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Gastric mucus glycoproteins, known as gastric mucins, are high-molecular-weight, heavily O-glycosylated glycoproteins secreted by specialized epithelial cells in the stomach lining[2][4][6]. These mucins are responsible for the viscosity and gel-forming properties of gastric mucus, enabling it to form a thick protective layer that lubricates stomach contents and shields the underlying epithelium from acidic gastric juice and digestive enzymes, thereby preventing autodigestion[1][3]. Structurally, gastric mucins have a protein backbone with extensive O-linked glycan modifications, especially in their central domains rich in serine, threonine, and proline (“PTS” domains)[2][6]. The glycan structures can differ in disease states, impacting stomach health, with qualitative and quantitative changes associated with inflammation, tumorigenesis, and susceptibility to infection[2][4]. Mucins are essential components of the mucosal innate immune barrier and play a role in maintaining gastrointestinal homeostasis, but they are not considered a direct drug target, receptor, or enzyme themselves[4][6]. The mucin family includes several specific gene products (MUC1, MUC5AC, MUC6, etc.), but “gastric mucus glycoproteins” is not a canonical name for an individual therapeutic target, making the entry non-specific and potentially misleading[6][4].
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