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2017 Cardiovascular Research Day Abstract Book

61 Secretory

61 Secretory phospholipase A2 group IIA (PLA2G2A) enhances metabolism and insulin sensitivity Michael Kuefner 1 • Kevin Pham 1 • JeAnna Redd 2 • Erin Stephenson, PhD 3 • Innocence Harvey 2 • Xiong Deng, PhD 1 • Dave Bridges, PhD 2 • Eric Boilard, PhD 4 • Marshal Elam, MD, PhD 1 • Edwards Park, PhD 1 1Pharmacology, University of Tennessee Health Science Center • 2 Nutritional Sciences, University of Michigan School of Public Health • 3 Physiology, University of Tennessee Health Science Center • 4Infectious Diseases and Immunity, CHUQ Research Center and Division of Rheumatology Graduate Student Secretory phospholipase A2 group IIA (PLA2G2A) is a member of a family of secretory phospholipases that have been implicated in inflammation, atherogenesis, and antibacterial actions. Here, we evaluated the role of PLA2G2A in the metabolic response to a high fat diet. C57BL/6 (BL/6) mice do not express PLA2g2a due to a frameshift mutation. We fed BL/6 mice expressing the human PLA2G2A gene (IIA+ mice) a fat diet and assessed the physiologic response. After 10 weeks on the high fat diet, the BL/6 mice were obese, but the IIA+ mice did not gain weight or accumulate lipid. The lean mass in chow- and high fat-fed IIA+ mice was constant and similar to the BL/6 mice on a chow diet. Surprisingly, the IIA+ mice had an elevated metabolic rate, which was not due to differences in physical activity. The IIA+ mice were more insulin sensitive and glucose tolerant than the BL/6 mice, even when the IIA+ mice were provided the high fat diet. The IIA+ mice had increased expression of uncoupling protein 1 (UCP1), sirtuin 1 (SIRT1), and PPARγ coactivator 1α (PGC-1α) in brown adipose tissue (BAT), suggesting that PLA2G2A activates mitochondrial uncoupling in BAT. Our data indicate that PLA2G2A has a previously undiscovered impact on insulin sensitivity and metabolism. 77

62 Making Good: Secretory Quality Control in Lipoprotein Lipase Trafficking Benjamin Roberts 1 • Saskia Neher, PhD 1 1Biochemistry and Biophysics, UNC Chapel Hill Graduate Studnet Lipoprotein lipase (LPL) is an essential vascular regulator of serum triglycerides. Patients without LPL activity suffer from hypertriglyceridemia. Chronic elevated blood triglycerides increase the risks of acute pancreatitis, atherosclerosis, and cardiac disease. There is no cure for LPL deficiency available in the United States. Of the over 70 clinical LPL clinical mutations, some affect intracellular LPL trafficking. It is clear that misfolded LPL is subject to post-Endoplasmic Reticulum (ER) quality control, which results in its degradation. The regulation of this process and the LPL partners that promote LPL degradation are not well understood. To study atypical LPL trafficking we fluorescently tagged two clinically-identified LPL variants to follow intracellular LPL transport. We also characterized the trafficking of WT LPL produced in cells lacking its folding chaperone Lipase Maturation Factor 1. Finally, we used mass spectrometry to search for intracellular binding partners unique to misfolded LPL. Using these techniques, we quantified post-ER quality control of folded and misfolded LPL. These studies enhance our understanding of the regulation in LPL trafficking and help to explain the consequences of some LPL mutations resulting in LPL deficiency. 78

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