MUC1 and the MUCs: A Family of Human Mucins with Impact in Cancer Biology

@article{Baldus2004MUC1AT,
  title={MUC1 and the MUCs: A Family of Human Mucins with Impact in Cancer Biology},
  author={Stephan Ernst Baldus and Katja Engelmann and Franz-Georg Hanisch},
  journal={Critical Reviews in Clinical Laboratory Sciences},
  year={2004},
  volume={41},
  pages={189 - 231}
}
Mucins represent a family of glycoproteins characterized by repeat domains and a dense O-glycosylation. During the last two decades, the gene and peptide structures of various mucins as well as their glycosylation states were partly elucidated. Characteristic tumor-associated alterations of the expression patterns and glycosylation profiles were observed in biochemical, immunochemical, and histological studies and are discussed in the light of efforts to use the most prominent member in this… 
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192 Citations

Analysis of mucins: role in laboratory diagnosis
  • A. Mall
  • Biology, Medicine
    Journal of Clinical Pathology
  • 2008
TLDR
The emerging roles of mucins such as MUC1 and MUC4 in cancer and some other diseases are discussed, and how underglycosylated and truncated mucins are exploited as markers of disease and to monitor widespread metastasis is stressed, making them useful in patient management.
Reflections on MUC1 glycoprotein: the hidden potential of isoforms in carcinogenesis
TLDR
This review aims to encompass a detailed characterization of MUC1 role in carcinogenesis, highlighting recent findings in cell differentiation and uncovering new evidences of M UC1 isoforms involvement in malignant phenotype.
MUC1: A target molecule for cancer therapy
MUC1 is a mucin family protein, overexpressed in more than 90 % of breast cancers in an underglycosylated form, exposing the core peptides of the extracellular domain that act as a potential target…
Overexpression and altered glycosylation of MUC1 in malignant mesothelioma
TLDR
The results suggest that specific MUC1 characteristics may be useful for mesothelioma diagnosis and should also be investigated as a potential therapeutic target.
Mucin-type O-glycosylation and its potential use in drug and vaccine development.
Tn Glycosylation of the MUC6 Protein Modulates Its Immunogenicity and Promotes the Induction of Th17-biased T Cell Responses*
TLDR
Results indicate that Tn glycosylation of the MUC6 protein strongly affects its B and T cell immunogenicity, and might favor immune escape of tumor cells.
MUC1 and metastatic cancer
TLDR
The role of M UC1 in metastatic progression is addressed by assessing clinical studies reporting MUC1 levels at various disease stages, reviewing mouse models utilized to study the role, and discussing mechanisms of Muc1 upregulation.
Transmembrane mucins as novel therapeutic targets
TLDR
Rises in the normally low levels of mucin fragments in serum have been used as markers of disease, such as tumor burden, for many years and several approaches are being examined that target mucins for immunization or nanomedicine using mucin-specific antibodies.
Characterization of cancer associated mucin type O-glycans using the exchange sialylation properties of mammalian sialyltransferase ST3Gal-II.
TLDR
Overall, the exchange sialylation property of ST3Gal-II provides an efficient avenue to identify mucinous proteins for applications in glycoproteomics and cancer research.
The mucin-type glycosylating enzyme polypeptide N-acetylgalactosaminyltransferase 14 promotes the migration of ovarian cancer by modifying mucin 13.
TLDR
Evidence that GALNT14 may contribute to ovarian carcinogenesis through aberrant glycosylation of MUC13, but not through the IL-8 pathway is provided, providing novel insights into understanding the function of M UC13 on neoplasm metastasis and may aid in the development of new anticancer drugs for EOC.
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References

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TLDR
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