Abstract P1049: Determination Of Proteome-wide Post-translational Modifications By Lysine Acetylation In Ischemic Cardiac Cells

Abstract

Introduction: In ischemic cardiomyopathy, cardiac muscle gets damaged due to ischemia and the heart loses its ability to pump blood properly, leading to heart failure. Considering the effect of ischemic cardiomyopathy on the global population, it is vital to understand the impact of ischemia on the cardiac cells and how ischemic condition changes different cellular functions through post-translational modifications (PTM) of cellular proteins. Acetylation, one such PTM, is known to affect protein synthesis, epigenetic modification, and metabolism. This study aims to identify global acetylation changes due to ischemic conditions. Methods: Rat ventricular cardiomyocytes were exposed to reduced oxygen conditions for 12 hours, and the proteins were isolated for acetylation analysis. Mass spectrometry was performed on these proteins to analyze global changes in acetylation due to ischemia. Results: Our result shows that 180 proteins are differentially acetylated during ischemia, and these acetylated proteins are found to be localized in different subcellular organelles like mitochondria, nucleus, cytoplasm, etc. These PTMs tune the cellular protein function and regulate different cellular functions such as protein synthesis, epigenetic modification, and metabolism. Conclusion: Understanding cellular changes due to post-translational acetylation modification may help in the design of therapeutic agents against ischemia-mediated heart disease.