| First Author | Crawley SC | Year | 1999 |
| Journal | Biochem Biophys Res Commun | Volume | 263 |
| Issue | 3 | Pages | 728-36 |
| PubMed ID | 10512748 | Mgi Jnum | J:57982 |
| Mgi Id | MGI:1346268 | Doi | 10.1006/bbrc.1999.1466 |
| Citation | Crawley SC, et al. (1999) Genomic organization and structure of the 3' region of human MUC3: alternative splicing predicts membrane-bound and soluble forms of the mucin. Biochem Biophys Res Commun 263(3):728-36 |
| abstractText | The MUC3 gene encodes a large, glycosylated mucin produced by intestinal epithelial cells to form a protective barrier against the external environment. Recently published cDNA sequences for the carboxyl-terminal region of MUC3 polypeptide indicated that rodent Muc3 possesses two epidermal growth factor (EGF)-like domains, and putative transmembrane and cytoplasmic domains, whereas the sequence of human MUC3 predicted termination after the first EGF-like domain. Here we describe the complete genomic sequence encompassing the carboxyl terminal region of human MUC3, revealing the boundaries of 11 exons. RT-PCR and cDNA library cloning experiments indicate that the gene is alternatively spliced, yielding a major membrane-bound form as well as multiple soluble forms. Thus, this work indicates that both membrane-bound and soluble MUC3 mucin proteins are produced by alternative splicing of a single gene. A potentially important polymorphism involving a Tyr residue with a proposed role in signalling is described as well. Copyright 1999 Academic Press. |
