[1] |
Schlapbach LJ, Kissoon N, Alhawsawi A, et al. World Sepsis Day: a global agenda to target a leading cause of morbidity and mortality. Am J Physiol Lung Cell Mol Physiol, 2020; 319, L518−22. doi: 10.1152/ajplung.00369.2020 |
[2] |
Balayan S, Chauhan N, Chandra R, et al. Recent advances in developing biosensing based platforms for neonatal sepsis. Biosens Bioelectron, 2020; 169, 112552. doi: 10.1016/j.bios.2020.112552 |
[3] |
McNamara JF, Harris PNA, Chatfield MD, et al. Long term sepsis readmission, mortality and cause of death following Gram negative bloodstream infection: a propensity matched observational linkage study. Int J Infect Dis, 2022; 114, 34−44. doi: 10.1016/j.ijid.2021.10.047 |
[4] |
Chousalkar K, Gast R, Martelli F, et al. Review of egg-related salmonellosis and reduction strategies in United States, Australia, United Kingdom and New Zealand. Crit Rev Microbiol, 2018; 44, 290−303. doi: 10.1080/1040841X.2017.1368998 |
[5] |
Chroni A, Rallidis L, Vassou D, et al. Identification and characterization of a rare variant in apolipoprotein A-IV, p. (V336M), and evaluation of HDL functionality in a Greek cohort with extreme HDL cholesterol levels. Arch Biochem Biophys, 2020; 696, 108655. doi: 10.1016/j.abb.2020.108655 |
[6] |
Akkoyun DÇ, Akyuz A, Doğan M, et al. Quercetin inhibits heart injury in lipopolysaccharide-induced endotoxemic model by suppressing the effects of reactive oxygen species. Anal Quant Cytopathol Histopathol, 2016; 38, 183−8. |
[7] |
Wei XQ, Meng XL, Yuan YX, et al. Quercetin exerts cardiovascular protective effects in LPS-induced dysfunction in vivo by regulating inflammatory cytokine expression, NF-κB phosphorylation, and caspase activity. Mol Cell Biochem, 2018; 446, 43−52. doi: 10.1007/s11010-018-3271-6 |
[8] |
Liu G, Wu KJ, Zhang L, et al. Metformin attenuated endotoxin-induced acute myocarditis via activating AMPK. Int Immunopharmacol, 2017; 47, 166−72. doi: 10.1016/j.intimp.2017.04.002 |
[9] |
Panaro MA, Acquafredda A, Cavallo P, et al. Inflammatory responses in embryonal cardiomyocytes exposed to LPS challenge: an in vitro model of deciphering the effects of LPS on the heart. Curr Pharm Des, 2010; 16, 754−65. doi: 10.2174/138161210790883516 |
[10] |
Shen L, Weber CR, Turner JR. The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state. J Cell Biol, 2008; 181, 683−95. doi: 10.1083/jcb.200711165 |
[11] |
Mokhtari B, Badalzadeh R. The potentials of distinct functions of autophagy to be targeted for attenuation of myocardial ischemia/reperfusion injury in preclinical studies: an up-to-date review. J Physiol Biochem, 2021; 77, 377−404. doi: 10.1007/s13105-021-00824-x |
[12] |
Larsen KE, Sulzer D. Autophagy in neurons: a review. Histol Histopathol, 2002; 17, 897−908. |
[13] |
Zhang C, Syed TW, Liu RJ, et al. Role of endoplasmic reticulum stress, autophagy, and inflammation in cardiovascular disease. Front Cardiovasc Med, 2017; 4, 29. doi: 10.3389/fcvm.2017.00029 |
[14] |
Mechesso AF, Quah YX, Park SC. Ginsenoside Rg3 reduces the adhesion, invasion, and intracellular survival of Salmonella enterica serovar Typhimurium. J Ginseng Res, 2021; 45, 75−85. doi: 10.1016/j.jgr.2019.09.002 |
[15] |
Chiu B, Jantuan E, Shen F, et al. Autophagy-inflammasome interplay in heart failure: a systematic review on basics, pathways, and therapeutic perspectives. Ann Clin Lab Sci, 2017; 47, 243−52. |
[16] |
Ashrafizadeh M, Tavakol S, Ahmadi Z, et al. Therapeutic effects of kaempferol affecting autophagy and endoplasmic reticulum stress. Phytother Res, 2020; 34, 911−23. doi: 10.1002/ptr.6577 |
[17] |
Mohammadinejad R, Ahmadi Z, Tavakol S, et al. Berberine as a potential autophagy modulator. J Cell Physiol, 2019; 234, 14914−26. doi: 10.1002/jcp.28325 |
[18] |
Nagata S, Nakano H. Apoptotic and non-apoptotic cell death. Springer. 2017. |
[19] |
Mughal W, Dhingra R, Kirshenbaum LA. Striking a balance: autophagy, apoptosis, and necrosis in a normal and failing heart. Curr Hypertens Rep, 2012; 14, 540−7. doi: 10.1007/s11906-012-0304-5 |
[20] |
Cong L, Bai YP, Guo ZG. The crosstalk among autophagy, apoptosis, and pyroptosis in cardiovascular disease. Front Cardiovasc Med, 2022; 9, 997469. doi: 10.3389/fcvm.2022.997469 |
[21] |
Dong Y, Chen HW, Gao JL, et al. Molecular machinery and interplay of apoptosis and autophagy in coronary heart disease. J Mol Cell Cardiol, 2019; 136, 27−41. doi: 10.1016/j.yjmcc.2019.09.001 |
[22] |
Zheng XT, Chen WW, Gong FC, et al. The role and mechanism of pyroptosis and potential therapeutic targets in sepsis: a review. Front Immunol, 2021; 12, 711939. doi: 10.3389/fimmu.2021.711939 |
[23] |
Wei SQ, Feng M, Zhang SD. Molecular characteristics of cell pyroptosis and its inhibitors: a review of activation, regulation, and inhibitors. Int J Mol Sci, 2022; 23, 16115. doi: 10.3390/ijms232416115 |
[24] |
Jia Y, Li DZ, Yu J, et al. Potential diabetic cardiomyopathy therapies targeting pyroptosis: a mini review. Front Cardiovasc Med, 2022; 9, 985020. doi: 10.3389/fcvm.2022.985020 |
[25] |
Zhang P, Zang MR, Sang ZZ, et al. Vitamin C alleviates LPS-induced myocardial injury by inhibiting pyroptosis via the ROS-AKT/mTOR signalling pathway. BMC Cardiovasc Disord, 2022; 22, 561. doi: 10.1186/s12872-022-03014-9 |
[26] |
Li Q, Zhang MM, Zhao Y, et al. Irisin protects against LPS-stressed cardiac damage through inhibiting inflammation, apoptosis, and pyroptosis. SHOCK, 2021; 56, 1009−18. doi: 10.1097/SHK.0000000000001775 |
[27] |
Ouyang CH, You JY, Xie ZL. The interplay between autophagy and apoptosis in the diabetic heart. J Mol Cell Cardiol, 2014; 71, 71−80. doi: 10.1016/j.yjmcc.2013.10.014 |
[28] |
Yu JH, Hu GL, Cao HB, et al. Quercetin ameliorates lipopolysaccharide-induced duodenal inflammation through modulating autophagy, programmed cell death and intestinal mucosal barrier function in chicken embryos. Animals, 2022; 12, 3524. doi: 10.3390/ani12243524 |
[29] |
Afrin S, Gasparrini M, Forbes-Hernandez TY, et al. Protective effects of Manuka honey on LPS-treated RAW 264.7 macrophages. Part 1: Enhancement of cellular viability, regulation of cellular apoptosis and improvement of mitochondrial functionality. Food Chem Toxicol, 2018; 121, 203−13. doi: 10.1016/j.fct.2018.09.001 |
[30] |
Häkkinen SH, Kärenlampi SO, Heinonen IM, et al. Content of the flavonols quercetin, myricetin, and kaempferol in 25 edible berries. J Agric Food Chem, 1999; 47, 2274−9. doi: 10.1021/jf9811065 |
[31] |
Gasparrini M, Afrin S, Forbes-Hernández TY, et al. Protective effects of Manuka honey on LPS-treated RAW 264.7 macrophages. Part 2: Control of oxidative stress induced damage, increase of antioxidant enzyme activities and attenuation of inflammation. Food Chem Toxicol, 2018; 120, 578−87. doi: 10.1016/j.fct.2018.08.001 |
[32] |
Gasparrini M, Forbes-Hernandez TY, Giampieri F, et al. Anti-inflammatory effect of strawberry extract against LPS-induced stress in RAW 264.7 macrophages. Food Chem Toxicol, 2017; 102, 1−10. doi: 10.1016/j.fct.2017.01.018 |
[33] |
Ulusoy HG, Sanlier N. A minireview of quercetin: from its metabolism to possible mechanisms of its biological activities. Crit Rev Food Sci Nutr, 2020; 60, 3290−303. doi: 10.1080/10408398.2019.1683810 |
[34] |
Lotfi N, Yousefi Z, Golabi M, et al. The potential anti-cancer effects of quercetin on blood, prostate and lung cancers: an update. Front Immunol, 2023; 14, 1077531. doi: 10.3389/fimmu.2023.1077531 |
[35] |
Paskeh MDA, Entezari M, Clark C, et al. Targeted regulation of autophagy using nanoparticles: new insight into cancer therapy. Biochim Biophys Acta Mol Basis Dis, 2022; 1868, 166326. doi: 10.1016/j.bbadis.2021.166326 |
[36] |
Ashrafizadeh M, Paskeh MDA, Mirzaei S, et al. Targeting autophagy in prostate cancer: preclinical and clinical evidence for therapeutic response. J Exp Clin Cancer Res, 2022; 41, 105. doi: 10.1186/s13046-022-02293-6 |
[37] |
Liu J, Wang SC, Zhang QJ, et al. Selenomethionine alleviates LPS-induced chicken myocardial inflammation by regulating the miR-128-3p-p38 MAPK axis and oxidative stress. Metallomics, 2020; 12, 54−64. doi: 10.1039/c9mt00216b |
[38] |
Frantz S, Kobzik L, Kim YD, et al. Toll4 (TLR4) expression in cardiac myocytes in normal and failing myocardium. J Clin Invest, 1999; 104, 271−80. doi: 10.1172/JCI6709 |
[39] |
Zanoni I, Bodio C, Broggi A, et al. Similarities and differences of innate immune responses elicited by smooth and rough LPS. Immunol Lett, 2012; 142, 41−7. doi: 10.1016/j.imlet.2011.12.002 |
[40] |
Kogut M, He HQ, Kaiser P. Lipopolysaccharide binding protein/CD14/TLR4-dependent recognition of salmonella LPS induces the functional activation of chicken heterophils and up-regulation of pro-inflammatory cytokine and chemokine gene expression in these cells. Anim Biotechnol, 2005; 16, 165−81. doi: 10.1080/10495390500264896 |
[41] |
Panaro MA, Cianciulli A, Gagliardi N, et al. CD14 major role during lipopolysaccharide-induced inflammation in chick embryo cardiomyocytes. FEMS Immunol Med Microbiol, 2008; 53, 35−45. doi: 10.1111/j.1574-695X.2008.00397.x |
[42] |
Rossetti C, Peri F. The role of toll-like receptor 4 in infectious and non Infectious Inflammation. Springer. 2021. |
[43] |
De Vicente LG, Muñoz VR, Pinto AP, et al. TLR4 deletion increases basal energy expenditure and attenuates heart apoptosis and ER stress but mitigates the training-induced cardiac function and performance improvement. Life Sci, 2021; 285, 119988. doi: 10.1016/j.lfs.2021.119988 |
[44] |
Karnati HK, Pasupuleti SR, Kandi R, et al. TLR-4 signalling pathway: MyD88 independent pathway up-regulation in chicken breeds upon LPS treatment. Vet Res Commun, 2015; 39, 73−8. doi: 10.1007/s11259-014-9621-2 |
[45] |
Wang XP, Guo DQ, Li WL, et al. Danshen (Salvia miltiorrhiza) restricts MD2/TLR4-MyD88 complex formation and signalling in acute myocardial infarction-induced heart failure. J Cell Mol Med, 2020; 24, 10677−92. doi: 10.1111/jcmm.15688 |
[46] |
Zhang LL, Zhang C, Peng JP. Application of nanopore sequencing technology in the clinical diagnosis of infectious diseases. Biomed Environ Sci, 2022; 35, 381−92. |
[47] |
Kogut MH, Rothwell L, Kaiser P. Priming by recombinant chicken interleukin-2 induces selective expression of IL-8 and IL-18 mRNA in chicken heterophils during receptor-mediated phagocytosis of opsonized and nonopsonized Salmonella enterica serovar enteritidis. Mol Immunol, 2003; 40, 603−10. doi: 10.1016/j.molimm.2003.08.002 |
[48] |
Akseh S, Nemati M, Zamani-Gharehchamani E, et al. Amnion membrane proteins attenuate LPS-induced inflammation and apoptosis by inhibiting TLR4/NF-κB pathway and repressing MicroRNA-155 in rat H9c2 cells. Immunopharmacol Immunotoxicol, 2021; 43, 487−94. doi: 10.1080/08923973.2021.1945086 |
[49] |
Handley SA, Miller VL. General and specific host responses to bacterial infection in Peyer's patches: a role for stromelysin-1 (matrix metalloproteinase-3) during Salmonella enterica infection. Mol Microbiol, 2007; 64, 94−110. doi: 10.1111/j.1365-2958.2007.05635.x |
[50] |
Lalu MM, Csont T, Schulz R. Matrix metalloproteinase activities are altered in the heart and plasma during endotoxemia. Crit Care Med, 2004; 32, 1332−7. doi: 10.1097/01.CCM.0000127778.16609.EC |
[51] |
Iriti M, Kubina R, Cochis A, et al. Rutin, a quercetin glycoside, restores chemosensitivity in human breast cancer cells. Phytother Res, 2017; 31, 1529−38. doi: 10.1002/ptr.5878 |
[52] |
Liu XC, Zheng L, Liu M, et al. Protective effects of rutin on lipopolysaccharide-induced heart injury in mice. J Toxicol Sci, 2018; 43, 329−37. doi: 10.2131/jts.43.329 |
[53] |
Shu J, Gu YW, Jin L, et al. Matrix metalloproteinase 3 regulates angiotensin II-induced myocardial fibrosis cell viability, migration and apoptosis. Mol Med Rep, 2021; 23, 151. |
[54] |
Collins MM, Ryan AK. Manipulating claudin expression in avian embryos. Methods Mol Biol, 2011; 762, 195−212. |
[55] |
Simard A, Di Pietro E, Ryan AK. Gene expression pattern of Claudin-1 during chick embryogenesis. Gene Expr Patterns, 2005; 5, 553−60. doi: 10.1016/j.modgep.2004.10.009 |
[56] |
Simard A, Di Pietro E, Young CR, et al. Alterations in heart looping induced by overexpression of the tight junction protein Claudin-1 are dependent on its C-terminal cytoplasmic tail. Mech Dev, 2006; 123, 210−27. doi: 10.1016/j.mod.2005.12.004 |
[57] |
Kostin S. Zonula occludens-1 and connexin 43 expression in the failing human heart. J Cell Mol Med, 2007; 11, 892−5. doi: 10.1111/j.1582-4934.2007.00063.x |
[58] |
El Refaey M, Coles S, Musa H, et al. Altered expression of zonula occludens-1 affects cardiac Na+ channels and increases susceptibility to ventricular arrhythmias. Cells, 2022; 11, 665. doi: 10.3390/cells11040665 |
[59] |
Zhang JL, Vincent KP, Peter AK, et al. Cardiomyocyte expression of ZO-1 is essential for normal atrioventricular conduction but does not alter ventricular function. Circ Res, 2020; 127, 284−97. doi: 10.1161/CIRCRESAHA.119.315539 |
[60] |
Chen Y, Liu YQ, Dorn II GW. Mitochondrial fusion is essential for organelle function and cardiac homeostasis. Circ Res, 2011; 109, 1327−31. doi: 10.1161/CIRCRESAHA.111.258723 |
[61] |
Yu WC, Mei X, Zhang Q, et al. Yap overexpression attenuates septic cardiomyopathy by inhibiting DRP1-related mitochondrial fission and activating the ERK signaling pathway. J Recept Signal Transduct, 2019; 39, 175−86. doi: 10.1080/10799893.2019.1641822 |
[62] |
Bullon P, Cordero MD, Quiles JL, et al. Mitochondrial dysfunction promoted by Porphyromonas gingivalis lipopolysaccharide as a possible link between cardiovascular disease and periodontitis. Free Radic Biol Med, 2011; 50, 1336−43. doi: 10.1016/j.freeradbiomed.2011.02.018 |
[63] |
Xu T, Dong Q, Luo YX, et al. Porphyromonas gingivalis infection promotes mitochondrial dysfunction through Drp1-dependent mitochondrial fission in endothelial cells. Int J Oral Sci, 2021; 13, 28. doi: 10.1038/s41368-021-00134-4 |
[64] |
Tong MM, Zablocki D, Sadoshima J. The role of Drp1 in mitophagy and cell death in the heart. J Mol Cell Cardiol, 2020; 142, 138−45. doi: 10.1016/j.yjmcc.2020.04.015 |
[65] |
Zhao QC, Yan S, Lu J, et al. Drp1 regulates transcription of ribosomal protein genes in embryonic hearts. J Cell Sci, 2022; 135, jcs258956. doi: 10.1242/jcs.258956 |
[66] |
Sharp WW, Fang YH, Han M, et al. Dynamin-related protein 1 (Drp1)-mediated diastolic dysfunction in myocardial ischemia-reperfusion injury: therapeutic benefits of Drp1 inhibition to reduce mitochondrial fission. FASEB J, 2014; 28, 316−26. doi: 10.1096/fj.12-226225 |
[67] |
Ikeda Y, Shirakabe A, Maejima Y, et al. Endogenous Drp1 mediates mitochondrial autophagy and protects the heart against energy stress. Circ Res, 2015; 116, 264−78. doi: 10.1161/CIRCRESAHA.116.303356 |
[68] |
Ren J, Sowers JR, Zhang YM. Autophagy and cardiometabolic diseases. Academic Press. 2018. |
[69] |
Chang X, He YH, Wang L, et al. Puerarin alleviates LPS-induced H9C2 cell injury by inducing mitochondrial autophagy. J Cardiovasc Pharmacol, 2022; 80, 600−8. |
[70] |
Ben-Shaul V, Lomnitski L, Nyska A, et al. The effect of natural antioxidants, NAO and apocynin, on oxidative stress in the rat heart following LPS challenge. Toxicol Lett, 2001; 123, 1−10. |
[71] |
Sul OJ, Ra SW. Quercetin prevents LPS-induced oxidative stress and inflammation by modulating NOX2/ROS/NF-kB in lung epithelial cells. Molecules, 2021; 26, 6949. doi: 10.3390/molecules26226949 |
[72] |
Lushnikova EL, Nepomnyashchikh LM, Pichigin VI, et al. Expression of mRNA of apolipoprotein E, apolipoprotein A-IV, and matricellular proteins in the myocardium and intensity of fibroplastic processes during experimental hypercholesterolemia. Bull Exp Biol Med, 2013; 156, 271−5. doi: 10.1007/s10517-013-2328-5 |
[73] |
Zhang WQ, Liu XH, Zhou JT, et al. Apolipoprotein A-IV restrains fat accumulation in skeletal and myocardial muscles by inhibiting lipogenesis and activating PI3K-AKT signalling. Arch Physiol Biochem, 2023, 1-11. |
[74] |
Wang Y, Zhang ZZ, Wu Y, et al. Quercetin postconditioning attenuates myocardial ischemia/reperfusion injury in rats through the PI3K/Akt pathway. Braz J Med Biol Res, 2013; 46, 861−7. doi: 10.1590/1414-431X20133036 |
[75] |
Ravindranath TM, Goto M, Bakr S, et al. LPS-induced changes in myocardial markers in neonatal rats. Biol Neonate, 2003; 84, 319−24. doi: 10.1159/000073641 |
[76] |
Lado-Abeal J, Martinez-Sánchez N, Cocho JA, et al. Lipopolysaccharide (LPS)-induced septic shock causes profound changes in myocardial energy metabolites in pigs. Metabolomics, 2018; 14, 131. doi: 10.1007/s11306-018-1433-x |
[77] |
Yamaguchi O. Autophagy in the Heart. Circ J, 2019; 83, 697−704. doi: 10.1253/circj.CJ-18-1065 |
[78] |
Drosatos K, Pollak NM, Pol CJ, et al. Cardiac myocyte KLF5 regulates Ppara expression and cardiac function. Circ Res, 2016; 118, 241−53. doi: 10.1161/CIRCRESAHA.115.306383 |
[79] |
Kumari R, Ray AG, Mukherjee D, et al. Downregulation of PTEN promotes autophagy via concurrent reduction in apoptosis in cardiac hypertrophy in PPAR α-/- mice. Front Cardiovasc Med, 2022; 9, 798639. doi: 10.3389/fcvm.2022.798639 |
[80] |
Saikia R, Joseph J. AMPK: a key regulator of energy stress and calcium-induced autophagy. J Mol Med, 2021; 99, 1539−51. doi: 10.1007/s00109-021-02125-8 |
[81] |
Eisenberg-Lerner A, Bialik S, Simon HU, et al. Life and death partners: apoptosis, autophagy and the cross-talk between them. Cell Death Differ, 2009; 16, 966−75. doi: 10.1038/cdd.2009.33 |
[82] |
Kajstura J, Mansukhani M, Cheng W, et al. Programmed cell death and expression of the protooncogene bcl-2 in myocytes during postnatal maturation of the heart. Exp Cell Res, 1995; 219, 110−21. doi: 10.1006/excr.1995.1211 |
[83] |
Grzegorzewska AK, Hrabia A, Paczoska-Eliasiewicz HE. Localization of apoptotic and proliferating cells and mRNA expression of caspases and Bcl-2 in gonads of chicken embryos. Acta Histochem, 2014; 116, 795−802. doi: 10.1016/j.acthis.2014.01.012 |
[84] |
Sun YX, Cai Y, Qian SH, et al. Beclin-1 improves mitochondria-associated membranes in the heart during endotoxemia. FASEB Bioadv, 2021; 3, 123−35. doi: 10.1096/fba.2020-00039 |
[85] |
Sun YX, Yao X, Zhang QJ, et al. Beclin-1-dependent autophagy protects the heart during sepsis. Circulation, 2018; 138, 2247−62. doi: 10.1161/CIRCULATIONAHA.117.032821 |
[86] |
Maejima Y, Isobe M, Sadoshima J. Regulation of autophagy by Beclin 1 in the heart. J Mol Cell Cardiol, 2016; 95, 19−25. doi: 10.1016/j.yjmcc.2015.10.032 |
[87] |
Haq S, Grondin J, Banskota S, et al. Autophagy: roles in intestinal mucosal homeostasis and inflammation. J Biomed Sci, 2019; 26, 19. doi: 10.1186/s12929-019-0512-2 |
[88] |
Liao ZH, Dai ZK, Cai CY, et al. Knockout of Atg5 inhibits proliferation and promotes apoptosis of DF-1 cells. In Vitro Cell Dev Biol Anim, 2019; 55, 341−8. doi: 10.1007/s11626-019-00342-7 |
[89] |
Zhu CM, Zhang SY, Liu D, et al. A novel gene prognostic signature based on differential DNA methylation in breast cancer. Front Genet, 2021; 12, 742578. doi: 10.3389/fgene.2021.742578 |
[90] |
Liu L, Chen ML, Lin K, et al. Inhibiting caspase-12 mediated inflammasome activation protects against oxygen-glucose deprivation injury in primary astrocytes. Int J Med Sci, 2020; 17, 1936−45. doi: 10.7150/ijms.44330 |
[91] |
Nakagawa T, Zhu H, Morishima N, et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β. Nature, 2000; 403, 98−103. doi: 10.1038/47513 |
[92] |
Morishima N, Nakanishi K, Takenouchi H, et al. An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12. J Biol Chem, 2002; 277, 34287−94. doi: 10.1074/jbc.M204973200 |
[93] |
Salvamoser R, Brinkmann K, O'Reilly LA, et al. Characterisation of mice lacking the inflammatory caspases-1/11/12 reveals no contribution of caspase-12 to cell death and sepsis. Cell Death Differ, 2019; 26, 1124−37. doi: 10.1038/s41418-018-0188-2 |
[94] |
Liu HH, Wang SJ, Gong LJ, et al. SIRT6 ameliorates LPS-induced apoptosis and tight junction injury in ARDS through the ERK1/2 pathway and autophagy. Int J Med Sci, 2023; 20, 581−94. doi: 10.7150/ijms.80920 |
[95] |
Wang JY, Luan YY, Fan EK, et al. TBK1/IKKε negatively regulate lps-induced neutrophil necroptosis and lung inflammation. SHOCK, 2021; 55, 338−48. doi: 10.1097/SHK.0000000000001632 |
[96] |
Liu YL, Hsu CC, Huang HJ, et al. Gallic acid attenuated LPS-induced neuroinflammation: protein aggregation and necroptosis. Mol Neurobiol, 2020; 57, 96−104. doi: 10.1007/s12035-019-01759-7 |
[97] |
Wang YC, Jiang L, Li YF, et al. Excessive selenium supplementation induced oxidative stress and endoplasmic reticulum stress in chicken spleen. Biol Trace Elem Res, 2016; 172, 481−7. doi: 10.1007/s12011-015-0596-9 |