OMIM :  158340

GENECARD : MUC1

CGAP : 89603

Biochemical type

• Mucins are high molecular weight glycoproteins that provide a protective layer on epithelial surfaces and are involved in cell-cell interactions, signaling, and metastasis. Parry S, Silverman HS, McDermott K, Willis A, Hollingsworth MA, Harris A.

• Biochemical characterization of the soluble form of tumor antigen MUC1. Beatty P, Hanisch FG, Stolz DB, Finn OJ, Ciborowski P.

• Mucins are high molecular weight glycoproteins having oligosaccharides attached to the apomucin protein backbone by O-glycosidic linkages. Yonezawa S, Sato E.

• MUC 1 is a type I transmembrane protein with a large number of tandem repeat consisting of 20 amino acids. Hinoda Y, Imai K.

Cell location

• MUC1 is expressed at the apical surface of ductal epithelia of tissues. Burdick MD, Harris A, Reid CJ, Iwamura T, Hollingsworth MA.

Cell type distribution

• MUC1, is a human tumor antigen expressed in breast, pancreatic and ovarian cancers. Pecher G, Spahn G, Schirrmann T, Kulbe H, Ziegner M, Schenk JA, Sandig V.

• MUC1 is expressed at the apical surface of ductal epithelia of tissues, including breast, pancreas, airway, and the gastrointestinal tract. Burdick MD, Harris A, Reid CJ, Iwamura T, Hollingsworth MA.

• MUC1 core peptide was highly expressed on apical membranes of bronchus, breast, salivary gland, pancreas, prostate, and uterus, and was sparsely expressed in gastric surface cells, gallbladder, small intestine, and colonic epithelium. Ho SB, Niehans GA, Lyftogt C, Yan PS, Cherwitz DL, Gum ET, Dahiya R, Kim YS.

Clinical

• MUC1-transfected DC would be an attractive tool in constructing cancer vaccines. Pecher G, Spahn G, Schirrmann T, Kulbe H, Ziegner M, Schenk JA, Sandig V.

• The immunohistochemical mucin expression pattern distinguishes different types of intraductal papillary mucinous neoplasms of the pancreas and determines their relationship to mucinous noncystic carcinoma and ductal adenocarcinoma. Luttges J, Zamboni G, Longnecker D, Kloppel G.

• Mucin antigen presents as a valuable marker of cancer progression and prognosis. Baldus SE, Goergen D, Hanisch FG, Dienes HP.

• Mucins in the diagnosis and therapy of pancreatic cancer. Ho JJ.

• Mucin-peptide-HSP-complexes could be the basis of developing new kinds of tumor vaccines. Schreiber J, Stahn R, Schenk JA, Karsten U, Pecher G.

• Cytotoxic immune response is directed primarily against epitopes on the tandem repeat domain of MUC1. Magarian-Blander J, Hughey RP, Kinlough C, Poland PA, Finn OJ.

• Adoptive immunotherapy for pancreatic cancer, using MUC1 specific CTL. Masaki Y, Oka M.

• Expression of mucin carbohydrates and core proteins in carcinomas of the ampulla of Vater: their relationship to prognosis. Kitamura H, Yonezawa S, Tanaka S, Kim YS, Sato E.

• New mucin core protein genes and their clinical application. Imai K.

• Analysis of mucin gene expression may be of value in the differential diagnosis of pancreatic lesions. Balague C, Audie JP, Porchet N, Real FX.

• Serological pancreatic tumor markers and the MUC1 apomucin. Ho JJ, Kim YS.

• Cytokeratins and mucins as molecular markers of cell differentiation and neoplastic transformation in the exocrine pancreas. Vila MR, Balague C, Real FX.

• Molecular biological analyses of mucin core proteins and their clinical. Application. Hinoda Y, Imai K.

• Cellular mucins: targets for immunotherapy. Apostolopoulos V, McKenzie IF.

• The "truncated" mucin molecule may represent an effective means of immunizing patients with breast and pancreatic cancer.  Magarian-Blander J, Domenech N, Finn OJ.

Development

• Developmental expression of mucin genes MUC1 and MUC2. Chambers JA, Hollingsworth MA, Trezise AE, Harris A.

DNA Structure

• Analysis of the tissue-specific promoter of the MUC1 gene. Kovarik A, Peat N, Wilson D, Gendler SJ, Taylor-Papadimitriou J.

Function

• Mucins are involved in cell-cell interactions, signaling, and metastasis. Parry S, Silverman HS, McDermott K, Willis A, Hollingsworth MA, Harris A.

• The carbohydrates of mucins on the surface of tumor cells have been reported to inhibit cells of the immune system. These carbohydrates also act as ligands during the process of tumor cell metastasis. Ho JJ.

• MUC1-derived peptides are processed and presented in the context of MHC class I molecules on the surface of tumor cells. Agrawal B, Reddish MA, Christian B, VanHeele A, Tang L, Koganty RR, Longenecker BM.

• Naturally processed class II epitope from the tumor antigen MUC1 primes human CD4+ T cells. Hiltbold EM, Ciborowski P, Finn OJ.

• MUC1 functions include lubrication and protection of the epithelia. Burdick MD, Harris A, Reid CJ, Iwamura T, Hollingsworth MA.

• Human MUC1 mucin modifies the differentiated state of human pancreatic cells by altering cytokeratin expression and reducing adhesion to type I collagen but paradoxically enhancing the cellular contractile phenotype. Hudson MJ, Stamp GW, Hollingsworth MA, Pignatelli M, Lalani EN.

• Cell adhesion to E-selectin is mediated by ligands on mucinous glycoproteins, and adhesion can be inhibited by mucins. Sawada T, Ho JJ, Chung YS, Sowa M, Kim YS.

Gene Frequencey (tumor)

• Expression of MUC apomucins in normal pancreas and pancreatic tumours. Terada T, Ohta T, Sasaki M, Nakanuma Y, Kim YS.

Ligand Binding

• Mucins of the human pancreatic cancer cell line, SW1990, have both sialyl-Lewis(a) and sialyl-Lewis(x) carbohydrate ligands that are implicated in tumor cell metastasis. Ho JJ, Siddiki B, Kim YS.

• Muc 1 is associated with several of the serological pancreatic cancer carbohydrate markers, including CA19-9.Ho JJ, Kim YS.

Oncogenicity

• Enhancement of metastatic properties of pancreatic cancer cells by MUC1 gene encoding an anti-adhesion molecule. Satoh S, Hinoda Y, Hayashi T, Burdick MD, Imai K, Hollingsworth MA.

• Sialylated MUC1 mucin may be a factor in the metastatic potential of pancreatic ductal adenocarcinoma. Masaki Y, Oka M, Ogura Y, Ueno T, Nishihara K, Tangoku A, Takahashi M, Yamamoto M, Irimura T.

• Expression of mucin antigens in human cancers and its relationship with malignancy potential. Yonezawa S, Sato E.

Protein Structure       

• MUC1 consists of an extracellular subunit and a membrane-associated subunit. Parry S, Silverman HS, McDermott K, Willis A, Hollingsworth MA, Harris A.

• MUC1 is a type I transmembrane protein with a large number of tandem repeat consisting of 20 amino acids. Imai K.

Regulation

• glycosylation of the extracellular domain of MUC1 was essential for these biological adhesive functions. Satoh S, Hinoda Y, Hayashi T, Burdick MD, Imai K, Hollingsworth MA.

• sialic acids play an important role in determining the net negative charge of sialyl-Lewis(a) and sialyl-Lewis(x) rich mucins and in obscuring MUC1 peptide regions. Ho JJ, Siddiki B, Kim YS.

• Access to peptide regions of a surface mucin (MUC1) is reduced by sialic acids. Ho JJ, Cheng S, Kim YS.

Tumor incidence

• In intraductal papillary-mucinous neoplasm (IPMN) of the pancreas (n = 9), MUC1, MUC2, MUC3, and MUC5/6 apomucins were expressed in 8/9 (89 percent), 0/9 (0 per cent), 4/9 (44 per cent), and 9/9 (100 per cent) case, respectively. Terada T, Ohta T, Sasaki M, Nakanuma Y, Kim YS.