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Intestinal epithelial adhesion sites, primarily represented by the apical junctional complex (AJC), are critical structural components that maintain the integrity of the intestinal barrier. This complex includes tight junctions, adherens junctions, and desmosomes, which are composed of proteins such as claudins, occludin, and E-cadherin [1, 2]. These sites regulate the paracellular movement of water and solutes while providing a physical defense against the translocation of luminal bacteria and toxins into the underlying tissue [1]. Dysregulation of these adhesion sites is a hallmark of various gastrointestinal disorders, including inflammatory bowel disease (IBD) and celiac disease, where leaky gut contributes to chronic immune activation [3, 4]. Therapeutic approaches targeting these sites involve stabilizing junctional proteins or inhibiting the signaling pathways, such as the zonulin pathway, that trigger junctional disassembly [3, 5].
Modulation of tight junction permeability and stabilization of the epithelial barrier through the regulation of junctional proteins like claudins and occludin.
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