The MUC3 gene encodes a transmembrane mucin and is alternatively spliced

Williams, S. J., Munster, D. J., Quin, R. J., Gotley, D. C. and McGuckin, M. A. (1999) The MUC3 gene encodes a transmembrane mucin and is alternatively spliced. Biochemical and Biophysical Research Communication, 261 1: 83-89. doi:10.1006/bbrc.1999.1001

Author Williams, S. J.
Munster, D. J.
Quin, R. J.
Gotley, D. C.
McGuckin, M. A.
Title The MUC3 gene encodes a transmembrane mucin and is alternatively spliced
Journal name Biochemical and Biophysical Research Communication   Check publisher's open access policy
ISSN 0006-291X
Publication date 1999-01-01
Year available 1999
Sub-type Article (original research)
DOI 10.1006/bbrc.1999.1001
Open Access Status DOI
Volume 261
Issue 1
Start page 83
End page 89
Total pages 7
Place of publication New York, USA
Publisher Academic Press
Language eng
Subject C1
320302 Medical Biochemistry - Carbohydrates
730113 Digestive system and disorders
Abstract Epithelial mucins are a family of secreted and cell surface glycoproteins expressed by epithelial tissues and implicated in epithelial cell protection, adhesion modulation and signaling. The gene encoding human MUC3 (hMUC3), localised to chromosome 7q22, is most highly expressed in the small intestine. It has previously been reported to be a non-transmembrane mucin with minimal homology to its suggested orthologues from rat (rMuc3) and mouse (mMuc3). RT-PCR was performed to investigate the carboxyl terminus of the published sequence of hMUC3 from normal colon and small intestine tissues and also from a series of 10 colorectal cancer cell lines. Two distinct PCR products were identified. In contrast to the previously published hRMUC3 sequence, which terminates shortly after a single cysteine-rich EGF-like domain, conceptual protein translation of the dominant and largest PCR product identified two extracellular cysteine-rich EGF-like domains separated by an N-glycosylation-rich domain and a potential coiled-coil region, followed by a putative transmembrane region and a 75 amino acid cytoplasmic tail. The smaller of the two PCR products was found to be an alternative splice variant of MUC3 including the first EG;F-like domain but lacking part of the second EGF-like domain and the transmembrane region. Nine out of 10 colorectal cancer cell lines were found to express MUC3. Interestingly, one of the cell lines, LoVo, expressed predominantly the alternative splice form lacking a transmembrane domain. Structural homology of the new protein sequence of hMUC3 with rMuc3 and mMuc3 indicates it is closely related to the rodent proteins and is likely to be involved in ligand-binding and intracellular signaling. The new finding that MUC3 encodes a transmembrane molecule presents a new paradigm for the structure of this mucin and the manner in which it may function, (C) 1999 Academic Press.
Keyword Biochemistry & Molecular Biology
Rat Intestinal Mucin
Q-Index Code C1
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Medicine Publications
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 72 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 70 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Tue, 10 Jun 2008, 23:57:34 EST