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Tight Junctions

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Tight junctions are molecular seals between cells that prevent the leaking of fluids, ions, and other small solutes across cavities and compartments in multicellular organisms. They are mainly composed of claudin and occludin transmembrane proteins, and other proteins such as tricellulin and JAM (junctional adhesion molecule). All these proteins are 4-pass transmembrane proteins, except JAM, which is a single-pass transmembrane protein belonging to the immunoglobulin superfamily. The...

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Related Experiment Video

Updated: Jul 10, 2026

Immunostaining and Dye Penetration Experiments to Define Core Pleated Septate Junction Proteins in Drosophila Embryonic Epithelia

Immunostaining and Dye Penetration Experiments to Define Core Pleated Septate Junction Proteins in Drosophila Embryonic Epithelia

Published on: February 27, 2026

Pollen proteolytic enzymes degrade tight junctions.

Sarah Runswick¹, Thomas Mitchell, Paul Davies

¹Faculty of Life Sciences, University of Manchester, Manchester, UK. david.garrod@manchester.ac.uk

Respirology (Carlton, Vic.)

|November 8, 2007

Summary

Pollen contains enzymes that break down epithelial tight junctions, increasing allergen entry. This study shows pollen peptidases disrupt these barriers, similar to dust mite enzymes, potentially worsening allergies.

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Sensing of Barrier Tissue Disruption with an Organic Electrochemical Transistor

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Published on: February 10, 2014

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Last Updated: Jul 10, 2026

Immunostaining and Dye Penetration Experiments to Define Core Pleated Septate Junction Proteins in Drosophila Embryonic Epithelia

Immunostaining and Dye Penetration Experiments to Define Core Pleated Septate Junction Proteins in Drosophila Embryonic Epithelia

Published on: February 27, 2026

Sensing of Barrier Tissue Disruption with an Organic Electrochemical Transistor

Sensing of Barrier Tissue Disruption with an Organic Electrochemical Transistor

Published on: February 10, 2014

Area of Science:

Immunology
Cell Biology
Allergy Research

Background:

Asthma and allergic rhinitis are increasing global health concerns.
Pollen, a common allergen, carries proteolytic enzymes.
Previous research linked house dust mite enzymes to compromised epithelial barrier function.

Purpose of the Study:

To investigate if pollen peptidases disrupt epithelial tight junctions.
To determine if pollen enzymes affect barrier integrity similarly to house dust mite enzymes.

Main Methods:

Applied pollen diffusates to cell monolayers (MDCK, Calu-3).
Assessed tight junction protein expression (occludin, claudin-1, ZO-1) via immunofluorescence and Western blotting.
Analyzed enzymatic activity using zymography and tested protease inhibitors.

Main Results:

All tested pollen diffusates reduced tight junction protein labeling.
Proteolytic activity was confirmed in pollen diffusates.
Enzyme inhibitors blocked the disruptive effect on tight junctions.

Conclusions:

Pollen peptidases disrupt epithelial tight junctions.
This disruption is a potential mechanism for enhanced allergen penetration.
Findings suggest a role for pollen enzymes in allergic rhinitis and asthma pathogenesis.