Molecular cloning and expression of human tumor-associated polymorphic epithelial mucin

Sandra J. Gendler, Carole A. Lancaster, Joyce Taylor-Papadimitriou, Trevor Duhig, Nigel Peat, Joy Burchell, Lucy Pemberton, El Nasir Lalani, David Wilson

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886 Citations (Scopus)


Human mammary cells present on the cell surface a polymorphic epithelial mucin (PEM) which is developmentally regulated and aberrantly expressed in tumors. PEM carries tumor-associated epitopes recognized by the monoclonal antibodies HMFG-1, HMFG-2, and SM-3. Previously isolated partial cDNA clones revealed that the core protein contained a large domain consisting of variable numbers of 20-amino acid repeat units. We now report the full sequence for PEM, as deduced from cDNA sequences. The encoded protein consists of three distinct regions: the amino terminus consisting of a putative signal peptide and degenerate tandem repeats; the major portion of the protein which is the tandem repeat region; the carboxyl terminus consisting of degenerate tandem repeats and a unique sequence containing a transmembrane sequence and a cytoplasmic tail. Potential O-glycosylation sites (serines or threonines) make up more than one-fourth of the amino acids. Length variations in the tandem repeat result in PEM being an expressed variable number tandem repeat locus. Tandem repeats appear to be a general characteristic of mucin core proteins.

Original languageEnglish
Pages (from-to)15286-15293
Number of pages8
JournalJournal of Biological Chemistry
Issue number25
Publication statusPublished - 5 Sept 1990
Externally publishedYes


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