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|Title:||Characterization of sarcomeric protein changes during mouse heart failure progression||Authors:||Lam, Do Thuy Uyen Ha||Keywords:||DRNTU::Science::Medicine||Issue Date:||2019||Abstract:||Cardiovascular disease, especially heart failure and its most common cause – myocardial infarction (MI), is the leading cause of morbidity and mortality. Following an MI event, the heart undergoes extensive remodelling where there is modification to the proteins especially the sarcomeric proteins responsible for the contractility function in cardiomyocytes. Although extensive studies have been done to elucidate the function of these proteins and their post-translational modifications (PTMs), little is known about the changes in expression and PTMs of these proteins during post- MI progression. In this study, we employed a mouse model of surgically-induced MI and two-dimensional gel electrophoresis to examine the changes in protein expression and phosphorylation level (the most prominent PTMs for sarcomeric proteins) following MI. We observed qualitatively an increase in tropomyosin dephosphorylation between day 10 and day 14 post-MI, quantitatively an elevated phosphorylation in myosin regulatory light chain at day 10 followed by its decrease to normal level at day 14. We also noticed a degradation of myosin binding protein C at both time-points. We conclude that following MI, sarcomeric proteins have their own timelines in adaptation to heart failure phenotype to maintain the myocyte contractility. It is unknown whether there is interaction between these timelines.||URI:||http://hdl.handle.net/10356/77111||Rights:||Nanyang Technological University||Fulltext Permission:||restricted||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SBS Student Reports (FYP/IA/PA/PI)|
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