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RAGE and STING Inflammatory Signaling in Breast Cancer Cells

Undergraduate #12
Discipline: Biological Sciences
Subcategory: Cancer Research

Christa Corley - Tougaloo College
Co-Author(s): Tae Kyoung Kwak and Barry Hudson, Department of Cell Biology, University of Miami Miller School of Medicine, Miami, FL



Receptor for Advanced Glycation End-products (RAGE) is a multi-ligand integral protein expressed in many cell types, and especially in cancer cells. Stimulators for interferon genes (STING) are proteins associated within the endoplasmic reticulum that response to foreign or mutated DNA in the cell. Once these receptors receive their ligand, RAGE and STING begin a signaling cascade that result in an inflammatory response. Inflammation’s association to cancer is a well-accepted concept. The most metastatic cancers are found at site with an increase in inflammation. We tested the hypothesis that RAGE signals through the STING pathway to mediate tumor inflammation. This paper focuses of finding out whether both of these proteins are found in human breast cancer cells and at what amount. Using Western Blots we will determine the protein amount of each. Preliminary results show that STING is found in high amounts in the presence of S100A9 proteins, (which is a RAGE ligand) in wild type mouse breast cancer cells. In RAGE knockout mouse breast cancer cells, STING proteins are reduced along with the S100A9 proteins. These data therefore suggest these pathways may overlap. We will determine the relative expression of RAGE / STING and their signaling pathways in human breast cancer. When comparing tumor lysates to human breast cancer cells we were able to determine that STING could be found in the micro environment rather than within the cancer cells. These data will set the stage for future work to probe the interaction of these pathways and as a therapeutic target in breast and other cancers.

Funder Acknowledgement(s): Howard Hughes Medical Institute

Faculty Advisor: Barry Hudson, bhudson@miami.edu

Role: My part included running protein assays and western blots.

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This material is based upon work supported by the National Science Foundation (NSF) under Grant No. DUE-1930047. Any opinions, findings, interpretations, conclusions or recommendations expressed in this material are those of its authors and do not represent the views of the AAAS Board of Directors, the Council of AAAS, AAAS’ membership or the National Science Foundation.

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