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Syncollin is a small, thermostable, predominantly beta-sheet protein most highly expressed in the zymogen granules of pancreatic acinar cells, with lower levels in intestinal epithelial cells and neutrophils[1][7]. It is involved in exocytosis by regulating the fusion of zymogen granules and may have a role in pore-forming activity on membranes. It exists as a homo-oligomer whose association state depends on pH, and is tightly bound to the granule membrane’s luminal surface[2]. Syncollin plays a direct antimicrobial role by binding to bacterial peptidoglycan, limiting the growth of both Gram-positive and Gram-negative bacteria, and damaging bacterial membranes[1]. Its expression is altered in pancreatic cancer, where it serves as a potential early detection biomarker. While it shares some structural features with the FXYD family of proteins, it is likely a pseudo-member and not a classical ion channel or transporter[4][5]. No approved drugs directly target syncollin, and there is no evidence it acts as a classical therapeutic target such as a receptor, enzyme, or transporter[5][9].
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