Mucin

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Mucins are a family of large, heavily glycosylated proteins. Although some mucins are membrane-bound due to the presence of a hydrophobic membrane-spanning domain that favors retention in the plasma membrane, the concentration here is on those mucins that are secreted on mucosal surfaces and saliva.

Mucin genes encode mucin monomers that are synthesized as rod-shape apomucin cores that are post-translationally modified by exceptionally abundant glycosylation. Two distinctly different regions are found in mature mucins:

  • The amino- and carboxy-terminal regions are very lightly glycosylated, but rich in cysteines, which are likely involved in establishing disulfide linkages within and among mucin monomers.

The dense "sugar coating" of mucins gives them considerable water-holding capacity and also makes them resistant to proteolysis, which may be important in maintaining mucosal barriers.

Mucins are secreted as massive aggregates of proteins with molecular masses of roughly 1 to 10 million Da. Within these aggregates, monomers are linked to one another mostly by non-covalent interactions, although intermolecular disulfide bonds may also play a role in this process. At least 19 human mucin genes have been distinguished by cDNA cloning--MUC1, 2, 3A, 3B, 4, 5AC, 5B, 6-9, 11-13, and 15-19. The major secreted airway mucins are MUC5AC and MUC5B, while MUC2 is secreted mostly in the intestine but also in the airway.

Increased mucin production occurs in Adenocarcinoma, a type of lung cancer, and in lung diseases such as asthma, bronchitis, COPD or cystic fibrosis.

[edit] References

Ali, M.S., et al. "Major secretory mucin expression in chronic sinusitis." Otolaryngol Head Neck Surg. 2005 Sep; 133(3); 423-8. PMID: 16143194

Perez-Vilar, J. and Hill, R. L. Mucin Family of Glycoproteins. Encyclopedia of Biological Chemistry (Lennarz & Lane, EDs.) Academic Press/Elsevier, Oxford, 2004, vol. 2, pp 758-764

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