Abstract
Glioblastoma (GBM) multiforme A is a highly variable, grade four cancer that affects the glial tissues of the brain and spinal cord. Cancer cells, including GBM, have purine metabolism markers that make them distinguishable for biochemical research, marked through the rate limiting step in the conversion of inosine monophosphate (IMP) to guanosine triphosphate (GTP), catalyzed by inosine monophosphate dehydrogenase (IMPDH). Cell cultures for both 3T3 cells, used to study normal cell cycles, and GBM cells were grown and replicated, until sufficient cells existed to extract the desired proteins. These proteins were then run through a gel electrophoresis apparatus, followed by a Western Blot analysis to immunostain the proteins, before subjecting them to various antibodies. Three different antibodies were used: actin, a biomarker for GBM prognosis, p53, a tumor marker and suppressor, and Ras, a guanosine nucleotide binding protein. Following the antibody treatments, the GBM proteins and antibodies were subjected to chemotherapy drugs, to observe if there were any changes in overall protein concentration.
College
College of Science & Engineering
Department
Chemistry
Campus
Winona
First Advisor/Mentor
Jonathon Mauser
Location
Ballroom - Kryzsko Commons
Start Date
4-18-2024 10:00 AM
End Date
4-18-2024 11:00 AM
Presentation Type
Poster Session
Format of Presentation or Performance
In-Person
Session
1b=10am-11am
Poster Number
58
Included in
Investigating Chemotherapeutic Resistance in Glioblastoma Multiforme A
Ballroom - Kryzsko Commons
Glioblastoma (GBM) multiforme A is a highly variable, grade four cancer that affects the glial tissues of the brain and spinal cord. Cancer cells, including GBM, have purine metabolism markers that make them distinguishable for biochemical research, marked through the rate limiting step in the conversion of inosine monophosphate (IMP) to guanosine triphosphate (GTP), catalyzed by inosine monophosphate dehydrogenase (IMPDH). Cell cultures for both 3T3 cells, used to study normal cell cycles, and GBM cells were grown and replicated, until sufficient cells existed to extract the desired proteins. These proteins were then run through a gel electrophoresis apparatus, followed by a Western Blot analysis to immunostain the proteins, before subjecting them to various antibodies. Three different antibodies were used: actin, a biomarker for GBM prognosis, p53, a tumor marker and suppressor, and Ras, a guanosine nucleotide binding protein. Following the antibody treatments, the GBM proteins and antibodies were subjected to chemotherapy drugs, to observe if there were any changes in overall protein concentration.
