Immunoglobulin Dynamics in Intestinal Epithelial Cells
Summary
The intestinal epithelium serves as a critical portal for immune surveillance, actively transporting polymeric immunoglobulins and shaping mucosal defence. Dimeric IgA, stabilised by the joining (J) chain, binds to the polymeric immunoglobulin receptor (pIgR) on the basolateral surface of enterocytes. Following receptor–ligand engagement, the complex undergoes clathrin-mediated endocytosis and is shuttled via endosomal compartments to the apical membrane. Proteolytic cleavage of pIgR releases the secretory component (SC)–IgA complex into the lumen as secretory IgA (sIgA), where it neutralises pathogens and modulates the microbiota. The biosynthesis, post-translational modification and turnover of pIgR and SC, along with regulated trafficking dynamics, determine the quantity, affinity and glycosylation profile of sIgA. This system not only maintains barrier integrity and immune exclusion but also transmits immunological memory from the gut mucosa to external secretions. Dysregulation of this pathway has been linked to inflammatory bowel disease, food allergy and impaired vaccine responses. Ongoing research aims to elucidate molecular checkpoints governing receptor recycling, SC cleavage and the impact of host genetics on immunoglobulin transcytosis, with a view to novel mucosal immunotherapies and targeted delivery of antibodies to the gut lumen.
Research from Nature Portfolio
No recent Nature Portfolio content available.
Immunoglobulin Dynamics in Intestinal Epithelial Cells publication trend
The graph below shows the total number of articles in immunoglobulin dynamics in intestinal epithelial cells across all publications each year (not limited to Nature Index journals).
Technical terms
Polymeric immunoglobulin receptor (pIgR): A transmembrane receptor on epithelial cells that binds dimeric IgA or pentameric IgM and mediates their transcellular transport.
Secretory component (SC): The extracellular domain of pIgR that remains bound to immunoglobulins after proteolytic cleavage, forming secretory IgA or IgM.
Transcytosis: The process by which molecules are transported across a cell in vesicles, moving from one membrane domain to another.
J chain: A small polypeptide essential for polymerisation of IgA and IgM, facilitating their recognition by pIgR.
Glycosylation: The attachment of carbohydrate chains to proteins, critical for receptor folding, stability and ligand binding.
References
- A transmembrane precursor of secretory component. The receptor for transcellular transport of polymeric immunoglobulins.. Journal of Biological Chemistry (1982).
- Structural and genetic heterogeneity of the receptor mediating translocation of immunoglobulin A dimer antibodies across epithelia in the rabbit.. Journal of Biological Chemistry (1983).
- Covalent Homodimers of Murine Secretory Component Induced by Epitope Substitution Unravel the Capacity of the Polymeric Ig Receptor to Dimerize Noncovalently in the Absence of IgA Ligand*. Journal of Biological Chemistry (1999).
About these summaries
This Nature Research Intelligence Topic summary is created with the cited references and a large language model. We take care to ground generated text with facts, and have systems in place to gain human feedback on the overall quality of the process in line with our AI principles. We strive to create accurate and useful summaries for people unfamiliar with the research topic and that supports this goal. These pages are a beta release and will be updated as we learn how best to help people gain value from a research topic summary.
Turn complex research questions into confident strategic decisions
When you're under pressure to set direction, justify investment, or understand your competitive position, you need more than raw data — you need trusted insights you can act on.
Benchmark your performance against global peers using robust, methodologically sound analysis.
Combine quantitative metrics with qualitative expert insight to uncover strengths, gaps and emerging opportunities.
Gain tailored, decision-ready recommendations aligned to your strategic priorities.
Talk to us to learn more about our data dashboards and bespoke strategy reports.
Grow research skills, confidence and careers with training built for every stage of the research lifecycle.
Developed with Nature Portfolio journal Editors and internationally renowned experts. Discover three ways to learn:
Self-paced, online courses in convenient bite-sized units, covering key skills across scientific writing, publishing, grant writing, data analysis, and more.
Expert trainer-led workshops with hands-on exercises and real-time feedback across core research skills, delivered via interactive group sessions.
Editor-led workshops combining core principles in writing and publishing, personalised 1:1 feedback from Nature Portfolio Editors and hands-on exercises.
Explore course catalogues and workshop agendas, enquire about the options or request institutional pricing.