MUC1

Official Full Name

mucin 1, cell surface associated

Organism

Homo sapiens

GeneID

4582

Background

This gene encodes a membrane-bound protein that is a member of the mucin family. Mucins are O-glycosylated proteins that play an essential role in forming protective mucous barriers on epithelial surfaces. These proteins also play a role in intracellular signaling. This protein is expressed on the apical surface of epithelial cells that line the mucosal surfaces of many different tissues including lung, breast stomach and pancreas. This protein is proteolytically cleaved into alpha and beta subunits that form a heterodimeric complex. The N-terminal alpha subunit functions in cell-adhesion and the C-terminal beta subunit is involved in cell signaling. Overexpression, aberrant intracellular localization, and changes in glycosylation of this protein have been associated with carcinomas. This gene is known to contain a highly polymorphic variable number tandem repeats (VNTR) domain. Alternate splicing results in multiple transcript variants.[provided by RefSeq, Feb 2011]

Synonyms

EMA; MCD; PEM; PUM; KL-6; MAM6; MCKD; PEMT; CD227; H23AG; MCKD1; MUC-1; ADMCKD; ADTKD2; Ca15-3; ADMCKD1; CA 15-3; MUC-1/X; MUC1/ZD; MUC-1/SEC;

Protein Sequence

MTPGTQSPFFLLLLLTVLTVVTGSGHASSTPGGEKETSATQRSSVPSSTEKNAVSMTSSVLSSHSPGSGSSTTQGQDVTLAPATEPASGSAATWGQDVTSVPVTRPALGSTTPPAHDVTSAPDNKPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDNRPALGSTAPPVHNVTSASGSASGSASTLVHNGTSARATTTPASKSTPFSIPSHHSDTPTTLASHSTKTDASSTHHSSVPPLTSSNHSTSPQLSTGVSFFFLSFHISNLQFNSSLEDPSTDYYQELQRDISEMFLQIYKQGGFLGLSNIKFRPGSVVVQLTLAFREGTINVHDVETQFNQYKTEAASRYNLTISDVSVSDVPFPFSAQSGAGVPGWGIALLVLVCVLVALAIVYLIALAVCQCRRKNYGQLDIFPARDTYHPMSEYPTYHTHGRYVPPSSTDRSPYEKVSAGNGGSSLSYTNPAVAATSANL

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Disease

Acute myeloid leukaemia, Bipolar disorder, Brain cancer, Breast cancer, Cervical cancer, Colorectal cancer, Esophageal cancer, Liver cancer, Lung cancer, Multiple myeloma, Myelodysplastic syndrome, Pancreatic cancer, Solid tumour/cancer, Stomach cancer

Approved Drug

Clinical Trial Drug

29 +

Discontinued Drug

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Detailed Information

MUC1 mucin (abbreviated as MUC1) is a high glycosylation, high molecular weight protein encoded by the MUC1 gene. It lubricates and protects the normal epithelium, and also mediates signal transduction and cell adhesion, immune activation and inhibition. In tumor tissues, MUC1 is often abnormally expressed, non-polarly distributed, and glycosylation is incomplete due to increased glycosyltransferase activity, which exposes the hidden epitopes under normal conditions and becomes a biological treatment target for tumors.

Figure 1. Schematic representation of the structure of MUC1. (Nath, S., et al. 2014)

MUC1 Function

MUC1 is a member of the mucin family, also known as polymorphic epithelial mucin (PEM), epithelial membrane antigen (EMA), CD227 and CA153. MUC1 has a relative molecular mass greater than 400 000 and is a transmembrane glycoprotein mainly distributed in glandular epithelial cells. The MUC1 gene is transcribed to form different cDNA products, which are encoded to produce the corresponding isoforms, membrane-bound MUC1 and secreted MUC1. Early understanding of the biological function of membrane-bound MUC1 was mainly limited to its mechanical effects such as lubrication, protection and regulation of adhesion between cells. Recent studies have found that membrane-bound MUC1 as an oncogene can lead to normal cell transformation and inhibit apoptosis.

Under normal circumstances, MUC1 is widely distributed on the surface of normal mucosa of the body. The expression of MUC1 is found at the top of the luminal surface of glandular epithelial cells such as breast, ovary, respiratory tract, gastrointestinal tract and genitourinary tract. Subsequently, bone marrow hematopoietic cells are also expressed. The study also confirmed the high expression of MUC1 in hematological malignancies. In malignant tumor tissues such as breast cancer, gastric cancer, colon cancer, multiple myeloma and other cancer tissues, the expression of MUC1 is abnormal in quality and quantity. It is embodied in the following three aspects: (1) the expression level is increased by more than 10 times of normal, and the degree of increase is proportional to the degree of malignancy of the tumor; (2) the polarity distribution disappears, and the surface of the whole glandular epithelial cells expresses MUC1. It is also expressed in the cytosol; (3) the glycosylation of the sugar chain is incomplete, the sugar chain is shortened, the branch is few, and the structure is simple, leading to the formation of new sugar chain epitopes (such as TF, Tn, STn glycoforms) and peptide chain epitopes (such as the PDTRP region), making MUC1 a tumor antigen that can be recognized by the immune system.

MUC1 and Tumor

MUC1 has abnormal expression in various degrees in various tumor tissues such as esophageal cancer, gastrointestinal cancer, breast cancer, ovarian cancer and bladder cancer. Elevated or abnormal mRNA or protein expression of MUC1 often indicates tumor invasion and metastasis and is associated with the prognosis of the patient. The mechanism may be: (1) the filamentous MUC1 molecule with high density expressed on the surface of cancer cell membrane can block the interaction between the ligand immobilized on the membrane surface and its receptor, and reduce the integrin-mediated cell-cell interaction in the extracellular matrix. It has been confirmed that the expression of M UC1 down-regulates E-eadherin, thereby causing the adhesion of tumors to each other; (2) the VN TR sequence of MUC1 is incompletely glycosylated, resulting in a change in its spatial conformation and an increase in steric hindrance, which inhibits adhesion between tumor cells and enhances the invasiveness of tumor cells; (3) the Sialy LeX epitope on MUC1 acts as a ligand for E-cadherin and interacts with E-cadherin on damaged or inflammatory endothelial cells, which causes adhesion of tumor cells to vascular endothelial cells. As a result, cancer cells tend to pass through the walls of blood vessels, facilitating tumor metastasis.

References:

Nath, S. , & Mukherjee, P. . (2014). Muc1: a multifaceted oncoprotein with a key role in cancer progression. Trends in Molecular Medicine, 20(6), 332-342.
Goode, G. , Gunda, V. , & Chaika, N. V. . (2017). Correction muc1 facilitates metabolomic reprogramming in triple-negative breast cancer. Plos One, 12(5), e0176820.
Maeda, T. , Hiraki, M. , Jin, C. , Rajabi, H. , Tagde, A. , & Alam, M. , et al. (2018). Muc1-c induces pd-l1 and immune evasion in triple-negative breast cancer. Cancer Res., 78(1), 205-215.

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