
  • To discuss findings in catfish and humans to elucidate the functional significance of IgD.

Main Methods:

  • Comparative genomics through extensive sequencing of vertebrate genomes.
  • Analysis of structural data and gene organization.
  • Review of functional studies in model organisms like catfish and humans.

Main Results:

  • IgD homologs are found in all vertebrate taxa except birds, indicating an ancient origin.
  • Recent functional studies suggest IgD plays a distinct role in vertebrate immune responses.
  • Data from catfish and humans offer insights into IgD's potential functions.

Conclusions:

  • IgD is an evolutionarily ancient immunoglobulin isotype with a conserved presence across vertebrates.
  • Emerging evidence points to a unique and significant function for IgD in immune system regulation and response.