GPX-2 Protein Synthesis Using Recombinant E. Coli

dc.contributorSandulache, Vlad
dc.contributorSandulache, Vlad
dc.contributor.authorZaman, Ameer
dc.date.accessioned2023-07-07T01:24:55Z
dc.date.available2023-07-07T01:24:55Z
dc.date.issued2023-04-13
dc.description.abstractChemotherapeutic treatments for Head and Neck Squamous Cell Carcinoma (HNSCC), though sometimes unsuccessful, cause high levels of oxidative stress in cancer cells. Chemotherapy provides a selection pressure that forces cancer cells to alter their metabolism and upregulate certain processes to continue to replicate under these new stressors.1 GPX-2, or glutathione peroxidase 2, is part of a family of antioxidants. Under chemotherapeutic pressures, a significant overexpression of the GPX-2 system that is involved with fatty acid oxidation, oxidative stress, and protein processing is observed. 2. Because of its role in mobilizing a response to chemotherapeutic agents and potentially affecting cancer cell resistance, it is a promising target for small molecule inhibition. In our research, we show the synthesis of this integral protein using a three-plasmid system in an E. Coli model.
dc.description.departmentHonors College
dc.description.departmentBiology and Biochemistry, Department of
dc.identifier.urihttps://hdl.handle.net/10657/14917
dc.language.isoen
dc.rightsThe author of this work is the copyright owner. UH Libraries and the Texas Digital Library have their permission to store and provide access to this work. Further transmission, reproduction, or presentation of this work is prohibited except with permission of the author(s).
dc.subjectBiology
dc.titleGPX-2 Protein Synthesis Using Recombinant E. Coli
dc.typePoster

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