MUC1 is a compound protein with intensive O-linked glycosylation. Mucins line the top surface of animal tissue cells in the lungs, stomach, intestines, and other organs. Mucins shield the body from infection by infectious agent binding to oligosaccharides in the living thing domain, preventing the infectious agent from reaching the cell surface. Overexpression of MUC1 is commonly related to colon, breast, ovarian, respiratory organ and duct gland cancers.
MUC1 prevents the interaction of immune cells with receptors on the neoplastic cell surface through steric hindrance. This inhibits an anti-tumor immunologic response. Using MUC1, vaccines are being tested against a type of blood cancer referred to as myeloma. The technology in theory be applied to all best-known cancers, including prostate and carcinoma, solid and non-solid tumors. This technique would activate the system by coaching T-cells to look out and destroy cells that show a selected molecule of MUC1. MUC1 is found in many animal tissue cells, however it's expressed in cancer cells, and its associated glycans are shorter than those of non-tumor-associated MUC1.
Overexpression of MUC1 in fibroblasts accumulated the phosphorylation of Akt. MUC1 was shown to extend expression of Bcl-xL. The presence of free Bcl-2 and Bcl-xL prevents the discharge of cytochrome from mitochondria, thereby preventing cell death. MUC1 protoplasm tail is shuttled to the mitochondria through interaction with hsp90. This interaction is iatrogenic through phosphorylation of the MUC1 protoplasm. Src is activated by the EGF receptor family matter Neuregulin. The protoplasm tail is then inserted into the mitochondrial outer membrane. Localization of MUC1 to the mitochondria prevents the activation of apoptotic mechanisms.