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Mucin in Cancer: a Stealth Cloak for Cancer Cells

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Journal BMB Rep
Date 2021 Jun 22
PMID 34154702
Citations 19
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Abstract

Mucins are high molecular-weight epithelial glycoproteins and are implicated in many physiological processes, including epithelial cell protection, signaling transduction, and tissue homeostasis. Abnormality of mucus expression and structure contributes to biological properties related to human cancer progression. Tumor growth sites induce inhospitable conditions. Many kinds of research suggest that mucins provide a microenvironment to avoid hypoxia, acidic, and other biological conditions that promote cancer progression. Given that the mucus layer captures growth factors or cytokines, we propose that mucin helps to ameliorate inhospitable conditions in tumor-growing sites. Additionally, the composition and structure of mucins enable them to mimic the surface of normal epithelial cells, allowing tumor cells to escape from immune surveillance. Indeed, human cancers such as mucinous carcinoma, show a higher incidence of invasion to adjacent organs and lymph node metastasis than do non-mucinous carcinoma. In this minireview, we discuss how mucin provides a tumor-friendly environment and contributes to increased cancer malignancy in mucinous carcinoma. [BMB Reports 2021; 54(7): 344-355].

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References
1.
Chen S, Hung W, Wang P, Paul C, Konstantopoulos K . Mesothelin binding to CA125/MUC16 promotes pancreatic cancer cell motility and invasion via MMP-7 activation. Sci Rep. 2013; 3:1870. PMC: 3660778. DOI: 10.1038/srep01870. View

2.
Day F, Jorissen R, Lipton L, Mouradov D, Sakthianandeswaren A, Christie M . PIK3CA and PTEN gene and exon mutation-specific clinicopathologic and molecular associations in colorectal cancer. Clin Cancer Res. 2013; 19(12):3285-96. DOI: 10.1158/1078-0432.CCR-12-3614. View

3.
Gubbels J, Belisle J, Onda M, Rancourt C, Migneault M, Ho M . Mesothelin-MUC16 binding is a high affinity, N-glycan dependent interaction that facilitates peritoneal metastasis of ovarian tumors. Mol Cancer. 2006; 5(1):50. PMC: 1635730. DOI: 10.1186/1476-4598-5-50. View

4.
Leir S, Harris A . MUC6 mucin expression inhibits tumor cell invasion. Exp Cell Res. 2011; 317(17):2408-19. DOI: 10.1016/j.yexcr.2011.07.021. View

5.
Cherrin C, Haskell K, Howell B, Jones R, Leander K, Robinson R . An allosteric Akt inhibitor effectively blocks Akt signaling and tumor growth with only transient effects on glucose and insulin levels in vivo. Cancer Biol Ther. 2010; 9(7):493-503. PMC: 2987445. DOI: 10.4161/cbt.9.7.11100. View