Molecular cloning and expression of human tumor-associated polymorphic epithelial mucin
Document Type
Article
Department
Pathology and Laboratory Medicine
Abstract
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 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.
Publication (Name of Journal)
Journal of Biological Chemistry
Recommended Citation
J. GendlerS,, S.,
A. Lancaster, C.,
Taylor-Papadimitriou, J.,
Duhig,, T.,
Peat, N.,
Burchell, J.,
Pemberton, L.,
Lalani, E.,
D, W.
(1990). Molecular cloning and expression of human tumor-associated polymorphic epithelial mucin. Journal of Biological Chemistry, 265(25), 15286-15293.
Available at:
https://ecommons.aku.edu/pakistan_fhs_mc_pathol_microbiol/685