Acyl peptide enzyme hydrolase, abbreviated as APEH, is a cytosolic protease with both exopeptidase and endopeptidase activities. APEH is primarily responsible for the removal of N-terminal acetylated amino acids from its peptide substrates; however, APEH can also internally cleave proteins that have become oxidized (hence is also called Oxidized Protein Hydrolase). APEH appears to play a cytoprotective role since it has been reported to have reduced activity in type-two diabetes, Alzheimer's disease, and various cancers. One mechanism of APEH's reduced activity comes from enzyme inhibition by inflammatory mediators, suggesting that diseases associated with chronic inflammation would have reduced APEH activity. A recent paper showed that APEH enzyme can be activated with various tea extracts and this activation of APEH may be included among the many health benefits of drinking tea. For this project, we are building on that work by investigating other potential activators of APEH. To start, a selection of vitamins has been considered and is being tested to identify activators of APEH using enzyme kinetics. Finding additional activators with known chemical structures is beneficial to elucidating how APEH is regulated in the cell. Understanding how APEH can be activated may be therapeutically-desired in diseases associated with APEH down-regulation and chronic inflammation.
University / Institution: Weber State University
Format: In Person
SESSION D (3:30-5:00PM)
Faculty Mentor: Tracy Covey