CHED 849 |
| Vacuolar ATPases are a family of ATP-dependent proton pumps, found in a variety of intracellular compartments in eukaryotic cells. In order to acidify the vacuole, these transmembrane proteins hydrolyze ATPs to move and pump H+s. Since understanding V-ATPase function is a crucial step toward discovering new facts about kidney failure, osteoporosis, sperm motility and maturation, and cancerous cells, many researches are being performed on these special proteins. Previous studies show that glucose regulates assembly or disassembly of V-ATPase. However, the signaling pathways which connect V-ATPase dissociation and glucose metabolism have not been identified. In this project, the goal is to find “coupling points” between glycolysis and V-ATPase function through inhibition of a specific glycolytic enzyme. In vivo Phosphorus 31 NMR aimed at monitoring pH of different compartments (in response to the inhibition), using the chemical shifts of inorganic phosphates. |
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Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster
Division of Chemical Education |