HSP70 Ameliorates Septic Acute Kidney Injury via Binding with TRAF6 to Inhibit of Inflammation-Mediated Apoptosis

References

• Peerapornratana S, Manrique-Caballero CL, Gomez H, Kellum JA. Acute kidney injury from sepsis: current concepts, epidemiology, pathophysiology, prevention and treatment. Kidney Int. 2019;96(5):1083–1099. doi:10.1016/j.kint.2019.05.026
   PubMed Web of Science ®Google Scholar
• Gando S, Shiraishi A, Yamakawa K, et al. Role of disseminated intravascular coagulation in severe sepsis. Thromb Res. 2019;178:182–188. doi:10.1016/j.thromres.2019.04.025
   PubMed Web of Science ®Google Scholar
• Skube SJ, Katz SA, Chipman JG, Tignanelli CJ. Acute Kidney Injury and Sepsis. Surg Infect (Larchmt). 2018;19(2):216–224. doi:10.1089/sur.2017.261
   PubMed Web of Science ®Google Scholar
• Dellepiane S, Marengo M, Cantaluppi V. Detrimental cross-talk between sepsis and acute kidney injury: new pathogenic mechanisms, early biomarkers and targeted therapies. Crit Care. 2016;20:20. doi:10.1186/s13054-016-1198-4
   PubMed Web of Science ®Google Scholar
• Zhou Y, Xu W, Zhu H. CXCL8(3-72) K11R/G31P protects against sepsis-induced acute kidney injury via NF-kappaB and JAK2/STAT3 pathway. Biol Res. 2019;52(1):29. doi:10.1186/s40659-019-0236-5
   PubMed Web of Science ®Google Scholar
• Kaushal GP. Autophagy protects proximal tubular cells from injury and apoptosis. Kidney Int. 2012;82(12):1250–1253. doi:10.1038/ki.2012.337
   PubMed Web of Science ®Google Scholar
• Qian Y, Commane M, Ninomiya-Tsuji J, Matsumoto K, Li X. IRAK-mediated translocation of TRAF6 and TAB2 in the interleukin-1-induced activation of NFkappa B. J Biol Chem. 2001;276(45):41661–41667. doi:10.1074/jbc.M102262200
   PubMed Web of Science ®Google Scholar
• Kopp E, Medzhitov R. Recognition of microbial infection by toll-like receptors. Curr Opin Immunol. 2003;15(4):396–401. doi:10.1016/S0952-7915(03)00080-3
   PubMed Web of Science ®Google Scholar
• Plociennikowska A, Hromada-Judycka A, Borzecka K, Kwiatkowska K. Co-operation of TLR4 and raft proteins in LPS-induced pro-inflammatory signaling. Cell Mol Life Sci. 2015;72(3):557–581. doi:10.1007/s00018-014-1762-5
   PubMed Web of Science ®Google Scholar
• Bellomo R, Kellum JA, Ronco C, et al. Acute kidney injury in sepsis. Intensive Care Med. 2017;43(6):816–828. doi:10.1007/s00134-017-4755-7
   PubMed Web of Science ®Google Scholar
• Gomez H, Kellum JA. Sepsis-induced acute kidney injury. Curr Opin Crit Care. 2016;22(6):546–553. doi:10.1097/MCC.0000000000000356
   PubMed Web of Science ®Google Scholar
• Hunt C, Calderwood S. Characterization and sequence of a mouse hsp70 gene and its expression in mouse cell lines. Gene. 1990;87(2):199–204. doi:10.1016/0378-1119(90)90302-8
   PubMed Web of Science ®Google Scholar
• Wilhide ME, Tranter M, Ren X, et al. Identification of a NF-kappaB cardioprotective gene program: NF-kappaB regulation of Hsp70.1 contributes to cardioprotection after permanent coronary occlusion. J Mol Cell Cardiol. 2011;51(1):82–89. doi:10.1016/j.yjmcc.2011.03.011
   PubMed Web of Science ®Google Scholar
• Van Molle W, Wielockx B, Mahieu T, et al. HSP70 protects against TNF-induced lethal inflammatory shock. Immunity. 2002;16(5):685–695. doi:10.1016/S1074-7613(02)00310-2
   PubMed Web of Science ®Google Scholar
• Lee KH, Lee CT, Kim YW, Han SK, Shim YS, Yoo CG. Heat shock protein 70 negatively regulates the heat-shock-induced suppression of the IkappaB/NF-kappaB cascade by facilitating IkappaB kinase renaturation and blocking its further denaturation. Exp Cell Res. 2005;307(1):276–284. doi:10.1016/j.yexcr.2005.03.014
   PubMed Web of Science ®Google Scholar
• King TA, Ghazaleh RA, Juhn SK, Adams GL, Ondrey FG. Induction of heat shock protein 70 inhibits NF-kappa-B in squamous cell carcinoma. Otolaryngol Head Neck Surg. 2005;133(1):70–79. doi:10.1016/j.otohns.2004.04.038
   PubMed Web of Science ®Google Scholar
• Uchinami H, Yamamoto Y, Kume M, et al. Effect of heat shock preconditioning on NF-kappaB/I-kappaB pathway during I/R injury of the rat liver. Am J Physiol Gastrointest Liver Physiol. 2002;282(6):G962–971. doi:10.1152/ajpgi.00466.2001
   PubMed Web of Science ®Google Scholar
• Dokladny K, Lobb R, Wharton W, Ma TY, Moseley PL. LPS-induced cytokine levels are repressed by elevated expression of HSP70 in rats: possible role of NF-kappaB. Cell Stress Chaperones. 2010;15(2):153–163. doi:10.1007/s12192-009-0129-6
   PubMed Web of Science ®Google Scholar
• Wang Z, Jin H, Li C, Hou Y, Mei Q, Fan D. Heat shock protein 72 protects kidney proximal tubule cells from injury induced by triptolide by means of activation of the MEK/ERK pathway. Int J Toxicol. 2009;28(3):177–189. doi:10.1177/1091581809337418
   PubMed Web of Science ®Google Scholar
• Wang Z, Gall JM, Bonegio RG, et al. Induction of heat shock protein 70 inhibits ischemic renal injury. Kidney Int. 2011;79(8):861–870. doi:10.1038/ki.2010.527
   PubMed Web of Science ®Google Scholar
• Wei S, Gao Y, Dai X, et al. SIRT1-mediated HMGB1 deacetylation suppresses sepsis-associated acute kidney injury. Am J Physiol Renal Physiol. 2019;316(1):F20–F31. doi:10.1152/ajprenal.00119.2018
   PubMed Web of Science ®Google Scholar
• Feoktistova M, Geserick P, Leverkus M. Crystal violet assay for determining viability of cultured cells. Cold Spring Harb Protoc. 2016;2016(4):pdbprot087379. doi:10.1101/pdb.prot087379
   Google Scholar
• Kumaran GK, Hanukoglu I. Identification and classification of epithelial cells in nephron segments by actin cytoskeleton patterns. FEBS J. 2020;287(6):1176–1194. doi:10.1111/febs.15088
   PubMed Web of Science ®Google Scholar
• Ma T, Yang B, Gillespie A, Carlson EJ, Epstein CJ, Verkman AS. Severely impaired urinary concentrating ability in transgenic mice lacking aquaporin-1 water channels. J Biol Chem. 1998;273(8):4296–4299. doi:10.1074/jbc.273.8.4296
   PubMed Web of Science ®Google Scholar
• Vallon V, Verkman AS, Schnermann J. Luminal hypotonicity in proximal tubules of aquaporin-1-knockout mice. Am J Physiol Renal Physiol. 2000;278(6):F1030–1033. doi:10.1152/ajprenal.2000.278.6.F1030
   PubMed Web of Science ®Google Scholar
• Glodowski SD, Wagener G. New insights into the mechanisms of acute kidney injury in the intensive care unit. J Clin Anesth. 2015;27(2):175–180. doi:10.1016/j.jclinane.2014.09.011
   PubMed Web of Science ®Google Scholar
• Murugan R, Karajala-Subramanyam V, Lee M, et al. Acute kidney injury in non-severe pneumonia is associated with an increased immune response and lower survival. Kidney Int. 2010;77(6):527–535. doi:10.1038/ki.2009.502
   PubMed Web of Science ®Google Scholar
• Feder ME, Hofmann GE. Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu Rev Physiol. 1999;61:243–282. doi:10.1146/annurev.physiol.61.1.243
   PubMed Web of Science ®Google Scholar
• Srivastava P. Roles of heat-shock proteins in innate and adaptive immunity. Nat Rev Immunol. 2002;2(3):185–194. doi:10.1038/nri749
   PubMed Web of Science ®Google Scholar
• Polla BS, Bachelet M, Elia G, Santoro MG. Stress proteins in inflammation. Ann N Y Acad Sci. 1998;851:75–85. doi:10.1111/j.1749-6632.1998.tb08979.x
   PubMed Web of Science ®Google Scholar
• Basile DP, Donohoe D, Cao X, Van Why SK. Resistance to ischemic acute renal failure in the Brown Norway rat: a new model to study cytoprotection. Kidney Int. 2004;65(6):2201–2211. doi:10.1111/j.1523-1755.2004.00637.x
   PubMed Web of Science ®Google Scholar
• Hsu JH, Yang RC, Lin SJ, et al. Exogenous heat shock cognate protein 70 pretreatment attenuates cardiac and hepatic dysfunction with associated anti-inflammatory responses in experimental septic shock. Shock. 2014;42(6):540–547. doi:10.1097/SHK.0000000000000254
   PubMed Web of Science ®Google Scholar
• Jo SK, Ko GJ, Boo CS, Cho WY, Kim HK. Heat preconditioning attenuates renal injury in ischemic ARF in rats: role of heat-shock protein 70 on NF-kappaB-mediated inflammation and on tubular cell injury. J Am Soc Nephrol. 2006;17(11):3082–3092. doi:10.1681/ASN.2005101077
   PubMed Web of Science ®Google Scholar
• Shi Y, Tu Z, Tang D, et al. The inhibition of LPS-induced production of inflammatory cytokines by HSP70 involves inactivation of the NF-kappaB pathway but not the MAPK pathways. Shock. 2006;26(3):277–284. doi:10.1097/01.shk.0000223134.17877.ad
   PubMed Web of Science ®Google Scholar
• Tanaka T, Shibazaki A, Ono R, Kaisho T. HSP70 mediates degradation of the p65 subunit of nuclear factor kappaB to inhibit inflammatory signaling. Sci Signal. 2014;7(356):ra119. doi:10.1126/scisignal.2005533
   PubMed Web of Science ®Google Scholar
• Chen H, Wu Y, Zhang Y, et al. Hsp70 inhibits lipopolysaccharide-induced NF-kappaB activation by interacting with TRAF6 and inhibiting its ubiquitination. FEBS Lett. 2006;580(13):3145–3152. doi:10.1016/j.febslet.2006.04.066
   PubMed Web of Science ®Google Scholar
• Wang LC, Liao LX, Lv HN, et al. Highly selective activation of heat shock protein 70 by allosteric regulation provides an insight into efficient neuroinflammation inhibition. EBioMedicine. 2017;23:160–172. doi:10.1016/j.ebiom.2017.08.011
   PubMed Web of Science ®Google Scholar
• Guicciardi ME, Gores GJ. Life and death by death receptors. FASEB J. 2009;23(6):1625–1637. doi:10.1096/fj.08-111005
   PubMed Web of Science ®Google Scholar
• Boatright KM, Salvesen GS. Mechanisms of caspase activation. Curr Opin Cell Biol. 2003;15(6):725–731. doi:10.1016/j.ceb.2003.10.009
   PubMed Web of Science ®Google Scholar
• Kroemer G, Galluzzi L, Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol Rev. 2007;87(1):99–163. doi:10.1152/physrev.00013.2006
   PubMed Web of Science ®Google Scholar
• Pistritto G, Trisciuoglio D, Ceci C, Garufi A, D’Orazi G. Apoptosis as anticancer mechanism: function and dysfunction of its modulators and targeted therapeutic strategies. Aging-Us. 2016;8(4):603–619. doi:10.18632/aging.100934
   Web of Science ®Google Scholar
• Degterev A, Boyce M, Yuan J. A decade of caspases. Oncogene. 2003;22(53):8543–8567. doi:10.1038/sj.onc.1207107
   PubMed Web of Science ®Google Scholar
• Lee SY, Lee YS, Choi HM, et al. Distinct pathophysiologic mechanisms of septic acute kidney injury: role of immune suppression and renal tubular cell apoptosis in murine model of septic acute kidney injury. Crit Care Med. 2012;40(11):2997–3006. doi:10.1097/CCM.0b013e31825b912d
   PubMed Web of Science ®Google Scholar
• Zhang B, Zeng M, Li M, et al. Protopine protects mice against LPS-induced acute kidney injury by inhibiting apoptosis and inflammation via the TLR4 signaling pathway. Molecules. 2019;25(1):15. doi:10.3390/molecules25010015
   PubMed Web of Science ®Google Scholar
• Lerolle N, Nochy D, Guerot E, et al. Histopathology of septic shock induced acute kidney injury: apoptosis and leukocytic infiltration. Intensive Care Med. 2010;36(3):471–478. doi:10.1007/s00134-009-1723-x
   PubMed Web of Science ®Google Scholar
• Zhu Y, Fu Y, Lin H. Baicalin inhibits renal cell apoptosis and protects against acute kidney injury in pediatric sepsis. Med Sci Monit. 2016;22:5109–5115. doi:10.12659/MSM.899061
   PubMed Web of Science ®Google Scholar