Evaluation of glucose transmembrane protein activity during competitive binding in glioblastoma under normal and low oxygen conditions

Glucose is the primary substrate that cancer cells use to grow and produce lactate. Cancer cells use lactate to sustain the tumor microenvironment and facilitate cancer growth. 2-deoxy-glucose (2-DG) is a glucose analog which acts as a competitive inhibitor by binding onto glucose transmembrane proteins and prevents cancer growth via limiting hexokinase phosphorylation, preventing glycolysis through stopping production of glucose-6-phosphate (G6P). However, in glioblastoma, it is relatively unknown whether affinity of 2-DG for glucose transmembrane proteins changes over time when glucose is present under different levels of oxygen exposure. In this study, we supplement biological assays testing glucose transmembrane protein expression related to ligand binding affinity of 2-DG under normal oxygen (i.e., 20% O₂) and low oxygen (i.e., 2% O₂) exposure with a variety of nuclear magnetic resonance (NMR) analysis. The purpose of this study is to better understand the relationship between oxygen exposure and changes in transmembrane protein activity over time in glioblastoma cells.