Abstract
Mucin family comprises secretory and membrane-bound mucins. Mucins contain a variety of O-linked oligosaccharides that comprise more than 50 % of the mucin molecule by weight. Several mucin-type O-glycans have been revealed to be cancer-associated carbohydrate antigens. They are useful for diagnosis and monitoring of cancer progression. Several secretory mucins form a gel to protect and lubricate luminal epithelial surfaces. In addition to this protective function, many evidences have been obtained that several membrane-bound mucins are involved in signaling events that contribute to the progression of cancer. MUC1 is aberrantly overexpressed in various malignant tumors, and its expression level is correlated with poor prognosis. MUC1 engages in signal transduction by interacting with receptors for growth and differentiation factors, which contributes growth and survival of cancer cells. The oncogenic effects of MUC1 are revealed to occur through the interaction of MUC1-C-terminal domain with various signaling molecules and subsequent transportation of the resultant complexes to the nucleus.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Andrianifahanana M, Moniaux N, Batra SK (2006) Regulation of mucin expression: mechanistic aspects and implications for cancer and inflammatory diseases. Biochim Biophys Acta 1765:189–222
Bafna S, Kaur S, Batra SK (2010) Membrane-bound mucins: the mechanistic basis for alterations in the growth and survival of cancer cells. Oncogene. 29:2893–2904
Brockhausen I (1999) Pathways of O-glycan biosynthesis in cancer cells. Biochim Biophys Acta. 1473:67–95
Inoue M, Takahashi S, Yamashina I, Kaibori M, Okumura T, Kamiyama Y, Vichier-Guerre S, Cantacuzène D, Nakada H (2001) High density O-glycosylation of the MUC2 tandem repeat unit by N-acetylgalactosaminyltransferase-3 in colonic adenocarcinoma extracts. Cancer Res 61:950–956
Julien S, Lagadec C, Krzewinski-Recchi MA, Courtand G, Le Bourhis X, Delannoy P (2005) Stable expression of sialyl-Tn antigen in T47-D cells induces a decrease of cell adhesion and an increase of cell migration. Breast Cancer Res Treat. 90:77–84
Matsumoto Y, Zhang Q, Akita K, Nakada H, Hamamura K, Tsuchida A, Okajima T, Furukawa K, Urano T, Furukawa K (2013) Trimeric Tn antigen on syndecan 1 produced by ppGalNAc-T13 enhances cancer metastasis via a complex formation with integrin α5β1 and matrix metalloproteinase 9. J Biol Chem 288:24264–24276
Nakada H, Inoue M, Numata Y, Tanaka N, Funakoshi I, Fukui S, Mellors A, Yamashina I (1993) Epitopic structure of Tn glycophorin A for an anti-Tn antibody (MLS 128). Proc Natl Acad Sci U S A. 90:2495–2499
Shen Q, Rahn JJ, Zhang J, Gunasekera N, Sun X, Shaw AR, Hendzel MJ, Hoffman P, Bernier A, Hugh JC (2008) MUC1 initiates Src-CrkL-Rac1/Cdc42-mediated actin cytoskeletal protrusive motility after ligating intercellular adhesion molecule-1. Mol. Cancer Res. 6:555–567
Singh PK, Hollingsworth MA (2006) Cell surface-associated mucins in signal transduction. Trends Cell Biol 16:467–476
Tanida S, Akita K, Ishida A, Mori Y, Toda M, Inoue M, Ohta M, Yashiro M, Sawada T, Hirakawa K, Nakada H (2013) Binding of the sialic acid-binding lectin, Siglec-9, to the membrane mucin, MUC1, induces recruitment of β-catenin and subsequent cell growth. J Biol Chem 288:31842–31852
Toda M, Hisano R, Yurugi H, Akita K, Maruyama K, Inoue M, Adachi T, Tsubata T, Nakada H (2009) Ligation of tumour-produced mucins to CD22 dramatically impairs splenic marginal zone B-cells. Biochem J 417:673–683
Wang Y, Ju T, Ding X, Xia B, Wang W, Xia L, He M, Cummings RD (2010) Cosmc is an essential chaperone for correct protein O-glycosylation. Proc Natl Acad Sci U S A.107:9228–9233
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2015 Springer Japan
About this entry
Cite this entry
Nakada, H. (2015). Mucin and Cancer. In: Taniguchi, N., Endo, T., Hart, G., Seeberger, P., Wong, CH. (eds) Glycoscience: Biology and Medicine. Springer, Tokyo. https://doi.org/10.1007/978-4-431-54841-6_195
Download citation
DOI: https://doi.org/10.1007/978-4-431-54841-6_195
Received:
Accepted:
Published:
Publisher Name: Springer, Tokyo
Print ISBN: 978-4-431-54840-9
Online ISBN: 978-4-431-54841-6
eBook Packages: Biomedical and Life SciencesReference Module Biomedical and Life Sciences