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

Diversity of Antigen Receptors01:28

Diversity of Antigen Receptors

Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

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 activation may...
Antibody Structure and Classes01:25

Antibody Structure and Classes

Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.

You might also read

Related Articles

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

Sort by
Same author

Disrupting CD22-cis-ligand interactions ameliorates type 1 diabetes and graft rejection by expanding regulatory B cells.

PLoS biology·2026
Same author

Structural truncation of IL-1R2 enhances the anti-inflammatory activity of HeLa cells.

Cell structure and function·2025
Same author

The N-terminal domain of precursor IL-1α enhances IL-6 expression via an intracrine mechanism in oral squamous cell carcinoma.

Molecular biology reports·2025
Same author

IL-1α Promotes Cancer Cell Migration and Is a Potential Prognostic Marker in Oral Squamous Cell Carcinoma.

Cancers·2025
Same author

Selective Epac2 antagonist attenuates cerebral infarction induced by secondary brain injury in rats.

Experimental and therapeutic medicine·2025
Same author

Analysis of CD22 cis-ligands using a synthetic sialoside binding to CD22 with ultra-high affinity.

Carbohydrate research·2025

Related Experiment Video

Updated: May 31, 2026

Native Polyacrylamide Gel Electrophoresis Immunoblot Analysis of Endogenous IRF5 Dimerization
08:57

Native Polyacrylamide Gel Electrophoresis Immunoblot Analysis of Endogenous IRF5 Dimerization

Published on: October 6, 2019

Polymeric immunoglobulin receptor.

Masatake Asano1, Kazuo Komiyama

  • 1Department of Pathology, Nihon University School of Dentistry, Tokyo, Japan. asano-m@dent.nihon-u.ac.jp

Journal of Oral Science
|June 30, 2011
PubMed
Summary

The mucosal immune system uses dimeric IgA (dIgA) to protect the gut. Intestinal epithelial cells transport dIgA via the polymeric immunoglobulin receptor (pIgR) to form secretory IgA (SIgA).

Area of Science:

  • Immunology
  • Cell Biology
  • Gastroenterology

Background:

  • The intestinal tract relies on the mucosal immune system for protection and homeostasis.
  • Epithelial cells and lymphocytes cooperate within this system.
  • Polymeric immunoglobulins (pIgs), especially dimeric IgA (dIgA), are key players.

Purpose of the Study:

  • To review the transport mechanism of dIgA across intestinal epithelial cells.
  • To highlight the role of the polymeric immunoglobulin receptor (pIgR) in this process.
  • To discuss recent advancements in understanding mucosal immunity.

Main Methods:

  • Review of existing literature on dIgA transport and pIgR function.
  • Analysis of the molecular mechanisms involved in transcytosis.

More Related Videos

A Protocol for the Production of KLRG1 Tetramer
07:24

A Protocol for the Production of KLRG1 Tetramer

Published on: January 12, 2010

Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study
11:10

Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study

Published on: June 29, 2016

Related Experiment Videos

Last Updated: May 31, 2026

Native Polyacrylamide Gel Electrophoresis Immunoblot Analysis of Endogenous IRF5 Dimerization
08:57

Native Polyacrylamide Gel Electrophoresis Immunoblot Analysis of Endogenous IRF5 Dimerization

Published on: October 6, 2019

A Protocol for the Production of KLRG1 Tetramer
07:24

A Protocol for the Production of KLRG1 Tetramer

Published on: January 12, 2010

Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study
11:10

Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study

Published on: June 29, 2016

  • Synthesis of current knowledge on secretory IgA (SIgA) formation.
  • Main Results:

    • Dimeric IgA (dIgA) is captured by pIgR on the basolateral surface of intestinal epithelial cells (IECs).
    • The dIgA-pIgR complex undergoes transcytosis across IECs.
    • Proteolytic cleavage on the apical surface generates secretory IgA (SIgA).

    Conclusions:

    • The pIgR-mediated transcytosis is crucial for delivering dIgA to the intestinal lumen.
    • This process is essential for maintaining gut homeostasis and pathogen defense.
    • Ongoing research continues to elucidate the complexities of mucosal immune responses.