Intestinal mucin glycoprotein (MUC)

Intestinal mucin glycoproteins are large, heavily O-glycosylated proteins that constitute the primary structural framework of the mucus layer overlying the intestinal epithelium (UniProt P17062). The predominant form in the human intestine is Mucin-2 (MUC2), a gel-forming mucin secreted by specialized goblet cells that organizes into a complex, stratified barrier (PubMed 23470503). This barrier serves a dual purpose: it provides physical lubrication for the passage of luminal contents and acts as a selective filter that prevents the translocation of commensal bacteria and pathogens into the underlying tissue (PubMed 21666637). Beyond their structural role, these glycoproteins are essential for mucosal immunity, as they harbor antimicrobial peptides and provide a glycan-rich niche for beneficial microbiota (PubMed 25263224). Alterations in mucin expression, structure, or glycosylation are critically linked to the pathogenesis of inflammatory bowel diseases (IBD), such as ulcerative colitis, and are frequently observed in the progression of colorectal malignancies (PubMed 22262161). Therapeutic interventions targeting these mucins aim to restore barrier integrity by stimulating secretion, enhancing the viscoelastic properties of the mucus gel, or modulating the glycan profiles to favor a healthy microbial environment (PubMed 12192111).

Other names

Mucin-2MUC2Intestinal mucusSecretory mucinGel-forming mucinMembrane-associated mucin

Pharmacological agents interact with intestinal mucins by inducing their synthesis and secretion from goblet cells, chemically modifying the disulfide bridges to alter gel rheology, or physically adhering to the mucin layer to reinforce the mucosal barrier (PubMed 12192111, PubMed 24856657).