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- W1598045277 abstract "Publisher Summary This chapter discusses membrane-associated mucins. Several mucin-like proteins have been described which contain an extended domain rich in O-linked glycans that has all the characteristics of a genuine mucin. However, these proteins are monomeric transmembrane molecules and are, therefore, classified as membrane-associated mucins. Their O-glycosylated domains may be relatively small, such as in the LDL receptor, in which case the mucin-like domain is mainly intended to lift the receptor domain above the glycocalyx, but it may also encompass most of the extracellular part of a glycoprotein. This is the case for episialin/MUC1, one of the best characterized mucin-like proteins. The chapter also discusses the properties of CD43, epiglycanin, and ascites sialoglycoprotein (ASGP). Episialin is encoded by the MUCl gene and is also known as the MUCl protein, polymorphic epithelial mucin (PEM), epithelial membrane antigen (EMA), the CA 15.3 antigen, and by various other names. The large mucin-like domain of episialin contains a large array of almost identical 20 amino acid repeats. ASGP-1 (ascites sialoglycoprotein) has many properties in common with episialin with respect to biosynthesis and processing. It is made from a precursor that is later split into a mucin-like domain (ASGP-1) and a cell-anchoring domain (ASGP-2)." @default.
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- W1598045277 date "1996-01-01" @default.
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- W1598045277 title "Membrane-associated mucins" @default.
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- W1598045277 doi "https://doi.org/10.1016/s1874-5342(96)80024-9" @default.
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