Mucin-17 is a protein that in humans is encoded by the MUC17gene.[1][2]
Membrane mucins, such as MUC17, function in epithelial cells to provide cytoprotection, maintain luminal structure, provide signal transduction, and confer antiadhesive properties upon cancer cells that lose their apical/basal polarization.[supplied by OMIM][2]
References
↑Gum JR Jr; Crawley SC; Hicks JW; Szymkowski DE; Kim YS (Feb 2002). "MUC17, a novel membrane-tethered mucin". Biochem Biophys Res Commun. 291 (3): 466–475. doi:10.1006/bbrc.2002.6475. PMID11855812.
Malmberg EK, Pelaseyed T, Petersson AC, et al. (2008). "The C-terminus of the transmembrane mucin MUC17 binds to the scaffold protein PDZK1 that stably localizes it to the enterocyte apical membrane in the small intestine". Biochem. J. 410 (2): 283–9. doi:10.1042/BJ20071068. PMID17990980.
Moniaux N, Junker WM, Singh AP, et al. (2006). "Characterization of human mucin MUC17. Complete coding sequence and organization". J. Biol. Chem. 281 (33): 23676–23685. doi:10.1074/jbc.M600302200. PMID16737958.
Oh JH, Yang JO, Hahn Y, et al. (2006). "Transcriptome analysis of human gastric cancer". Mamm. Genome. 16 (12): 942–954. doi:10.1007/s00335-005-0075-2. PMID16341674.
Ho JJ, Jaituni RS, Crawley SC, et al. (2004). "N-glycosylation is required for the surface localization of MUC17 mucin". Int. J. Oncol. 23 (3): 585–92. doi:10.3892/ijo.23.3.585. PMID12888891.
Van Klinken BJ, Van Dijken TC, Oussoren E, et al. (1997). "Molecular cloning of human MUC3 cDNA reveals a novel 59 amino acid tandem repeat region". Biochem. Biophys. Res. Commun. 238 (1): 143–148. doi:10.1006/bbrc.1997.7258. PMID9299468.