請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/85097
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 姜至剛(Chih-Kang Chiang) | |
dc.contributor.author | Chong-Sun Khoi | en |
dc.contributor.author | 許崇善 | zh_TW |
dc.date.accessioned | 2023-03-19T22:43:27Z | - |
dc.date.copyright | 2022-10-03 | |
dc.date.issued | 2022 | |
dc.date.submitted | 2022-08-12 | |
dc.identifier.citation | 1. Garbarino, J. and S.L. Sturley, Saturated with fat: new perspectives on lipotoxicity. Curr Opin Clin Nutr Metab Care, 2009. 12(2): p. 110-6. 2. Weinberg, J.M., Lipotoxicity. Kidney Int, 2006. 70(9): p. 1560-6. 3. Lim, S. and J.B. Meigs, Ectopic fat and cardiometabolic and vascular risk. Int J Cardiol, 2013. 169(3): p. 166-76. 4. Nishi, H., T. Higashihara, and R. Inagi, Lipotoxicity in Kidney, Heart, and Skeletal Muscle Dysfunction. Nutrients, 2019. 11(7). 5. Kimura, I., et al., Free Fatty Acid Receptors in Health and Disease. Physiol Rev, 2020. 100(1): p. 171-210. 6. White, B., Dietary fatty acids. Am Fam Physician, 2009. 80(4): p. 345-50. 7. Abumrad, N.A. and N.O. Davidson, Role of the gut in lipid homeostasis. Physiol Rev, 2012. 92(3): p. 1061-85. 8. Miao, X., et al., Data-Independent Acquisition-Based Quantitative Proteomic Analysis Reveals the Protective Effect of Apigenin on Palmitate-Induced Lipotoxicity in Human Aortic Endothelial Cells. J Agric Food Chem, 2020. 68(33): p. 8836-8846. 9. Pilz, S. and W. Marz, Free fatty acids as a cardiovascular risk factor. Clin Chem Lab Med, 2008. 46(4): p. 429-34. 10. Flood, V.M., et al., Fatty acid intakes and food sources in a population of older Australians. Asia Pac J Clin Nutr, 2007. 16(2): p. 322-30. 11. Ahn, J., et al., Trends in the Intake of Fatty Acids and Their Food Source According to Obese Status Among Korean Adult Population Using KNHANES 2007-2017. Food Nutr Bull, 2020. 41(1): p. 77-88. 12. Davies, I.G., et al., Saturated and trans-fatty acids in UK takeaway food. Int J Food Sci Nutr, 2016. 67(3): p. 217-24. 13. Te Morenga, L. and J.M. Montez, Health effects of saturated and trans-fatty acid intake in children and adolescents: Systematic review and meta-analysis. PLoS One, 2017. 12(11): p. e0186672. 14. Innis, S.M., Palmitic Acid in Early Human Development. Crit Rev Food Sci Nutr, 2016. 56(12): p. 1952-9. 15. Abdelmagid, S.A., et al., Comprehensive profiling of plasma fatty acid concentrations in young healthy Canadian adults. PLoS One, 2015. 10(2): p. e0116195. 16. Ibrahim, A., et al., Local Mitochondrial ATP Production Regulates Endothelial Fatty Acid Uptake and Transport. Cell Metab, 2020. 32(2): p. 309-319 e7. 17. Lee, G.S., et al., Fatty Acid-Binding Protein 5 Mediates the Uptake of Fatty Acids, but not Drugs, Into Human Brain Endothelial Cells. J Pharm Sci, 2018. 107(4): p. 1185-1193. 18. Son, N.H., et al., Endothelial cell CD36 optimizes tissue fatty acid uptake. J Clin Invest, 2018. 128(10): p. 4329-4342. 19. Ibrahim, A., et al., Insulin-stimulated adipocytes secrete lactate to promote endothelial fatty acid uptake and transport. J Cell Sci, 2022. 135(5). 20. Wang, H., et al., Pigment Epithelial-Derived Factor Deficiency Accelerates Atherosclerosis Development via Promoting Endothelial Fatty Acid Uptake in Mice With Hyperlipidemia. J Am Heart Assoc, 2019. 8(22): p. e013028. 21. Rohlenova, K., et al., Endothelial Cell Metabolism in Health and Disease. Trends Cell Biol, 2018. 28(3): p. 224-236. 22. Bierhansl, L., et al., Central Role of Metabolism in Endothelial Cell Function and Vascular Disease. Physiology (Bethesda), 2017. 32(2): p. 126-140. 23. Schoors, S., et al., Fatty acid carbon is essential for dNTP synthesis in endothelial cells. Nature, 2015. 520(7546): p. 192-197. 24. Potente, M. and T. Makinen, Vascular heterogeneity and specialization in development and disease. Nat Rev Mol Cell Biol, 2017. 18(8): p. 477-494. 25. Incalza, M.A., et al., Oxidative stress and reactive oxygen species in endothelial dysfunction associated with cardiovascular and metabolic diseases. Vascul Pharmacol, 2018. 100: p. 1-19. 26. Endemann, D.H. and E.L. Schiffrin, Endothelial dysfunction. J Am Soc Nephrol, 2004. 15(8): p. 1983-92. 27. Pate, M., et al., Endothelial cell biology: role in the inflammatory response. Adv Clin Chem, 2010. 52: p. 109-30. 28. Cui, Y., et al., κ-Opioid receptor stimulation reduces palmitate-induced apoptosis via Akt/eNOS signaling pathway. Lipids Health Dis, 2019. 18(1): p. 52. 29. Zhan, X.R., et al., Life and death of human vascular endothelial cells by stimulation with free fatty acids through death receptors. Horm Metab Res, 2015. 47(2): p. 107-13. 30. Wu, Y., et al., MiR-3691-5p is upregulated in docosahexaenoic acid-treated vascular endothelial cell and targets serpin family E member 1. J Cell Biochem, 2020. 121(3): p. 2363-2371. 31. Zhai, J., et al., Salvianolic Acid B Attenuates Apoptosis of HUVEC Cells Treated with High Glucose or High Fat via Sirt1 Activation. Evid Based Complement Alternat Med, 2019. 2019: p. 9846325. 32. Qiu, L., et al., Honokiol ameliorates endothelial dysfunction through suppression of PTX3 expression, a key mediator of IKK/IκB/NF-κB, in atherosclerotic cell model. Exp Mol Med, 2015. 47(7): p. e171. 33. Gan, Y.R., et al., Dickkopf‑1/cysteine‑rich angiogenic inducer 61 axis mediates palmitic acid‑induced inflammation and apoptosis of vascular endothelial cells. Mol Med Rep, 2021. 23(2). 34. Chen, L., et al., Activating transcription factor 4 regulates angiogenesis under lipid overload via methionine adenosyltransferase 2A-mediated endothelial epigenetic alteration. Faseb j, 2021. 35(6): p. e21612. 35. Wang, M., et al., Proteome-scale profiling reveals MAFF and MAFG as two novel key transcription factors involved in palmitic acid-induced umbilical vein endothelial cell apoptosis. BMC Cardiovasc Disord, 2021. 21(1): p. 448. 36. Lee, D.M., et al., Monounsaturated fatty acids protect against palmitate-induced lipoapoptosis in human umbilical vein endothelial cells. PLoS One, 2019. 14(12): p. e0226940. 37. Wang, J., et al., Clopidogrel reduces apoptosis and promotes proliferation of human vascular endothelial cells induced by palmitic acid via suppression of the long non-coding RNA HIF1A-AS1 in vitro. Mol Cell Biochem, 2015. 404(1-2): p. 203-10. 38. Khan, M.J., et al., Inhibition of autophagy rescues palmitic acid-induced necroptosis of endothelial cells. J Biol Chem, 2012. 287(25): p. 21110-20. 39. Hu, Q., et al., Dihydromyricetin inhibits NLRP3 inflammasome-dependent pyroptosis by activating the Nrf2 signaling pathway in vascular endothelial cells. Biofactors, 2018. 44(2): p. 123-136. 40. Pober, J.S. and W.C. Sessa, Evolving functions of endothelial cells in inflammation. Nat Rev Immunol, 2007. 7(10): p. 803-15. 41. Ishida, T., et al., Eicosapentaenoic Acid Prevents Saturated Fatty Acid-Induced Vascular Endothelial Dysfunction: Involvement of Long-Chain Acyl-CoA Synthetase. J Atheroscler Thromb, 2015. 22(11): p. 1172-85. 42. Zhao, W., et al., Adiponectin protects palmitic acid induced endothelial inflammation and insulin resistance via regulating ROS/IKKβ pathways. Cytokine, 2016. 88: p. 167-176. 43. Bharat, D., et al., Blueberry Metabolites Attenuate Lipotoxicity-Induced Endothelial Dysfunction. Mol Nutr Food Res, 2018. 62(2). 44. Rao, C., et al., Nucleophosmin contributes to vascular inflammation and endothelial dysfunction in atherosclerosis progression. J Thorac Cardiovasc Surg, 2021. 161(5): p. e377-e393. 45. Shi, X., et al., Clinopodium chinense Attenuates Palmitic Acid-Induced Vascular Endothelial Inflammation and Insulin Resistance through TLR4-Mediated NF- κ B and MAPK Pathways. Am J Chin Med, 2019. 47(1): p. 97-117. 46. He, B., et al., Homoplantaginin Inhibits Palmitic Acid-induced Endothelial Cells Inflammation by Suppressing TLR4 and NLRP3 Inflammasome. J Cardiovasc Pharmacol, 2016. 67(1): p. 93-101. 47. Ren, G., et al., Long-chain acyl-CoA synthetase-1 mediates the palmitic acid-induced inflammatory response in human aortic endothelial cells. Am J Physiol Endocrinol Metab, 2020. 319(5): p. E893-e903. 48. Mao, Y., et al., STING-IRF3 Triggers Endothelial Inflammation in Response to Free Fatty Acid-Induced Mitochondrial Damage in Diet-Induced Obesity. Arterioscler Thromb Vasc Biol, 2017. 37(5): p. 920-929. 49. Szendroedi, J., et al., Lipid-induced insulin resistance is not mediated by impaired transcapillary transport of insulin and glucose in humans. Diabetes, 2012. 61(12): p. 3176-80. 50. Wei, Y., D. Wang, and M.J. Pagliassotti, Saturated fatty acid-mediated endoplasmic reticulum stress and apoptosis are augmented by trans-10, cis-12-conjugated linoleic acid in liver cells. Mol Cell Biochem, 2007. 303(1-2): p. 105-13. 51. Hetz, C., The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat Rev Mol Cell Biol, 2012. 13(2): p. 89-102. 52. Inagi, R., Y. Ishimoto, and M. Nangaku, Proteostasis in endoplasmic reticulum--new mechanisms in kidney disease. Nat Rev Nephrol, 2014. 10(7): p. 369-78. 53. Ghemrawi, R., S.F. Battaglia-Hsu, and C. Arnold, Endoplasmic Reticulum Stress in Metabolic Disorders. Cells, 2018. 7(6). 54. Almanza, A., et al., Endoplasmic reticulum stress signalling - from basic mechanisms to clinical applications. FEBS J, 2019. 286(2): p. 241-278. 55. Li, Y., et al., Ilexgenin A inhibits endoplasmic reticulum stress and ameliorates endothelial dysfunction via suppression of TXNIP/NLRP3 inflammasome activation in an AMPK dependent manner. Pharmacol Res, 2015. 99: p. 101-15. 56. Lu, Y., et al., Endoplasmic reticulum stress involved in high-fat diet and palmitic acid-induced vascular damages and fenofibrate intervention. Biochem Biophys Res Commun, 2015. 458(1): p. 1-7. 57. Luo, R., et al., Mesenchymal stem cells alleviate palmitic acid-induced endothelial-to-mesenchymal transition by suppressing endoplasmic reticulum stress. Am J Physiol Endocrinol Metab, 2020. 319(6): p. E961-e980. 58. Gustavo Vazquez-Jimenez, J., et al., Palmitic acid but not palmitoleic acid induces insulin resistance in a human endothelial cell line by decreasing SERCA pump expression. Cell Signal, 2016. 28(1): p. 53-9. 59. Hansen, M., D.C. Rubinsztein, and D.W. Walker, Autophagy as a promoter of longevity: insights from model organisms. Nat Rev Mol Cell Biol, 2018. 19(9): p. 579-593. 60. Jiang, F., Autophagy in vascular endothelial cells. Clin Exp Pharmacol Physiol, 2016. 43(11): p. 1021-1028. 61. Kroemer, G., G. Marino, and B. Levine, Autophagy and the integrated stress response. Mol Cell, 2010. 40(2): p. 280-93. 62. Khandia, R., et al., A Comprehensive Review of Autophagy and Its Various Roles in Infectious, Non-Infectious, and Lifestyle Diseases: Current Knowledge and Prospects for Disease Prevention, Novel Drug Design, and Therapy. Cells, 2019. 8(7). 63. Dikic, I. and Z. Elazar, Mechanism and medical implications of mammalian autophagy. Nat Rev Mol Cell Biol, 2018. 19(6): p. 349-364. 64. Chen, P., et al., Palmitic acid-induced autophagy increases reactive oxygen species via the Ca(2+)/PKCα/NOX4 pathway and impairs endothelial function in human umbilical vein endothelial cells. Exp Ther Med, 2019. 17(4): p. 2425-2432. 65. Zhao, Q., et al., Naringenin Exerts Cardiovascular Protective Effect in a Palmitate-Induced Human Umbilical Vein Endothelial Cell Injury Model via Autophagy Flux Improvement. Mol Nutr Food Res, 2019. 63(24): p. e1900601. 66. Lee, J., et al., C1q/TNF-related protein-9 attenuates palmitic acid-induced endothelial cell senescence via increasing autophagy. Mol Cell Endocrinol, 2021. 521: p. 111114. 67. Zhou, X., et al., Resveratrol attenuates endothelial oxidative injury by inducing autophagy via the activation of transcription factor EB. Nutr Metab (Lond), 2019. 16: p. 42. 68. Song, J., et al., Resveratrol reduces intracellular reactive oxygen species levels by inducing autophagy through the AMPK-mTOR pathway. Front Med, 2018. 12(6): p. 697-706. 69. Mahmoud, A.M., et al., A novel role for small molecule glycomimetics in the protection against lipid-induced endothelial dysfunction: Involvement of Akt/eNOS and Nrf2/ARE signaling. Biochim Biophys Acta Gen Subj, 2017. 1861(1 Pt A): p. 3311-3322. 70. Li, X., et al., Acid Sphingomyelinase Down-regulation Alleviates Vascular Endothelial Insulin Resistance in Diabetic Rats. Basic Clin Pharmacol Toxicol, 2018. 123(6): p. 645-659. 71. Wang, Y., et al., Oxidative stress induced by palmitic acid modulates K(Ca)2.3 channels in vascular endothelium. Exp Cell Res, 2019. 383(2): p. 111552. 72. Yang, Q., et al., Activation of Nrf2 by Phloretin Attenuates Palmitic Acid-Induced Endothelial Cell Oxidative Stress via AMPK-Dependent Signaling. J Agric Food Chem, 2019. 67(1): p. 120-131. 73. Han, L., et al., Protocatechuic Acid Ameliorated Palmitic-Acid-Induced Oxidative Damage in Endothelial Cells through Activating Endogenous Antioxidant Enzymes via an Adenosine-Monophosphate-Activated-Protein-Kinase-Dependent Pathway. J Agric Food Chem, 2018. 66(40): p. 10400-10409. 74. Ke, J., et al., Synergistic effects of metformin with liraglutide against endothelial dysfunction through GLP-1 receptor and PKA signalling pathway. Sci Rep, 2017. 7: p. 41085. 75. Wang, L., et al., MD2 Blockage Protects Obesity-Induced Vascular Remodeling via Activating AMPK/Nrf2. Obesity (Silver Spring), 2017. 25(9): p. 1532-1539. 76. Kirkman, D.L., et al., Mitochondrial contributions to vascular endothelial dysfunction, arterial stiffness, and cardiovascular diseases. Am J Physiol Heart Circ Physiol, 2021. 320(5): p. H2080-H2100. 77. Broniarek, I., A. Koziel, and W. Jarmuszkiewicz, The effect of chronic exposure to high palmitic acid concentrations on the aerobic metabolism of human endothelial EA.hy926 cells. Pflugers Arch, 2016. 468(9): p. 1541-54. 78. Yuan, L., et al., Palmitic acid dysregulates the Hippo-YAP pathway and inhibits angiogenesis by inducing mitochondrial damage and activating the cytosolic DNA sensor cGAS-STING-IRF3 signaling mechanism. J Biol Chem, 2017. 292(36): p. 15002-15015. 79. Zhang, B., et al., D-chiro-inositol enriched Fagopyrum tataricum (L.) Gaench extract alleviates mitochondrial malfunction and inhibits ER stress/JNK associated inflammation in the endothelium. J Ethnopharmacol, 2018. 214: p. 83-89. 80. Yang, J., et al., Resveratrol attenuates oxidative injury in human umbilical vein endothelial cells through regulating mitochondrial fusion via TyrRS-PARP1 pathway. Nutr Metab (Lond), 2019. 16: p. 9. 81. Janus, A., et al., Insulin Resistance and Endothelial Dysfunction Constitute a Common Therapeutic Target in Cardiometabolic Disorders. Mediators Inflamm, 2016. 2016: p. 3634948. 82. Fratantonio, D., et al., Cyanidin-3-O-glucoside ameliorates palmitate-induced insulin resistance by modulating IRS-1 phosphorylation and release of endothelial derived vasoactive factors. Biochim Biophys Acta Mol Cell Biol Lipids, 2017. 1862(3): p. 351-357. 83. Li, C.Y., et al., Phlorizin Exerts Direct Protective Effects on Palmitic Acid (PA)-Induced Endothelial Dysfunction by Activating the PI3K/AKT/eNOS Signaling Pathway and Increasing the Levels of Nitric Oxide (NO). Med Sci Monit Basic Res, 2018. 24: p. 1-9. 84. Moran, M., et al., Transcriptome analysis-identified long noncoding RNA CRNDE in maintaining endothelial cell proliferation, migration, and tube formation. Sci Rep, 2019. 9(1): p. 19548. 85. Zhao, Y., et al., Overexpression of microRNA‑155 alleviates palmitate‑induced vascular endothelial cell injury in human umbilical vein endothelial cells by negatively regulating the Wnt signaling pathway. Mol Med Rep, 2019. 20(4): p. 3527-3534. 86. Waldherr, S.M., et al., Constitutive XBP-1s-mediated activation of the endoplasmic reticulum unfolded protein response protects against pathological tau. Nat Commun, 2019. 10(1): p. 4443. 87. Imanikia, S., et al., Neuronal XBP-1 Activates Intestinal Lysosomes to Improve Proteostasis in C. elegans. Curr Biol, 2019. 29(14): p. 2322-2338 e7. 88. Martin, D., et al., Unspliced X-box-binding protein 1 (XBP1) protects endothelial cells from oxidative stress through interaction with histone deacetylase 3. J Biol Chem, 2014. 289(44): p. 30625-34. 89. Yang, L., et al., Unspliced XBP1 Counteracts beta-Catenin to Inhibit Vascular Calcification. Circ Res, 2022. 130(2): p. 213-229. 90. Zhang, M., et al., LncRNA DANCR attenuates brain microvascular endothelial cell damage induced by oxygen-glucose deprivation through regulating of miR-33a-5p/XBP1s. Aging (Albany NY), 2020. 12(2): p. 1778-1791. 91. Li, J., J.J. Wang, and S.X. Zhang, Preconditioning with endoplasmic reticulum stress mitigates retinal endothelial inflammation via activation of X-box binding protein 1. J Biol Chem, 2011. 286(6): p. 4912-21. 92. Duan, Q., et al., MicroRNA-214 Is Upregulated in Heart Failure Patients and Suppresses XBP1-Mediated Endothelial Cells Angiogenesis. J Cell Physiol, 2015. 230(8): p. 1964-73. 93. Hosoi, T., M. Nakashima, and K. Ozawa, Incorporation of the Endoplasmic Reticulum Stress-Induced Spliced Form of XBP1 mRNA in the Exosomes. Front Physiol, 2018. 9: p. 1357. 94. Zeng, L., et al., Sustained activation of XBP1 splicing leads to endothelial apoptosis and atherosclerosis development in response to disturbed flow. Proc Natl Acad Sci U S A, 2009. 106(20): p. 8326-31. 95. Ong, C.K., et al., Genomic structure of human OKL38 gene and its differential expression in kidney carcinogenesis. J Biol Chem, 2004. 279(1): p. 743-54. 96. Hu, J., et al., Interaction of OKL38 and p53 in regulating mitochondrial structure and function. PLoS One, 2012. 7(8): p. e43362. 97. Li, R., et al., OKL38 is an oxidative stress response gene stimulated by oxidized phospholipids. J Lipid Res, 2007. 48(3): p. 709-15. 98. Yan, X., et al., Fatty acid epoxyisoprostane E2 stimulates an oxidative stress response in endothelial cells. Biochem Biophys Res Commun, 2014. 444(1): p. 69-74. 99. Romanoski, C.E., et al., Network for activation of human endothelial cells by oxidized phospholipids: a critical role of heme oxygenase 1. Circ Res, 2011. 109(5): p. e27-41. 100. Zeng, X., et al., Oleic acid ameliorates palmitic acid induced hepatocellular lipotoxicity by inhibition of ER stress and pyroptosis. Nutr Metab (Lond), 2020. 17: p. 11. 101. Escoula, Q., et al., Docosahexaenoic and Eicosapentaenoic Acids Prevent Altered-Muc2 Secretion Induced by Palmitic Acid by Alleviating Endoplasmic Reticulum Stress in LS174T Goblet Cells. Nutrients, 2019. 11(9). 102. Chen, Z., et al., Melatonin attenuates palmitic acid-induced mouse granulosa cells apoptosis via endoplasmic reticulum stress. J Ovarian Res, 2019. 12(1): p. 43. 103. Zhang, Y., et al., Chlorogenic acid against palmitic acid in endoplasmic reticulum stress-mediated apoptosis resulting in protective effect of primary rat hepatocytes. Lipids Health Dis, 2018. 17(1): p. 270. 104. Read, A. and M. Schroder, The Unfolded Protein Response: An Overview. Biology (Basel), 2021. 10(5). 105. Li, M., et al., ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1. Mol Cell Biol, 2000. 20(14): p. 5096-106. 106. Oyadomari, S. and M. Mori, Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ, 2004. 11(4): p. 381-9. 107. Lenna, S., R. Han, and M. Trojanowska, Endoplasmic reticulum stress and endothelial dysfunction. IUBMB Life, 2014. 66(8): p. 530-7. 108. Icli, B., et al., MicroRNA-615-5p Regulates Angiogenesis and Tissue Repair by Targeting AKT/eNOS (Protein Kinase B/Endothelial Nitric Oxide Synthase) Signaling in Endothelial Cells. Arterioscler Thromb Vasc Biol, 2019. 39(7): p. 1458-1474. 109. Lee, W.S., W.H. Yoo, and H.J. Chae, ER Stress and Autophagy. Curr Mol Med, 2015. 15(8): p. 735-45. 110. Schlafli, A.M., et al., Prognostic value of the autophagy markers LC3 and p62/SQSTM1 in early-stage non-small cell lung cancer. Oncotarget, 2016. 7(26): p. 39544-39555. 111. Levine, B., N. Mizushima, and H.W. Virgin, Autophagy in immunity and inflammation. Nature, 2011. 469(7330): p. 323-35. 112. Wouters, K., et al., Understanding hyperlipidemia and atherosclerosis: lessons from genetically modified apoe and ldlr mice. Clin Chem Lab Med, 2005. 43(5): p. 470-9. 113. Ghosh, A., et al., Role of free fatty acids in endothelial dysfunction. J Biomed Sci, 2017. 24(1): p. 50. 114. Theodorou, K. and R.A. Boon, Endothelial Cell Metabolism in Atherosclerosis. Front Cell Dev Biol, 2018. 6: p. 82. 115. Listenberger, L.L., D.S. Ory, and J.E. Schaffer, Palmitate-induced apoptosis can occur through a ceramide-independent pathway. J Biol Chem, 2001. 276(18): p. 14890-5. 116. Cui, W., et al., Free fatty acid induces endoplasmic reticulum stress and apoptosis of beta-cells by Ca2+/calpain-2 pathways. PLoS One, 2013. 8(3): p. e59921. 117. Lu, X., J. Drocco, and E.F. Wieschaus, Cell cycle regulation via inter-nuclear communication during the early embryonic development of Drosophila melanogaster. Cell Cycle, 2010. 9(14): p. 2908-10. 118. Vion, A.C., et al., Autophagy is required for endothelial cell alignment and atheroprotection under physiological blood flow. Proc Natl Acad Sci U S A, 2017. 114(41): p. E8675-E8684. 119. Zou, J., et al., Autophagy attenuates endothelial-to-mesenchymal transition by promoting Snail degradation in human cardiac microvascular endothelial cells. Biosci Rep, 2017. 37(5). 120. Wang, K., et al., Naringin inhibits autophagy mediated by PI3K-Akt-mTOR pathway to ameliorate endothelial cell dysfunction induced by high glucose/high fat stress. Eur J Pharmacol, 2020. 874: p. 173003. 121. Chen, X., et al., Chaiqi decoction ameliorates vascular endothelial injury in metabolic syndrome by upregulating autophagy. Am J Transl Res, 2020. 12(9): p. 4902-4922. 122. Zeng, L., et al., Vascular endothelial cell growth-activated XBP1 splicing in endothelial cells is crucial for angiogenesis. Circulation, 2013. 127(16): p. 1712-22. 123. Xu, X., et al., IRE1alpha/XBP1s branch of UPR links HIF1alpha activation to mediate ANGII-dependent endothelial dysfunction under particulate matter (PM) 2.5 exposure. Sci Rep, 2017. 7(1): p. 13507. 124. Zhang, Z., et al., The unfolded protein response regulates hepatic autophagy by sXBP1-mediated activation of TFEB. Autophagy, 2021. 17(8): p. 1841-1855. 125. Sharma, M., et al., Japanese encephalitis virus activates autophagy through XBP1 and ATF6 ER stress sensors in neuronal cells. J Gen Virol, 2017. 98(5): p. 1027-1039. 126. Zhang, X., et al., Induction of autophagy-dependent apoptosis in cancer cells through activation of ER stress: an uncovered anti-cancer mechanism by anti-alcoholism drug disulfiram. Am J Cancer Res, 2019. 9(6): p. 1266-1281. 127. Zhao, Y., et al., XBP1 splicing triggers miR-150 transfer from smooth muscle cells to endothelial cells via extracellular vesicles. Sci Rep, 2016. 6: p. 28627. 128. Chen, J., et al., ER stress triggers MCP-1 expression through SET7/9-induced histone methylation in the kidneys of db/db mice. Am J Physiol Renal Physiol, 2014. 306(8): p. F916-25. 129. Ge, P., et al., Downregulation of microRNA-512-3p enhances the viability and suppresses the apoptosis of vascular endothelial cells, alleviates autophagy and endoplasmic reticulum stress as well as represses atherosclerotic lesions in atherosclerosis by adjusting spliced/unspliced ratio of X-box binding protein 1 (XBP-1S/XBP-1U). Bioengineered, 2021. 12(2): p. 12469-12481. 130. Liu, M., et al., Allele-specific imbalance of oxidative stress-induced growth inhibitor 1 associates with progression of hepatocellular carcinoma. Gastroenterology, 2014. 146(4): p. 1084-96. 131. Tsai, C.H., et al., Docosahexaenoic acid promotes the formation of autophagosomes in MCF-7 breast cancer cells through oxidative stress-induced growth inhibitor 1 mediated activation of AMPK/mTOR pathway. Food Chem Toxicol, 2021. 154: p. 112318. 132. Yuan, Q., et al., METTL3 regulates PM2.5-induced cell injury by targeting OSGIN1 in human airway epithelial cells. J Hazard Mater, 2021. 415: p. 125573. 133. Gao, M., et al., LncRNA UCA1 attenuates autophagy-dependent cell death through blocking autophagic flux under arsenic stress. Toxicol Lett, 2018. 284: p. 195-204. 134. Daiber, A., et al., New Therapeutic Implications of Endothelial Nitric Oxide Synthase (eNOS) Function/Dysfunction in Cardiovascular Disease. Int J Mol Sci, 2019. 20(1). 135. Lin, F., et al., Hydrogen Sulfide Protects Against High Glucose-Induced Human Umbilical Vein Endothelial Cell Injury Through Activating PI3K/Akt/eNOS Pathway. Drug Des Devel Ther, 2020. 14: p. 621-633. 136. Duan, M.X., et al., Andrographolide Protects against HG-Induced Inflammation, Apoptosis, Migration, and Impairment of Angiogenesis via PI3K/AKT-eNOS Signalling in HUVECs. Mediators Inflamm, 2019. 2019: p. 6168340. 137. Bharath, L.P., et al., Impairment of autophagy in endothelial cells prevents shear-stress-induced increases in nitric oxide bioavailability. Can J Physiol Pharmacol, 2014. 92(7): p. 605-12. 138. Guo, F., et al., Autophagy regulates vascular endothelial cell eNOS and ET-1 expression induced by laminar shear stress in an ex vivo perfused system. Ann Biomed Eng, 2014. 42(9): p. 1978-88. 139. Liu, D., et al., Autophagy contributes to angiotensin II induced dysfunction of HUVECs. Clin Exp Hypertens, 2021. 43(5): p. 462-473. 140. Shao, J., et al., Effect of eNOS on Ischemic Postconditioning-Induced Autophagy against Ischemia/Reperfusion Injury in Mice. Biomed Res Int, 2019. 2019: p. 5201014. 141. Ross, R., Atherosclerosis--an inflammatory disease. N Engl J Med, 1999. 340(2): p. 115-26. 142. Frostegard, J., Immunity, atherosclerosis and cardiovascular disease. BMC Med, 2013. 11: p. 117. 143. McKeage, K. and G.M. Keating, Fenofibrate: a review of its use in dyslipidaemia. Drugs, 2011. 71(14): p. 1917-46. 144. Luo, R., et al., Curcumin Alleviates Palmitic Acid-Induced LOX-1 Upregulation by Suppressing Endoplasmic Reticulum Stress in HUVECs. Biomed Res Int, 2021. 2021: p. 9983725. 145. Jasinski, M., L. Jasinska, and M. Ogrodowczyk, Resveratrol in prostate diseases - a short review. Cent European J Urol, 2013. 66(2): p. 144-9. 146. Czamara, K., et al., Lipid Droplets Formation Represents an Integral Component of Endothelial Inflammation Induced by LPS. Cells, 2021. 10(6). 147. Mukohda, M., et al., Streptococcal Exotoxin Streptolysin O Causes Vascular Endothelial Dysfunction Through PKCbeta Activation. J Pharmacol Exp Ther, 2021. 379(2): p. 117-124. 148. Savira, F., et al., The effect of dihydroceramide desaturase 1 inhibition on endothelial impairment induced by indoxyl sulfate. Vascul Pharmacol, 2021. 141: p. 106923. 149. Wang, Q., et al., Microcystin-leucine arginine blocks vasculogenesis and angiogenesis through impairing cytoskeleton and impeding endothelial cell migration by downregulating integrin-mediated Rho/ROCK signaling pathway. Environ Sci Pollut Res Int, 2021. 28(47): p. 67108-67119. 150. Qin, X., et al., Ferritinophagy is involved in the zinc oxide nanoparticles-induced ferroptosis of vascular endothelial cells. Autophagy, 2021. 17(12): p. 4266-4285. 151. Rajendran, P., et al., Anti-Apoptotic Effect of Flavokawain A on Ochratoxin-A-Induced Endothelial Cell Injury by Attenuation of Oxidative Stress via PI3K/AKT-Mediated Nrf2 Signaling Cascade. Toxins (Basel), 2021. 13(11). 152. Khoi, C.S., et al., Selective Activation of Endoplasmic Reticulum Stress by Reactive-Oxygen-Species-Mediated Ochratoxin A-Induced Apoptosis in Tubular Epithelial Cells. Int J Mol Sci, 2021. 22(20). 153. Nguyen, M.T., K.H. Min, and W. Lee, Palmitic Acid-Induced miR-429-3p Impairs Myoblast Differentiation by Downregulating CFL2. Int J Mol Sci, 2021. 22(20). 154. Tashiro, E., et al., Involvement of miR-3180-3p and miR-4632-5p in palmitic acid-induced insulin resistance. Mol Cell Endocrinol, 2021. 534: p. 111371. 155. Huang, F., et al., Palmitic Acid Induces MicroRNA-221 Expression to Decrease Glucose Uptake in HepG2 Cells via the PI3K/AKT/GLUT4 Pathway. Biomed Res Int, 2019. 2019: p. 8171989. 156. Zhao, X.H., et al., MicroRNA-326 suppresses iNOS expression and promotes autophagy of dopaminergic neurons through the JNK signaling by targeting XBP1 in a mouse model of Parkinson's disease. J Cell Biochem, 2019. 120(9): p. 14995-15006. 157. Liang, H., et al., Hypoxia induces miR-153 through the IRE1alpha-XBP1 pathway to fine tune the HIF1alpha/VEGFA axis in breast cancer angiogenesis. Oncogene, 2018. 37(15): p. 1961-1975. 158. Cinque, L., et al., MiT/TFE factors control ER-phagy via transcriptional regulation of FAM134B. EMBO J, 2020. 39(17): p. e105696. 159. Ferro-Novick, S., F. Reggiori, and J.L. Brodsky, ER-Phagy, ER Homeostasis, and ER Quality Control: Implications for Disease. Trends Biochem Sci, 2021. 46(8): p. 630-639. 160. Grandjean, J.M.D., et al., Pharmacologic IRE1/XBP1s activation confers targeted ER proteostasis reprogramming. Nat Chem Biol, 2020. 16(10): p. 1052-1061. 161. Madhavan, A., et al., Pharmacologic IRE1/XBP1s activation promotes systemic adaptive remodeling in obesity. Nat Commun, 2022. 13(1): p. 608. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/85097 | - |
dc.description.abstract | 飽和脂肪酸 (saturated fatty acids) 與代謝症候群密切相關,也是心血管疾病 (cardiovascular disease, CVD) 的危險因子,其誘導的血管脂毒性在內質網壓力 (ER stress)下的機制尚不清楚。因此,在此研究中,我們探討剪接型 X盒 結合蛋白 1 (XBP1s) 的標的基因:氧化壓力誘導生長抑制因子 1 (oxidative stress induced growth inhibitor 1, OSGIN1) 在棕櫚酸(palmitic acid, PA) 誘導的血管功能障礙中所扮演的角色。 首先,PA會抑制人臍靜脈內皮細胞 (HUVEC) 的血管形成。同時,PA 誘導了 XBP1s 在HUVECs 中的表現。通過基因減量技術抑制 XBP1s (silencing XBP1s)可以減弱 XBP1s 的表現,同時也延緩細胞遷移(cell migration),並且減少內皮一氧化氮合成酶 (eNOS) 的表現。 在PA 的處理下,我們透過核醣核酸測序分析(RNA sequencing analysis)發現OSGIN1 可能是XBP1s 的標的基因。 接下來藉由基因減量技術抑制OSGIN1(silencing of OSGIN1)發現其可以透過降低磷酸化 eNOS (p-eNOS)來抑制細胞的遷移。 此外,PA 也會活化血管內皮細胞的自噬作用(autophagy); 我們透過使用 3-甲基腺嘌呤 (3-MA) 去証實3-MA可以抑制PA誘發的自噬作用並減少血管內皮細胞的遷移。另外,實驗結果發現,基因減量技術抑制 XBP1s 和 OSGIN1 會減少 LC3 II 的誘導;因此推論OSGIN1 可以維持自噬作用以保護血管內皮細胞的遷移作用。結論為,PA 會誘導血管內皮細胞的內質網壓力並活化 IRE1α-XBP1s途徑。 OSGIN1 是 XBP1s 的標的基因,其可通過調節自噬作用來保護內皮細胞以免受血管脂毒性的傷害。 | zh_TW |
dc.description.abstract | Saturated fatty acids (SFAs) are closely associated with metabolic syndrome and risk factors for cardiovascular disease (CVD), and the mechanism by which they induce vascular lipotoxicity under endoplasmic reticulum stress (ER stress) is unclear. Therefore, in the present study, we investigated the role of target genes of splicing X-box-binding proteins 1 (XBP1s): oxidative stress-induced growth inhibitor 1 (OSGIN1) in the induction of palmitic acid (PA) in vascular dysfunction . First, PA inhibits angiogenesis in human umbilical vein endothelial cells (HUVEC). Meanwhile, PA induced the expression of XBP1s in HUVECs. By silencing XBP1s, the expression of XBP1s can be attenuated, and it can also delay cell migration and reduce the expression of endothelial nitric oxide synthase (eNOS). Under PA treatment, we identified OSGIN1 as a possible target gene of XBP1s through RNA-sequencing analysis. Next, by silencing OSGIN1, it was found to inhibit cell migration by reducing phosphorylated eNOS (p-eNOS). In addition, PA can also activate autophagy in vascular endothelial cells; we used 3-methyladenine (3-MA) to demonstrate that 3-MA inhibits PA-induced autophagy and reduces vascular endothelial cell migration. Furthermore, the experimental results found that silencing XBP1s and OSGIN1 reduced the induction of LC3 II; therefore, it was speculated that OSGIN1 could maintain autophagy to protect vascular endothelial cell migration. In conclusion, PA induces endoplasmic reticulum stress and activates the IRE1α-XBP1s pathway in vascular endothelial cells. OSGIN1, a target gene of XBP1s, protects endothelial cells from vascular lipotoxicity by regulating autophagy. | en |
dc.description.provenance | Made available in DSpace on 2023-03-19T22:43:27Z (GMT). No. of bitstreams: 1 U0001-0908202222101400.pdf: 19409049 bytes, checksum: d950734f2affff515e32331cdf981376 (MD5) Previous issue date: 2022 | en |
dc.description.tableofcontents | 口試委員審定書 .......................................................................................................................... 2 誌謝 ................................................................................................................................................ 3 中文摘要 ......................................................................................................................................... 4 ABSTRACT ........................................................................................................................................ 6 LIST OF ABBREVIATIONS ................................................................................................................... 8 CONTENTS ...................................................................................................................................... 11 PART I: INTRODUCTION ................................................................................................................... 15 1.1 LIPOTOXICITY .............................................................................................................................. 15 1.2 FREE FATTY ACID AND PALMITIC ACID ....................................................................................... 16 1.3 UPTAKE OF FATTY ACID AND METABOLISM IN ENDOTHELIAL CELL ......................................... 19 1.4 ENDOTHELIAL DYSFUNCTION .................................................................................................... 20 1.5 PA AND APOPTOSIS/NECROPTOSIS/PYROPTOSIS ..................................................................... 20 1.6 PA AND INFLAMMATION ..............................................................................................................22 1.7 PA AND ER STRESS ..................................................................................................................... 25 1.8 PA AND AUTOPHAGY .................................................................................................................. 27 1.9 PA AND ROS ............................................................................................................................... 30 1.10 PA AND MITOCHONDRIAL DYSFUNCTION ................................................................................ 31 1.11 PA AND INSULIN RESISTANCE ................................................................................................... 33 1.12 PA AND LONG NONCODING RNA/MIRNA .................................................................................. 34 1.13 XBP1S AND VASCULAR ENDOTHELIAL CELLS .......................................................................... 34 1.14 OSGIN1 ...................................................................................................................................... 36 PART II: AIMS .................................................................................................................................. 37 PART III: MATERIALS AND METHODS ............................................................................................... 38 3.1 CELL CULTURE ............................................................................................................................ 38 3.2 BOVINE SERUM ALBUMIN (BSA)-CONJUGATED PALMITATE PREPARATION ............................. 38 3.3 MTS ASSAY .................................................................................................................................. 39 3.4 OIL RED O STAINING .................................................................................................................... 39 3.5 WOUND HEALING MIGRATION ASSAY ......................................................................................... 39 3.6 TUBE FORMATION ASSAY ............................................................................................................ 40 3.7 SMALL INTERFERING RNA (SIRNA) TRANSFECTION ................................................................... 40 3.8 QUANTITATIVE REAL-TIME POLYMERASE CHAIN REACTION (QRT-PCR) ................................... 40 3.9 WESTERN BLOTTING ANALYSIS ................................................................................................. 42 3.10 IMMUNOHISTOCHEMISTRY (IHC) STAINING ............................................................................ 43 3.11 INTRACELLULAR REACTIVE OXYGEN SPECIES (ROS) ASSAY .................................................... 43 3.12 STATISTICAL ANALYSIS ............................................................................................................. 43 PART IV: RESULTS ............................................................................................................................ 45 4.1 PA ACTIVATES ER STRESS-RELATED UPR SIGNALING IN ENDOTHELIAL CELLS ........................ 45 4.2 ENDOTHELIAL DYSFUNCTION DUE TO PA TREATMENT ............................................................. 46 4.3 PA EXPOSURE ACTIVATE IRE1Α–XBP1S AXIS TO REDUCE ENDOTHELIAL DYSFUNCTION.......... 46 4.4 XBP1S PROTECTS ENDOTHELIAL CELLS FROM LIPOTOXICITY VIA AUTOPHAGY ..................... 47 4.5 XBP1S REGULATED OSGIN1 AGAINST ENDOTHELIAL DYSFUNCTION VIA AUTOPHAGY ........... 48 4.6 OSGIN1 IS INVOLVED IN THE ATHEROSCLEROSIS PROCESS .................................................... 50 PART V: DISCUSSION ....................................................................................................................... 51 PART VI: CONCLUSION .................................................................................................................... 60 PART VII: FUTURE PERSPECTIVE ...................................................................................................... 61 7.1 REGULATION OF XBP1S ON PROMOTER REPORTER OF OSGIN1 ................................................ 61 7.2 WHETHER XBP1S REGULATED MIRNA AFFECT ANGIOGENESIS OF ENDOTHELIAL CELL AFTER PA TREATMENT ....... 61 7.3 WHETHER PA COULD REGULATE ER-PHAGY ACTIVITY DURING VASCULAR LIPOTOXICITY ...... 61 7.4 WHETHER IXA4 SELECTIVELY INDUCES ADAPTIVE IRE1/XBP1S SIGNALING IN ENDOTHELIAL CELL ..................... 62 PART VIII: PUBLISHED LIST ............................................................................................................... 63 PART IX: REFERRENCES: ................................................................................................................... 65 PART IX: FIGURES ............................................................................................................................ 89 FIGURE 1 .......................................................................................................................................... 89 FIGURE 2 .......................................................................................................................................... 91 FIGURE 3 .......................................................................................................................................... 93 FIGURE 4 .......................................................................................................................................... 96 FIGURE 5 .......................................................................................................................................... 99 FIGURE 6 ......................................................................................................................................... 104 FIGURE 7 ......................................................................................................................................... 106 SUPPLEMENTARY DATA .................................................................................................................. 107 | |
dc.language.iso | en | |
dc.title | X盒結合蛋白1標的氧化壓力誘導生長抑制因子1藉由維持自噬作用以保護棕櫚酸誘發的血管脂毒性 | zh_TW |
dc.title | Oxidative Stress-Induced Growth Inhibitor 1, a Target of X-Box-Binding Protein 1, Protects Palmitic Acid-Induced Vascular Lipotoxicity through Maintaining Autophagy | en |
dc.type | Thesis | |
dc.date.schoolyear | 110-2 | |
dc.description.degree | 博士 | |
dc.contributor.oralexamcommittee | 劉興華(Shing-Hwa Liu),林子玉(Tzu-Yu Lin),洪冠予(Kuan-Yu Hung),陳文彬(Wen-Pin Chen) | |
dc.subject.keyword | 棕櫚酸,氧化壓力誘導生長抑制因子 1,未摺疊蛋白反應,剪接型 X-盒結合蛋白 1,自噬作用,內皮一氧化氮合成酶,血管內皮細胞, | zh_TW |
dc.subject.keyword | palmitic acid,OSGIN1,unfolded protein response,XBP1s,autophagy,eNOS,endothelial cells, | en |
dc.relation.page | 107 | |
dc.identifier.doi | 10.6342/NTU202202226 | |
dc.rights.note | 同意授權(限校園內公開) | |
dc.date.accepted | 2022-08-12 | |
dc.contributor.author-college | 醫學院 | zh_TW |
dc.contributor.author-dept | 毒理學研究所 | zh_TW |
dc.date.embargo-lift | 2022-10-03 | - |
顯示於系所單位: | 毒理學研究所 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
U0001-0908202222101400.pdf 授權僅限NTU校內IP使用(校園外請利用VPN校外連線服務) | 18.95 MB | Adobe PDF | 檢視/開啟 |
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。