Carcinoembryonic antigen cell adhesion molecule, CEACAM5 (CEA, CD66e) is a well known tumor marker, in particular in colorectal carcinomas, where circulating CEA is used to monitor response to chemotherapy. This GPI anchored glycoprotein belongs to the CEA-related cell adhesion molecule (CEACAM) family and shares domains identity to other members, like CEACAM6. CEA is highly expressed at the surface of tumor cells in several epithelial tumors, including CRC, lung and gastric tumors and displays a limited expression in normal tissue where it is found solely at the luminal surface of columnar absorptive cells. This prompted us to develop an anti-CEA antibody-drug conjugate (ADC) for the treatment of CEA-positive tumors.
The etymology of NY‐ESO‐1 tells the story of its origins: NY stands for the city in which it was discovered by Chen et al.(1997) , at the Ludwig Institute for Cancer Research and Weill Medical College of Cornell University in New York , in 1997; ESO is for esophageal cancer where it was originally described by screening a tumor ‐ derived cDNA expression library with autologous serum of an esophageal cancer patient; and this was the first member of a new gene family.
The function of NY‐ESO‐1 is still unknown. There is no obvious predicted functional domain or binding domain to give clues on partners in function. The promise of NY‐ESO‐1 as a candidate for specific immune recognition of cancer comes from its restricted expression in normal tissues but frequent occurrence in cancer. Although originally described from the cDNA sequences of an esophageal tumor, NY‐ESO‐1 has shown a much more widespread incidence in a number of other tumor types. Since NY‐ESO‐1 and other CT antigens seem to be more often simultaneously expressed than not, establishing patterns in human cancer may eventually help classify tumor types, potential course of action and sensitivity to therapeutic approaches, and eventually represent a predictive tool.
The p53 gene has been mapped to chromosome 17. In the cell, p53 protein binds DNA, which in turn stimulates another gene to produce a protein called p21 that interacts with a cell division-stimulating protein (cdk2). When p21 is complexed with cdk2 the cell cannot pass through to the next stage of cell division. Mutant p53 can no longer bind DNA in an effective way, and as a consequence the p21 protein is not made available to act as the 'stop signal' for cell division. Thus cells divide uncontrollably, and form tumors.
Gnjatic S et al. NY‐ESO‐1: Review of an Immunogenic Tumor Antigen[J]. Advances in cancer research, 2006, 95: 1-30.
National Center for Biotechnology Information (US). Genes and Disease [Internet]. Bethesda (MD): National Center for Biotechnology Information (US); 1998-. The p53 tumor suppressor protein. Available from: http://www.ncbi.nlm.nih.gov/books/NBK22268/