Eicosapentaenoic acid attenuates renal lipotoxicity by restoring autophagic flux

References

• Levine B, Kroemer G. Autophagy in the pathogenesis of disease. Cell. 2008;132(1):27–42.
   PubMed Web of Science ®Google Scholar
• Choi AMK, Ryter SW, Levine B. Autophagy in human health and disease. N Engl J Med. 2013;368(7):651–662.
   PubMed Web of Science ®Google Scholar
• Mizushima N, Komatsu M. Autophagy: renovation of cells and tissues. Cell. 2011;147(4):728–741.
   PubMed Web of Science ®Google Scholar
• Clark SL. Cellular differentiation in the kidneys of newborn mice studies with the electron microscope. J Biophys Biochem Cytol. 1957;3(3):349–362.
   PubMedGoogle Scholar
• Kimura T, Takabatake Y, Takahashi A, et al. Autophagy protects the proximal tubule from degeneration and acute ischemic injury. J Am Soc Nephrol. 2011;22(5):902–913.
   PubMed Web of Science ®Google Scholar
• Namba T, Takabatake Y, Kimura T, et al. Autophagic clearance of mitochondria in the kidney copes with metabolic acidosis. J Am Soc Nephrol. 2014;25(10):2254–2266.
   PubMed Web of Science ®Google Scholar
• Yamamoto T, Takabatake Y, Kimura T, et al. Time-dependent dysregulation of autophagy: implications in aging and mitochondrial homeostasis in the kidney proximal tubule. Autophagy. 2016;12(5):801–813.
   PubMed Web of Science ®Google Scholar
• Maejima I, Takahashi A, Omori H, et al. Autophagy sequesters damaged lysosomes to control lysosomal biogenesis and kidney injury. Embo J. 2013;32(17):2336–2347.
   PubMed Web of Science ®Google Scholar
• Takahashi A, Takabatake Y, Kimura T, et al. Autophagy inhibits the accumulation of advanced glycation end products by promoting lysosomal biogenesis and function in the kidney proximal tubules. Diabetes. 2017;66(5):1359–1372.
   PubMed Web of Science ®Google Scholar
• Yamamoto T, Takabatake Y, Takahashi A, et al. High-fat diet-induced lysosomal dysfunction and impaired autophagic flux contribute to lipotoxicity in the kidney. J Am Soc Nephrol. 2017;28(5):1534–1551.
   PubMed Web of Science ®Google Scholar
• Brinton EA, Mason RP. Prescription omega-3 fatty acid products containing highly purified eicosapentaenoic acid (EPA). Lipids Health Dis. 2017;16(1):23.
   PubMedGoogle Scholar
• Wall R, Ross RP, Fitzgerald GF, et al. Fatty acids from fish: the anti-inflammatory potential of long-chain omega-3 fatty acids. Nutr Rev. 2010;68(5):280–289.
   PubMed Web of Science ®Google Scholar
• Wendel M, Heller AR. Anticancer actions of omega-3 fatty acids–current state and future perspectives. Anticancer Agents Med Chem. 2009;9(4):457–470.
   PubMed Web of Science ®Google Scholar
• Watts GF, Mori TA. Recent advances in understanding the role and use of marine ω3 polyunsaturated fatty acids in cardiovascular protection. Curr Opin Lipidol. 2011;22(1):70–71.
   PubMed Web of Science ®Google Scholar
• Mason RP, Jacob RF. Eicosapentaenoic acid inhibits glucose-induced membrane cholesterol crystalline domain formation through a potent antioxidant mechanism. Biochim Biophys Acta. 2015;1848(2):502–509.
   PubMed Web of Science ®Google Scholar
• Lu L, Okada N, Nakatani S, et al. Eicosapentaenoic acid-induced changes in membrane fluidity and cell adhesion molecules in cultured human keratinocytes. Br J Dermatol. 1995;133(2):217–222.
   PubMed Web of Science ®Google Scholar
• Yang X, Sheng W, Sun GY, et al. Effects of fatty acid unsaturation numbers on membrane fluidity and α-secretase-dependent amyloid precursor protein processing. Neurochem Int. 2011;58(3):321–329.
   PubMed Web of Science ®Google Scholar
• Borow KM, Nelson JR, Mason RP. Biologic plausibility, cellular effects, and molecular mechanisms of eicosapentaenoic acid (EPA) in atherosclerosis. Atherosclerosis. 2015;242(1):357–366.
   PubMed Web of Science ®Google Scholar
• Mason RP, Jacob RF, Shrivastava S, et al. Eicosapentaenoic acid reduces membrane fluidity, inhibits cholesterol domain formation, and normalizes bilayer width in atherosclerotic-like model membranes. Biochim Biophys Acta - Biomembr. 2016;1858(12):3131–3140.
   PubMed Web of Science ®Google Scholar
• Fukui M, Kang KS, Okada K, et al. EPA, an omega-3 fatty acid, induces apoptosis in human pancreatic cancer cells: role of ROS accumulation, caspase-8 activation, and autophagy induction. J Cell Biochem. 2013;114(1):192–203.
   PubMed Web of Science ®Google Scholar
• Gao B, Han Y-H, Wang L, et al. Eicosapentaenoic acid attenuates dexamethasome-induced apoptosis by inducing adaptive autophagy via GPR120 in murine bone marrow-derived mesenchymal stem cells. Cell Death Dis. 2016;7(5):e2235.
   PubMedGoogle Scholar
• Hsu H-C, Chen C-Y, Chiang C-H, et al. Eicosapentaenoic acid attenuated oxidative stress-induced cardiomyoblast apoptosis by activating adaptive autophagy. Eur J Nutr. 2014;53(2):541–547.
   PubMed Web of Science ®Google Scholar
• Brown WJ, Sullivan TR, Greenspan P. Nile red staining of lysosomal phospholipid inclusions. Histochemistry. 1992;97(4):349–354.
   PubMedGoogle Scholar
• Listenberger LL, Han X, Lewis SE, et al. Triglyceride accumulation protects against fatty acid-induced lipotoxicity. Proc Natl Acad Sci U S A. 2003;100(6):3077–3082.
   PubMed Web of Science ®Google Scholar
• Martina JA, Chen Y, Gucek M, et al. MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB. Autophagy. 2012;8(6):903–914.
   PubMed Web of Science ®Google Scholar
• Minami S, Yamamoto T, Takabatake Y, et al. Lipophagy maintains energy homeostasis in the kidney proximal tubule during prolonged starvation. Autophagy. 2017;13(10):1629–1647.
   PubMed Web of Science ®Google Scholar
• Bhatt-Wessel B, Jordan TW, Miller JH, et al. Role of DGAT enzymes in triacylglycerol metabolism. Arch Biochem Biophys. 2018;655:1–11.
   PubMed Web of Science ®Google Scholar
• Koliwad SK, Streeper RS, Monetti M, et al. DGAT1-dependent triacylglycerol storage by macrophages protects mice from diet-induced insulin resistance and inflammation. J Clin Invest. 2010;120(3):756–767.
   PubMed Web of Science ®Google Scholar
• Liu L, Trent CM, Fang X, et al. Cardiomyocyte-specific loss of diacylglycerol acyltransferase 1 (DGAT1) reproduces the abnormalities in lipids found in severe heart failure. J Biol Chem. 2014;289(43):29881–29891.
   PubMed Web of Science ®Google Scholar
• Ackerman D, Tumanov S, Qiu B, et al. Triglycerides promote lipid homeostasis during hypoxic stress by balancing fatty acid saturation. Cell Rep. 2018;24(2596–2605.e5). DOI:https://doi.org/10.1016/j.celrep.2018.08.015.
   Google Scholar
• Nguyen TB, Louie SM, Daniele JR, et al. DGAT1-dependent lipid droplet biogenesis protects mitochondrial function during starvation-induced autophagy. Dev Cell. 2017;42(1):9–21.e5.
   PubMed Web of Science ®Google Scholar
• Mason RP, Jacob RF, Shrivastava S, et al. Eicosapentaenoic acid reduces membrane fluidity, inhibits cholesterol domain formation, and normalizes bilayer width in atherosclerotic-like model membranes. Biochim Biophys Acta. 2016;1858(12):3131–3140.
   PubMed Web of Science ®Google Scholar
• Yasuda M, Tanaka Y, Kume S, et al. Fatty acids are novel nutrient factors to regulate mTORC1 lysosomal localization and apoptosis in podocytes. Biochim Biophys Acta. 2014;1842(7):1097–1108.
   PubMed Web of Science ®Google Scholar
• Liu M, Zhou L, Zhang B, et al. Elevation of n-3/n-6 PUFAs ratio suppresses mTORC1 and prevents colorectal carcinogenesis associated with APC mutation. Oncotarget. 2016;7(47):76944–76954.
   PubMedGoogle Scholar
• Wei H-K, Deng Z, Jiang S-Z, et al. Eicosapentaenoic acid abolishes inhibition of insulin-induced mTOR phosphorylation by LPS via PTP1B downregulation in skeletal muscle. Mol Cell Endocrinol. 2017;439(5):116–125.
   Web of Science ®Google Scholar
• Settembre C, De Cegli R, Mansueto G, et al. TFEB controls cellular lipid metabolism through a starvation-induced autoregulatory loop. Nat Cell Biol. 2013;15(6):647–658.
   PubMed Web of Science ®Google Scholar
• Herbst EAF, Paglialunga S, Gerling C, et al. Omega-3 supplementation alters mitochondrial membrane composition and respiration kinetics in human skeletal muscle. J Physiol. 2014;592(6):1341–1352.
   PubMed Web of Science ®Google Scholar
• Folch J, Lees M, Sloane Stanley GH. A simple method for the isolation and purification of total lipides from animal tissues. J Biol Chem. 1957;226(1):497–509.
   PubMed Web of Science ®Google Scholar
• Rambold AS, Cohen S, Lippincott-Schwartz J. Fatty acid trafficking in starved cells: regulation by lipid droplet lipolysis, autophagy, and mitochondrial fusion dynamics. Dev Cell. 2015;32(6):678–692.
   PubMed Web of Science ®Google Scholar
• Matsui I, Ito T, Kurihara H, et al. Snail, a transcriptional regulator, represses nephrin expression in glomerular epithelial cells of nephrotic rats. Lab Invest. 2007;87(3):273–283.
   PubMed Web of Science ®Google Scholar
• Bligh EG, Dyer WJ. A rapid method of total lipid extraction and purification. Can J Biochem Physiol. 1959;37(8):911–917.
   PubMedGoogle Scholar
• Tsugawa H, Ohta E, Izumi Y, et al. MRM-DIFF: data processing strategy for differential analysis in large scale MRM-based lipidomics studies. Front Genet. 2014;5:471.
   PubMed Web of Science ®Google Scholar
• Takeda H, Koike T, Izumi Y, et al. Lipidomic analysis of plasma lipoprotein fractions in myocardial infarction-prone rabbits. J Biosci Bioeng. 2015;120(4):476–482.
   PubMed Web of Science ®Google Scholar