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Gut epithelial tight junction proteins are a large family of transmembrane and cytoplasmic proteins that form the structural “tight junctions” at the apical part of epithelial cell membranes in the intestinal tract[2][4][5]. Major families of these proteins include occludin, claudins, junctional adhesion molecules (JAMs), and tricellulin (transmembrane components), and scaffolding proteins such as zonula occludens (ZO-1, ZO-2, ZO-3), cingulin, and afadin[1][4][5]. Tight junctions are essential for the selective permeability of the intestinal barrier, maintaining separation between the external environment and the body’s internal milieu[2][3]. Their dynamic regulation is critical for nutrient transport, maintaining immune homeostasis, and preventing pathogen and toxin entry. Alterations in tight junction proteins are associated with diseases such as IBD, metabolic syndrome, autoimmune diseases, and cancer[1][2][4]. Many interventions—pharmacological, dietary, or microbial—seek to modulate these proteins to restore barrier function in disease[1][5]. Key points: - “Gut epithelial tight junction proteins” refers to a group, not a single protein, so is not a canonical target name but a category; each protein (e.g., occludin, claudin-1) could be a distinct target[1][2][4]. - They are multi-protein complexes vital to epithelial barrier integrity. - Their dysfunction or modulation is both a therapeutic target and a disease biomarker[2][3][4][5].
Modulation/restoration of tight junction protein assembly; Inhibition of tight junction disassembly; Reduction of paracellular permeability
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