Poly-iga Receptor
Poly-iga Receptor - Related Videos
10:27
Recognition of Epidermal Transglutaminase by IgA and Tissue Transglutaminase 2 Antibodies in a Rare Case of Rhesus Dermatitis
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Cited by 10 •
2011
Dermatitis herpetiformis (DH) is a chronic inflammatory condition characterized by an autoimmune reaction between IgA and epidermal transglutaminase (eTG). DH develops in a very small portion of gluten-sensitive and/or celiac patients. The results of this study indicate that DH can also develop in a rhesus monkey host with symptoms of idiopatic dermatitis.
12:03
Receptor Autoradiography Protocol for the Localized Visualization of Angiotensin II Receptors
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Cited by 14 •
2016
Here we present a protocol to describe the localization of angiotensin II Type 1 receptors in the rat brain by quantitative, densitometric, in vitro receptor autoradiography using an iodine-125 labeled analog of angiotensin II.
11:34
Controlled Synthesis and Fluorescence Tracking of Highly Uniform Poly(N-isopropylacrylamide) Microgels
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Cited by 5 •
2016
Non-stirred precipitation polymerization provides a rapid, reproducible prototyping approach to the synthesis of stimuli-sensitive poly(N-isopropylacrylamide) microgels of narrow size distribution. In this protocol synthesis, light scattering characterization and single particle fluorescence tracking of these microgels in a wide-field microscopy setup are demonstrated.
07:13
Induction of Maternal Immune Activation in Mice at Mid-gestation Stage with Viral Mimic Poly(I:C)
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Cited by 25 •
2016
Maternal immune activation (MIA) is a model for an environmental risk factor of autism and schizophrenia. The goal of this article is to provide a step-by-step procedure of how to induce MIA in the pregnant mice in order to enhance the reproducibility of this model.
04:55
Assaying Surface Expression of Chemosensory Receptors in Heterologous Cells
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Cited by 6 •
2011
Here we demonstrate a protocol to carry out live cell staining that can be used to detect odorant receptors on the surface of HEK293T cells conveniently. In addition, it may also be used to assay for surface expression of other chemosensory receptors or GPCRs.
FAQs
Recognition depends on the joining chain, a component associated with polymeric antibodies. On the basolateral side of an epithelial cell, this feature enables the receptor to bind dimeric IgA and pentameric IgM. The interaction determines which immunoglobulin forms can enter the transport pathway and helps target them for delivery across the epithelial barrier.
Following binding, the receptor-antibody complex enters endocytic vesicles at the basolateral surface. It then travels through the epithelial cell by transcytosis, a directional transport process that moves material from one cell surface to the opposite surface. This intracellular route positions the complex at the apical membrane, where antibody release can occur.
Dimeric IgA and pentameric IgM are the polymeric antibody forms identified as pIgR cargo. Their association with the joining chain allows both classes to use the same epithelial transport mechanism. Consequently, the system can deliver two antibody types into mucus, extending antibody-mediated protection at mucosal surfaces rather than limiting transport to IgA alone.
At the apical surface, proteolytic cleavage separates the antibody from the receptor’s extracellular portion. That released portion, called the secretory component, remains associated with the transported antibody in secretory IgA or IgM. Cleavage therefore converts the intracellular transport complex into a secreted immune product that can function within mucus.
A study can follow the process in four linked stages: polymeric antibody binding at the basolateral surface, entry into endocytic vesicles, transcytotic movement through the epithelial cell, and apical cleavage with release. Examining these stages separately helps distinguish recognition, intracellular trafficking, and final secretion when investigating epithelial transport or mucosal immunity.
The receptor connects epithelial cell biology with immune protection at body surfaces. Its activity determines how secretory IgA and IgM reach mucus, where they help exclude pathogens and toxins. For this reason, pIgR-related studies can address mucosal immunity, infection, and the behavior of epithelial barriers within a single transport pathway.