During the development of breast cancer, tumor cells alter glycosylation of their proteins leading to changes in the growth, adhesion, signaling, and immune surveillance of the tumor. These glycosylation changes correlate with increasing tumor burden and poor prognosis. As an alternative to current immunochemical or proteomic methods for detection of breast cancer in patient serum, we have developed methods to cleave oligosaccharides (glycans) from their protein core. The resulting free glycan species are then analyzed by mass spectrometry, thereby creating a profile that contains distinct cancer glycan biomarkers. We are using these methods to determine if we can detect significant glycan differences in the supernatants of breast cancer cell lines that are not detected in a non-transformed mammary epithelial cell line. We are also using these methods to determine the glycosylation changes in a mouse model of metastatic breast cancer through analysis of mouse serum taken during the progression of it disease. Finally we are conducting serum glycan profiling on breast cancer patient sera and on sera from women without breast cancer.
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