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Cadherins are a superfamily of calcium-dependent cell adhesion molecules characterized by multiple extracellular cadherin repeat domains that mediate homophilic (like-with-like) binding at adherens junctions in animal tissues[1][2][5]. They are critical for maintaining tissue integrity, regulating cell sorting, and controlling morphogenesis during development. The cadherin family includes major subgroups: classical cadherins (such as E-cadherin, N-cadherin, and VE-cadherin), desmosomal cadherins (desmogleins and desmocollins), and protocadherins (primarily in the nervous system)[2][5]. Cadherin-mediated adhesion is essential for epithelial, neural, and endothelial structures and is tightly regulated through interactions with cytoplasmic proteins and the actin cytoskeleton[1][4]. Dysfunction of cadherins—especially downregulation or cleavage of E-cadherin—is strongly implicated in tumor progression and metastasis, among other pathologies[4]. While the family is of great biological and therapeutic interest, "cadherin" is not a single target but a superfamily, and precision is required (e.g., E-cadherin for epithelial tumors) when describing drug targeting efforts. In cancer, soluble forms of E-cadherin in blood may serve as biomarkers. For therapeutic development, loss of specificity within the cadherin family or broad inhibition may compromise critical cell-cell adhesions, leading to significant safety risks. Note: "Cadherin" alone is overly broad and not a precise target; canonical therapeutic and biomarker associations depend on subtype (CDH1/E-cadherin is the main drug-related entity). If a structured list for a specific member (e.g., "E-cadherin" or "N-cadherin") is needed, use that full name and associated gene/protein identifiers for more accurate entries.
Stabilization or inhibition of cell-cell adhesion (agonists/antagonists) Disruption of cadherin-mediated adhesion (e.g., some anti-cancer agents) Inhibition of proteolytic cleavage of cadherins (MMP inhibitors)
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