Tight Junction Disassembly
Tight Junction Disassembly - Related Videos
01:29
Tight Junctions
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2023
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...
04:15
Fluorescence Localization of Tight Junction Proteins and Stress Fibers in Endothelial Cells
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2025
Source: Alluri, H., et al. Oxygen-Glucose Deprivation and Reoxygenation as an In Vitro Ischemia-Reperfusion Injury Model for Studying Blood-Brain Barrier Dysfunction. J. Vis. Exp. (2015).The video demonstrates the fluorescent localization of tight junction proteins and stress fibers in rat brain microvascular endothelial cells (RBMECs). In the stressed monolayer, fluorescently labeled antibodies are used to tag the tight junction proteins, while fluorophore-tagged phalloidin labels the stress...
11:31
Analysis of Protein-protein Interactions and Co-localization Between Components of Gap, Tight, and Adherens Junctions in Murine Mammary Glands
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Cited by 5 •
2017
Intercellular junctions are requisites for mammary gland stage-specific functions and development. This manuscript provides a detailed protocol for the study of protein-protein interactions (PPIs) and co-localization using murine mammary glands. These techniques allow for the investigation of the dynamics of the physical association between intercellular junctions at different developmental stages.
02:49
Detection of Biofilm Disassembly Through a Dispersion Assay
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2025
The video showcases a biofilm dispersion assay using a multi-well plate. Buffer and glucose treatment disassemble the biofilm, releasing bacteria, while bile salts induce stress, retaining bacteria in the protective extracellular polymeric substance. Higher dispersion with buffer and glucose confirms successful biofilm disassembly, estimated by colony forming units measurement.
01:35
Disassembly of Intermediate Filaments
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2023
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs. Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
FAQs
Changes in claudins, occludin, and ZO proteins can alter the junctional seal at cell borders, thereby changing how substances move through the paracellular route, the space between adjacent cells. Because these proteins form part of the barrier-associated complex, examining their changes or removal from borders helps connect molecular remodeling with reduced epithelial or endothelial integrity during infection or inflammation.
Actomyosin contraction can contribute to force-related changes at junction-associated structures, while phosphorylation can modify protein behavior and endocytosis can remove junctional proteins from cell borders. These mechanisms represent different routes to a similar functional consequence: a less continuous barrier and altered paracellular transport. Distinguishing them helps relate permeability changes to cytoskeletal force, protein regulation, or membrane trafficking.
Bacterial factors, viral infection, and inflammatory mediators are distinct initiating contexts for the same barrier disruption. Their relevance differs experimentally: infection-associated changes can be examined alongside pathogen penetration, whereas inflammation-associated changes can be considered with leukocyte trafficking and immune signaling. Comparing these contexts helps determine how barrier disruption shapes disease rather than treating permeability as an isolated measurement.
Studies can connect molecular and functional outcomes by examining junction-associated proteins together with barrier permeability. Changes in claudins, occludin, or ZO proteins indicate remodeling at cell borders, while permeability measurements reveal the resulting transport change. In immunology and infection, observations of leukocyte trafficking, pathogen penetration, or immune signaling show how that remodeling affects tissue behavior.
Infection research uses tight junction disassembly to examine how barrier failure changes interactions among microbes, tissues, and immune responses. Increased permeability may facilitate pathogen penetration, while altered barrier properties can influence leukocyte trafficking and immune signaling. These outcomes make the process relevant to both mucosal and vascular barriers, where local structural changes can have broader consequences for host defense.
Barrier-preserving strategies can be evaluated by asking whether they limit the molecular and functional changes associated with disassembly. Conversely, controlled opening may be investigated for drug delivery when increased permeability is useful. This framework supports two complementary goals: preventing disease-related barrier failure and determining whether junctional opening can be applied selectively while retaining the barrier function needed by surrounding tissue.