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    Research Grants Awarded

    Serum Glycan Analysis in Breast Cancer

    Study Section:
    Detection, Diagnosis and Prognosis

    Scientific Abstract:
    A reliable method to detect early recurrent breast cancer or response to treatment is needed. During the development of breast cancer, tumor cells alter glycosylation of proteins leading to changes in the growth, adhesion, signaling, and immune surveillance of the tumor. These glycosylation changes are known to correlate with increasing tumor burden and poor prognosis. Some of the most glycosylated proteins in epithelial cells are mucins. Mucins are highly O -linked glycosylated proteins found on the cell surface and secreted by tumor cells into their extracellular environment and into the blood stream. Current immunochemical tests for MUC1, a mucin often associated with breast cancer, include CA 27.29, CA 15-3 or CA 19-9. However, these are not specific or sensitive enough for early detection or for monitoring disease, and are specifically not recommended by the American Society of Clinical Oncology. As an alternative to these immunochemical or other proteomic methods for detection of breast cancer in patient serum, we have developed methods to cleave O -linked oligosaccharides (glycans) from their protein core present in serum samples. The resulting free glycan species can be directly analyzed by mass spectrometry, thereby creating a profile that contains distinct cancer glycan biomarkers. We will use these methods in a pilot feasibility study. We will determine if we can detect significant glycan differences in the serum of breast cancer patients with and without active disease and if the glycan profile changes in women with metastatic breast cancer who are receiving active treatment.

    Lay Abstract:
    A reliable method to detect early recurrent breast cancer or response to treatment is needed. During the development of breast cancer, tumor cells change the structure of their proteins. These changes may allow cancer cells to grow, invade, and avoid detection by the body’s immune system. Change in the glycan group of proteins is termed “glycosylation” and these changes are associated with growing tumors and poor outcomes. Mucins are some of the most glycosylated proteins in cancer. MUC1 is a mucin often associated with breast cancer, and current available blood tests for MUC1 include CA 27.29, CA 15-3 or CA 19-9. However, these tests are not good enough for early detection or for monitoring disease, and are specifically not recommended by the American Society of Clinical Oncology. As an alternative, we have developed methods to remove these glycans from their proteins in patient blood samples. These free glycans can be directly examined by a powerful tool called mass spectrometry, and a distinct gylcan profile can be created. We will use these methods in a pilot feasibility study. We will determine if we can detect significant glycan differences in blood samples of breast cancer patients with and without active disease and if the glycan profile changes in women with metastatic breast cancer who are receiving active treatment.