Do reciprocal interactions between cell stress proteins and cytokines create a new intra-/extra-cellular signalling nexus?

Cell Stress and Chaperones

Volumn 18, Issue 6, 2013, Pages 685-701

  Henderson, Brian ^a   Kaiser, Frank ^a  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

Author keywords

Cell stress proteins; Cytokine networks; Cytokines; Systems biology; Unfolded protein response

Indexed keywords

CYTOKINE; HEAT SHOCK PROTEIN;

ENDOPLASMIC RETICULUM; HUMAN; METABOLISM; SIGNAL TRANSDUCTION; UNFOLDED PROTEIN RESPONSE;

CYTOKINES; ENDOPLASMIC RETICULUM; HEAT-SHOCK PROTEINS; HUMANS; SIGNAL TRANSDUCTION; UNFOLDED PROTEIN RESPONSE;

EID: 84898132858     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1007/s12192-013-0444-9     Document Type: Article

References (179)

1. Abcouwer, S.F., Marjon, P.L., Loper, R.K., Vander Jagt, D.L., Response of VEGF expression to amino acid deprivation and inducers of endoplasmic reticulum stress. Investig Ophthalmol Vis Sci 43 (2002), 2791–2798.
2. Adams, J., Kauffman, M., Development of the proteasome inhibitor Velcade (Bortezomib). Cancer Investig 22 (2004), 304–311 1:CAS:528:DC%2BD2cXjtl2qtb0%3D 10.1081/CNV-120030218.
3. Adolph, T.-E., Niederreiter, L., Blumberg, R.S., Kaser, A., Endoplasmic reticulum stress and inflammation. Dig Dis 30 (2012), 341–346 22796794 10.1159/000338121.
4. Ala, Y., Palluy, O., Favero, J., Bonne, C., Modat, G., Dornand, J., Hypoxia/reoxygenation stimulates endothelial cells to promote interleukin-1 and interleukin-6 production. Effects of free radical scavengers. Agents Actions 37 (1992), 134–139 1456174 1:CAS:528:DyaK38XlvV2qsLk%3D 10.1007/BF01987902.
5. Alloza, I., Baxter, A., Chen, Q., Matthiesen, R., Vandenbroeck, K., Celecoxib inhibits interleukin-12 alphabeta and beta2 folding and secretion by a novel COX2-independent mechanism involving chaperones of the endoplasmic reticulum. Mol Pharmacol 69 (2006), 1579–1587 16467190 1:CAS:528:DC%2BD28XksVWrt7s%3D 10.1124/mol.105.020669.
6. Ambade, A., Catalano, D., Lim, A., Mandrekar, P., Inhibition of heat shock protein (molecular weight 90 kDa) attenuates proinflammatory cytokines and prevents lipopolysaccharide-induced liver injury in mice. Hepatology 55 (2012), 1585–1595 22105779 1:CAS:528:DC%2BC38Xlslyju70%3D 10.1002/hep.24802.
7. Asea, A., Kraeft, S.K., Kurt-Jones, E.A., Stevenson, M.A., Chen, L.B., Finberg, R.W., Koo, G.C., Calderwood, S.K., HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nat Med 6 (2000), 435–442 10742151 1:CAS:528:DC%2BD3cXisVOru7g%3D 10.1038/74697.
8. Back, S.H., Kaufman, R.J., Endoplasmic reticulum stress and type 2 diabetes. Annu Rev Biochem 81 (2012), 767–793 22443930 1:CAS:528:DC%2BC38XhtVGlsL7K 10.1146/annurev-biochem-072909-095555.
9. Belka, C., Ahlers, A., Sott, C., Gaestel, M., Herrmann, F., Brach, M.A., Interleukin (IL)-6 signaling leads to phosphorylation of the small heat shock protein (Hsp)27 through activation of the MAP kinase and MAPKAP kinase 2 pathway in monocytes and monocytic leukemia cells. Leukemia 9 (1995), 288–294 7869766 1:STN:280:DyaK2M7nsVCjug%3D%3D.
10. Billiet, L., Furman, C., Larigauderie, G., Copin, C., Brand, K., Fruchart, J.C., Rouis, M., Extracellular human thioredoxin-1 inhibits lipopolysaccharide-induced interleukin-1beta expression in human monocyte-derived macrophages. J Biol Chem 280 (2005), 40310–40318 16207716 1:CAS:528:DC%2BD2MXht1Gjs7vP 10.1074/jbc.M503644200.
11. Björk, J.K., Sistonen, L., Regulation of the members of the mammalian heat shock factor family. FEBS J 277 (2010), 4126–4139 20945529 10.1111/j.1742-4658.2010.07828.x 1:CAS:528:DC%2BC3cXhtlegtL%2FN.
12. Blanchet, X., Langer, M., Weber, C., Koenen, R.R., von Hundelshausen, P., Touch of chemokines. Front Immunol, 3, 2012, 175 22807925 10.3389/fimmu.2012.00175.
13. Bocci, V., Paulesu, L., Studies on the biological effects of ozone 1. Induction of interferon gamma on human leucocytes. Haematologica 75 (1990), 510–515 2129118 1:CAS:528:DyaK3MXlt1KnsL0%3D.
14. Bogunovic, D., Byun, M., Durfee, L.A., Abhyankar, A., Sanal, O., Mansouri, D., Salem, S., Radovanovic, I., Grant, A.V., Adimi, P., Mansouri, N., Okada, S., Bryant, V.L., Kong, X.F., Kreins, A., Velez, M.M., Boisson, B., Khalilzadeh, S., Ozcelik, U., Darazam, I.A., Schoggins, J.W., Rice, C.M., Al-Muhsen, S., Behr, M., Vogt, G., Puel, A., Bustamante, J., Gros, P., Huibregtse, J.M., Abel, L., Boisson-Dupuis, S., Casanova, J.L., Mycobacterial disease and impaired IFN-γ immunity in humans with inherited ISG15 deficiency. Science 337 (2012), 1684–1688 22859821 1:CAS:528:DC%2BC38Xhtl2ntrjN 10.1126/science.1224026.
15. Boyce, M., Yuan, J., Cellular response to endoplasmic reticulum stress: a matter of life or death. Cell Death Differ 13:3 (2006), 363–373.
16. Bradbury, J.W., Vehrencamp, S.L., 1998, Sinauer Associates, Sunderland.
17. Broemer, M., Krappmann, D., Scheidereit, C., Requirement of Hsp90 activity for IkappaB kinase (IKK) biosynthesis and for constitutive and inducible IKK and NF-kappaB activation. Oncogene 23 (2004), 5378–5386 15077173 1:CAS:528:DC%2BD2cXlsVOmsbw%3D 10.1038/sj.onc.1207705.
18. Cahill, C.M., Waterman, W.R., Xie, Y., Auron, P.E., Calderwood, S.K., Transcriptional repression of the pro-interleukin 1beta gene by heat shock factor 1. J Biol Chem 271 (1996), 24874–24879 8926278 1:CAS:528:DyaK28XmtFegtLs%3D.
19. 2+, leading to induction of endoplasmic reticulum stress in pancreatic beta-cells. Diabetes 54 (2005), 452–461 15677503 1:CAS:528:DC%2BD2MXhsVCrsb0%3D 10.2337/diabetes.54.2.452.
20. Castells M (2011) The rise of the network society. Wiley-Blackwell.
21. Chang, J.W., Lee, S.H., Lu, Y., Yoo, Y.J., Transforming growth factor-beta1 induces the non-classical secretion of peroxiredoxin-I in A549 cells. Biochem Biophys Res Commun 345:1 (2006), 118–123.
22. Chen, Y.G., Ashok, B.T., Liu, X., Garikapaty, V.P., Mittelman, A., Tiwari, R.K., Induction of heat shock protein gp96 by immune cytokines. Cell Stress Chaperon 8:3 (2003), 242–248.
23. Chen, L., Jarujaron, S., Wu, X., Sun, L., Zha, W., Liang, G., Wang, X., Gurley, E.C., Studer, E.J., Hylemon, P.B., Pandak, W.M. Jr, Zhang, L., Wang, G., Li, X., Dent, P., Zhou, H., HIV protease inhibitor lopinavir-induced TNF-α and IL-6 expression is coupled to the unfolded protein response and ERK signaling pathways in macrophages. Biochem Pharmacol 78 (2009), 70–77 19447225 1:CAS:528:DC%2BD1MXmtVKksrs%3D 10.1016/j.bcp.2009.03.022.
24. Cheng, C.F., Sahu, D., Tsen, F., Zhao, Z., Fan, J., Kim, R., Wang, X., O'Brien, K., Li, Y., Kuang, Y., Chen, M., Woodley, D.T., Li, W., A fragment of secreted Hsp90α carries properties that enable it to accelerate effectively both acute and diabetic wound healing in mice. J Clin Invest 121 (2011), 4348–4361 22019588 1:CAS:528:DC%2BC3MXhsVCksLzF 10.1172/JCI46475.
25. Choi, S.E., Choi, K.M., Yoon, I.H., Shin, J.Y., Kim, J.S., Park, W.Y., IL-6 protects pancreatic islet β cells from pro-inflammatory cytokines-induced cell death and functional impairment in vitro and in vivo. Transpl Immunol 13 (2004), 43–53 15203128 1:CAS:528:DC%2BD2cXltVKjtL4%3D 10.1016/j.trim.2004.04.001.
26. Choi, K., Ni, L., Jonakait, G.M., Fas ligation and tumor necrosis factor α activation of murine astrocytes promote heat shock factor-1 activation and heat shock protein expression leading to chemokine induction and cell survival. J Neurochem 116 (2011), 438–448 21114495 1:CAS:528:DC%2BC3MXhsl2msbk%3D 10.1111/j.1471-4159.2010.07124.x.
27. Cnop, M., Ladrière, L., Igoillo-Esteve, M., Moura, R.F., Cunha, D.A., Causes and cures for endoplasmic reticulum stress in lipotoxic β-cell dysfunction. Diabetes Obes Metab 12:Suppl 2 (2010), 76–82 21029303 1:CAS:528:DC%2BC3cXhsVGgs7jI 10.1111/j.1463-1326.2010.01279.x.
28. Cortes-Bratti, X., Bassères, E., Herrera-Rodriguez, F., Botero-Kleiven, S., Coppotelli, G., Andersen, J.B., Masucci, M.G., Holmgren, A., Chaves-Olarte, E., Frisan, T., Avila-Cariño, J., Thioredoxin 80-activated-monocytes (TAMs) inhibit the replication of intracellular pathogens. PLoS One, 6, 2011, e16960 21365006 1:CAS:528:DC%2BC3MXisl2hu7Y%3D 10.1371/journal.pone.0016960.
29. Davies, M.J., Miranda, E., Roussel, B.D., Kaufman, R.J., Marciniak, S.J., Lomas, D.A., Neuroserpin polymers activate NF-kappaB by a calcium signaling pathway that is independent of the unfolded protein response. J Biol Chem 284 (2009), 18202–18209 19423713 1:CAS:528:DC%2BD1MXnslegtLw%3D 10.1074/jbc.M109.010744.
30. D'Cunha, J., Knight, E. Jr, Haas, A.L., Truitt, R.L., Borden, E.C., Immunoregulatory properties of ISG15, an interferon-induced cytokine. Proc Natl Acad Sci U S A 93 (1996), 211–215 8552607 10.1073/pnas.93.1.211.
31. de Waal, M.R., Abrams, J., Bennett, B., Figdor, C.G., de Vries, J.E., Interleukin 10 (IL-10) inhibits cytokine synthesis by human monocytes: an autoregulatory role of IL-10 produced by monocytes. J Exp Med 174 (1991), 1209–1220 10.1084/jem.174.5.1209.
32. de Zoeten, E.F., Wang, L., Butler, K., Beier, U.H., Akimova, T., Sai, H., Bradner, J.E., Mazitschek, R., Kozikowski, A.P., Matthias, P., Hancock, W.W., Histone deacetylase 6 and heat shock protein 90 control the functions of Foxp3(+) T-regulatory cells. Mol Cell Biol 31 (2011), 2066–2078 21444725 10.1128/MCB.05155-11 1:CAS:528:DC%2BC3MXotVyrs7g%3D.
33. De, A.K., Kodys, K.M., Yeh, B.S., Miller-Graziano, C., Exaggerated human monocyte IL-10 concomitant to minimal TNF-alpha induction by heat-shock protein 27 (Hsp27) suggests Hsp27 is primarily an antiinflammatory stimulus. J Immunol 165 (2000), 3951–3958 11034403 1:CAS:528:DC%2BD3cXntVyisbw%3D.
34. DeLay, M.L., Turner, M.J., Klenk, E.I., Smith, J.A., Sowders, D.P., Colbert, R.A., HLA-B27 misfolding and the unfolded protein response augment interleukin-23 production and are associated with Th17 activation in transgenic rats. Arthritis Rheum 60 (2009), 2633–2643 19714651 1:CAS:528:DC%2BD1MXht1WhtLjI 10.1002/art.24763.
35. Denis, R.G., Arruda, A.P., Romanatto, T., Milanski, M., Coope, A., Solon, C., Razolli, D.S., Velloso, L.A., TNF-α transiently induces endoplasmic reticulum stress and an incomplete unfolded protein response in the hypothalamus. Neuroscience 170 (2010), 1035–1044 20709159 1:CAS:528:DC%2BC3cXht1Cls7rJ 10.1016/j.neuroscience.2010.08.013.
36. Dietl, K., Renner, K., Dettmer, K., Timischl, B., Eberhart, K., Dorn, C., Hellerbrand, C., Kastenberger, M., Kunz-Schughart, L.A., Oefner, P.J., Andreesen, R., Gottfried, E., Kreutz, M.P., Lactic acid and acidification inhibit TNF secretion and glycolysis of human monocytes. J Immunol 184 (2010), 1200–1209 20026743 1:CAS:528:DC%2BC3cXhtVGisL8%3D 10.4049/jimmunol.0902584.
37. Diggle, S.P., Gardner, A., West, S.A., Griffin, A.S., Evolutionary theory of bacterial quorum sensing: when is a signal not a signal?. Phil Trans R Soc B 362 (2007), 1241–1249 17360270 1:CAS:528:DC%2BD2sXosF2js78%3D 10.1098/rstb.2007.2049.
38. Dinarello, C.A., Was the original endogenous pyrogen interleukin-1?. Bomford, R., Henderson, B., (eds.) Interleukin-1, inflammation and disease, 1989, Elsevier, New York, 17–28.
39. Dinarello, C.A., Historical review of cytokines. Eur J Immunol 37 (2007), S34–S45 17972343 1:CAS:528:DC%2BD2sXhsVSgtbbF 10.1002/eji.200737772.
40. Dinarello, C.A., IL-1: discoveries, controversies and future directions. Eur J Immunol 40 (2010), 599–606 20201008 1:CAS:528:DC%2BC3cXjtVWrs78%3D 10.1002/eji.201040319.
41. Elmarakby, A.A., Sullivan, J.C., Relationship between oxidative stress and inflammatory cytokines in diabetic nephropathy. Cardiovasc Ther 30 (2012), 49–59 20718759 1:CAS:528:DC%2BC38XjvVWjurs%3D 10.1111/j.1755-5922.2010.00218.x.
42. Ensor, J.E., Crawford, E.K., Hasday, J.D., Warming macrophages to febrile range destabilizes tumor necrosis factor-alpha mRNA without inducing heat shock. Am J Physiol 269 (1995), C1140–C1146 7491902 1:CAS:528:DyaK2MXpslOiurg%3D.
43. Ferm, M.T., Söderström, K., Jindal, S., Grönberg, A., Ivanyi, J., Young, R., Kiessling, R., Induction of human hsp60 expression in monocytic cell lines. Int Immunol 4 (1992), 305–311 1567788 1:STN:280:DyaK383jt1KjsQ%3D%3D 10.1093/intimm/4.3.305.
44. Frankenstein, Z., Alon, U., Cohen, I.R., The immune-body cytokine network defines a social architecture of cell interactions. Biol Direct, 1, 2006, 32 17062134 10.1186/1745-6150-1-32 1:CAS:528:DC%2BD28Xht1ajsb3M.
45. Freshney, N.W., Rawlinson, L., Guesdon, F., Jones, E., Cowley, S., Hsuan, J., Saklatvala, J., Interleukin-1 activates a novel protein kinase cascade that results in the phosphorylation of Hsp27. Cell 78 (1994), 1039–1049 7923354 1:CAS:528:DyaK2cXmt1ynt7k%3D 10.1016/0092-8674(94)90278-X.
46. Fu, Q.S., Song, A.X., Hu, H.Y., Structural aspects of ubiquitin binding specificities. Curr Protein Pept Sci 13 (2012), 482–489 22812525 1:CAS:528:DC%2BC38XhsVKku7%2FJ 10.2174/138920312802430581.
47. Gallucci, S., Matzinger, P., Danger signals: SOS to the immune system. Curr Opin Immunol 13 (2001), 114–119 11154927 1:CAS:528:DC%2BD3MXhtFChsLc%3D 10.1016/S0952-7915(00)00191-6.
48. Guesdon, F., Saklatvala, J., Identification of a cytoplasmic protein kinase regulated by IL-1 that phosphorylates the small heat shock protein, hsp27. J Immunol 147 (1991), 3402–3407 1940343 1:CAS:528:DyaK38XlslSiug%3D%3D.
49. Guy, G.R., Cairns, J., Ng, S.B., Tan, Y.H., Inactivation of a redox-sensitive protein phosphatase during the early events of tumor necrosis factor/interleukin-1 signal transduction. J Biol Chem 268 (1993), 2141–2148 8380591 1:CAS:528:DyaK3sXhsVGksbc%3D.
50. Hahm, E., Li, J., Kim, K., Huh, S., Rogelj, S., Cho, J., Extracellular protein disulfide isomerase regulates ligand binding activity of αMβ2 integrin and neutrophil recruitment during vascular inflammation. Blood 121 (2013), 3789–3800 23460613 1:CAS:528:DC%2BC3sXnsl2jtLk%3D 10.1182/blood-2012-11-467985.
51. Han, G., Li, F., Singh, T.P., Wolf, P., Wang, X.J., The pro-inflammatory role of TGFβ1: a paradox?. Int J Biol Sci 8 (2012), 228–235 22253566 1:CAS:528:DC%2BC38XhsFWisLs%3D 10.7150/ijbs.8.228.
52. Hanschmann EM, Godoy JR, Berndt C, Hudemann C, Lillig CH (2013) Thioredoxins, glutaredoxins, and peroxiredoxins—molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling. Antioxid Redox Signal. doi: 10.1089/ars.2012.4599.
53. Hayakawa, M., Miyashita, H., Sakamoto, I., Kitagawa, M., Tanaka, H., Yasuda, H., Karin, M., Kikugawa, K., Evidence that reactive oxygen species do not mediate NF-kappaB activation. EMBO J 22 (2003), 3356–3366 12839997 1:CAS:528:DC%2BD3sXltFyhurw%3D 10.1093/emboj/cdg332.
54. Hayakawa, K., Hiramatsu, N., Okamura, M., Yao, J., Paton, A.W., Paton, J.C., Kitamura, M., Blunted activation of NF-kappaB and NF-kappaB-dependent gene expression by geranylgeranylacetone: involvement of unfolded protein response. Biochem Biophys Res Commun 365 (2008), 47–53 17971294 1:CAS:528:DC%2BD2sXhtlalsL%2FM 10.1016/j.bbrc.2007.10.115.
55. He, H., Soncin, F., Grammatikakis, N., Li, Y., Siganou, A., Gong, J., Brown, S.A., Kingston, R.E., Calderwood, S.K., Elevated expression of heat shock factor (HSF) 2A stimulates HSF1-induced transcription during stress. J Biol Chem 278 (2003), 35465–34575 12813038 1:CAS:528:DC%2BD3sXntVajsro%3D 10.1074/jbc.M304663200.
56. Helqvist, S., Polla, B.S., Johannesen, J., Nerup, J., Heat shock protein induction in rat pancreatic islets by recombinant human interleukin 1 beta. Diabetologia 34 (1991), 150–156 1884886 1:CAS:528:DyaK3MXkt1Ogu7g%3D 10.1007/BF00418268.
57. Henderson, B., Pettipher, E.R., Arthritogenic actions of recombinant IL-1 and tumour necrosis factor α in the rabbit: Evidence for synergistic interactions between cytokines in vivo. Clin Exp Immunol 75 (1989), 306–310 2784740 1:CAS:528:DyaL1MXhslWmtL8%3D.
58. Henderson, B., Pockley, A.G., 2005, Cambridge University Press, Cambridge.
59. Henderson, B., Pockley, A.G., Molecular chaperones and protein-folding catalysts as intercellular signaling regulators in immunity and inflammation. J Leukoc Biol 88 (2010), 445–462 20445014 1:CAS:528:DC%2BC3cXhtFertrnL 10.1189/jlb.1209779.
60. Henderson, B., Pockley, A.G., Proteotoxic stress and circulating cell stress proteins in the cardiovascular diseases. Cell Stress Chaperones 17 (2012), 303–311 22215517 1:CAS:528:DC%2BC38XkvVentb4%3D 10.1007/s12192-011-0318-y.
61. Henderson B, Fares MA, Lund PA (2013) Chaperonin 60: a paradoxical, evolutionarily-conserved, protein family with multiple moonlighting functions. Biol Rev Camb Philos Soc. doi: 10.1111/brv.12037.
62. Higgs, G.A., Henderson, B., 2000, Birkhauser, Boston.
63. Howard, M., Roux, J., Lee, H., Miyazawa, B., Lee, J.W., Gartland, B., Howard, A.J., Matthay, M.A., Carles, M., Pittet, J.F., Activation of the stress protein response inhibits the STAT1 signalling pathway and iNOS function in alveolar macrophages: role of Hsp90 and Hsp70. Thorax 65 (2010), 346–353 20388761 10.1136/thx.2008.101139.
64. Hu, S., Ciancio, M.J., Lahav, M., Fujiya, M., Lichtenstein, L., Anant, S., Musch, M.W., Chang, E.B., Translational inhibition of colonic epithelial heat shock proteins by IFN-gamma and TNF-alpha in intestinal inflammation. Gastroenterology 133 (2007), 1893–1904 18054561 1:CAS:528:DC%2BD1cXnt1KqtQ%3D%3D 10.1053/j.gastro.2007.09.026.
65. Huang, Q.Q., Pope, R.M., The role of glycoprotein 96 in the persistent inflammation of rheumatoid arthritis. Arch Biochem Biophys 530 (2012), 1–6 23257071 10.1016/j.abb.2012.12.008 1:CAS:528:DC%2BC3sXhs1CisLo%3D.
66. Ibelgaufts H (2012) Cytokines and cells online pathfinder encyclopaedia. http://www.copewithcytokines.de/.
67. Inouye, S., Fujimoto, M., Nakamura, T., Takaki, E., Hayashida, N., Hai, T., Nakai, A., Heat shock transcription factor 1 opens chromatin structure of interleukin-6 promoter to facilitate binding of an activator or a repressor. J Biol Chem 282 (2007), 33210–33217 17766920 1:CAS:528:DC%2BD2sXht1ClurzK 10.1074/jbc.M704471200.
68. Itahana, Y., Piens, M., Sumida, T., Fong, S., Muschler, J., Desprez, P.Y., Regulation of clusterin expression in mammary epithelial cells. Exp Cell Res 313:5 (2007), 943–951.
69. Ishii, T., Warabi, E., Yanagawa, T., Novel roles of peroxiredoxins in inflammation, cancer and innate immunity. J Clin Biochem Nutr 50 (2012), 91–105 22448089 1:CAS:528:DC%2BC38Xmt1Shtb4%3D 10.3164/jcbn.11-109.
70. Jancic, C.C., Cabrini, M., Gabelloni, M.L., Rodríguez Rodrigues, C., Salamone, G., Trevani, A.S., Geffner, J., Low extracellular pH stimulates the production of IL-1β by human monocytes. Cytokine 57 (2012), 258–268 22154780 1:CAS:528:DC%2BC38XlsVKqtg%3D%3D 10.1016/j.cyto.2011.11.013.
71. Ji, S.Q., Neustrom, S., Willis, G.M., Spurlock, M.E., Proinflammatory cytokines regulate myogenic cell proliferation and fusion but have no impact on myotube protein metabolism or stress protein expression. J Interferon Cytokine Res 18:10 (1998), 879–888.
72. Johnson, B.J., Le, T.T., Dobbin, C.A., Banovic, T., Howard, C.B., Flores Fde, M., Vanags, D., Naylor, D.J., Hill, G.R., Suhrbier, A., Heat shock protein 10 inhibits lipopolysaccharide-induced inflammatory mediator production. J Biol Chem 280 (2005), 4037–4047 15546885 1:CAS:528:DC%2BD2MXhtVyntLs%3D 10.1074/jbc.M411569200.
73. Kang, M.W., Jang, J.Y., Choi, J.Y., Kim, S.H., Oh, J., Cho, B.S., Lee, C.E., Induction of IFN-gamma gene expression by thioredoxin: positive feed-back regulation of Th1 response by thioredoxin and IFN-gamma. Cell Physiol Biochem 21 (2008), 215–224 18209488 1:CAS:528:DC%2BD1cXps1ajuw%3D%3D 10.1159/000113763.
74. Karhumäki, E., Helin, H., Regulation of oxidative metabolism by interferon-gamma during human monocyte to macrophage differentiation. Med Biol 65 (1987), 261–266 2836672.
75. Kim, S.W., Lee, J.K., NO-induced downregulation of HSP10 and HSP60 expression in the postischemic brain. J Neurosci Res 85:6 (2007), 1252–1259.
76. Kim, A.H., Khanna, A., Aten, R.F., Olive, D.L., Behrman, H.R., Cytokine induction of heat shock protein in human granulosa-luteal cells. Mol Hum Reprod 2:8 (1996), 549–554.
77. Kitamura, M., Control of NF-κB and inflammation by the unfolded protein response. Int Rev Immunol 30 (2011), 4–15 21235322 1:CAS:528:DC%2BC3MXmtVClsQ%3D%3D 10.3109/08830185.2010.522281.
78. Kumar, H., Kawai, T., Akira, S., Pathogen recognition by the innate immune system. Int Rev Immunol 30 (2011), 16–34 21235323 1:CAS:528:DC%2BC3MXmtVCltw%3D%3D 10.3109/08830185.2010.529976.
79. Lee, Y.J., Lee, H.J., Choi, S.H., Jin, Y.B., An, H.J., Kang, J.H., Yoon, S.S., Lee, Y.S., Soluble HSPB1 regulates VEGF-mediated angiogenesis through their direct interaction. Angiogenesis 15 (2012), 229–242 22350794 1:CAS:528:DC%2BC38XnsVKrt74%3D 10.1007/s10456-012-9255-3.
80. Li, C., Liu, Q., Li, N., Chen, W., Wang, L., Wang, Y., Yu, Y., Cao, X., EAPF/Phafin-2, a novel endoplasmic reticulum-associated protein, facilitates TNF-alpha-triggered cellular apoptosis through endoplasmic reticulum-mitochondrial apoptotic pathway. J Mol Med (Berlin) 86 (2008), 471–484 1:CAS:528:DC%2BD1cXkvVSjt7g%3D 10.1007/s00109-007-0298-7.
81. Li, C., Li, J., Li, Y., Lang, S., Yougbare, I., Zhu, G., Chen, P., Ni, H., Crosstalk between platelets and the immune system: old systems with new discoveries. Adv Hematol, 2012, 2012, 384685 23008717.
82. Loeb, K.R., Haas, A.L., The interferon-inducible 15-kDa ubiquitin homolog conjugates to intracellular proteins. J Biol Chem 267 (1992), 7806–7813 1373138 1:CAS:528:DyaK38XktVGku7g%3D.
83. Löw-Friedrich, I., Weisensee, D., Mitrou, P., Schoeppe, W., Cytokines induce stress protein formation in cultured cardiac myocytes. Basic Res Cardiol 87 (1992), 12–18 1567350 10.1007/BF00795385.
84. Ma, H., Gong, H., Chen, Z., Liang, Y., Yuan, J., Zhang, G., Wu, J., Ye, Y., Yang, C., Nakai, A., Komuro, I., Ge, J., Zou, Y., Association of Stat3 with HSF1 plays a critical role in G-CSF-induced cardio-protection against ischemia/reperfusion injury. J Mol Cell Cardiol 52 (2012), 1282–1290 22426029 1:CAS:528:DC%2BC38XltVeiurc%3D 10.1016/j.yjmcc.2012.02.011.
85. Mahmood DF, Abderrazak A, Khadija EH, Simmet T, Rouis M (2013) The thioredoxin system as a therapeutic target in human health and disease. Antioxid Redox Signal. doi: 10.1089/ars.2012.4757.
86. Maier, J.A., Statuto, M., Ragnotti, G., Endogenous interleukin 1 alpha must be transported to the nucleus to exert its activity in human endothelial cells. Mol Cell Biol 14 (1994), 1845–1851 8114717 1:CAS:528:DyaK2cXhvV2nsbw%3D.
87. Maity, T.K., Henry, M.M., Tulapurkar, M.E., Shah, N.G., Hasday, J.D., Singh, I.S., Distinct, gene-specific effect of heat shock on heat shock factor-1 recruitment and gene expression of CXC chemokine genes. Cytokine 54 (2011), 61–67 21266308 1:CAS:528:DC%2BC3MXjsFClsrg%3D 10.1016/j.cyto.2010.12.017.
88. Majik, M.S., Yu, J.H., Jeong, L.S., A straightforward synthesis of K7174 a GATA-specific inhibitor. Bull Korean Chem Soc 33 (2012), 2903–2906 1:CAS:528:DC%2BC38XhsVyltb3P 10.5012/bkcs.2012.33.9.2903.
89. Manjili, M.H., 2012, Nova, New York.
90. Marcant, A., Denys, A., Melchior, A., Martinez, P., Deligny, A., Carpentier, M., Allain, F., Cyclophilin B attenuates the expression of TNF-α in lipopolysaccharide-stimulated macrophages through the induction of B cell lymphoma-3. J Immunol 189 (2012), 2023–2032 22798670 1:CAS:528:DC%2BC38XhtFaqsL%2FN 10.4049/jimmunol.1102803.
91. Marjon, P.L., Bobrovnikova-Marjon, E.V., Abcouwer, S.F., Expression of the pro-angiogenic factors vascular endothelial growth factor and interleukin-8/CXCL8 by human breast carcinomas is responsive to nutrient deprivation and endoplasmic reticulum stress. Mol Cancer, 3, 2004, 4 14738568 10.1186/1476-4598-3-4.
92. Martelli-Junior, H., Cotrim, P., Graner, E., Sauk, J.J., Coletta, R.D., Effect of transforming growth factor-beta1, interleukin-6, and interferon-gamma on the expression of type I collagen, heat shock protein 47, matrix metalloproteinase (MMP)-1 and MMP-2 by fibroblasts from normal gingiva and hereditary gingival fibromatosis. J Periodontol 74 (2003), 296–306 12710748 1:STN:280:DC%2BD3s7ptFektg%3D%3D 10.1902/jop.2003.74.3.296.
93. Matzinger, P., The danger model: a renewed sense of self. Science 296 (2002), 301–305 11951032 1:CAS:528:DC%2BD38XjtVWiurk%3D 10.1126/science.1071059.
94. Maynard Smith, J., Harper, D.G.C., 2003, Oxford University Press, Oxford.
95. McLaughlin, M., Alloza, I., Quoc, H.P., Scott, C.J., Hirabayashi, Y., Vandenbroeck, K., Inhibition of secretion of interleukin (IL)-12/IL-23 family cytokines by 4-trifluoromethyl-celecoxib is coupled to degradation via the endoplasmic reticulum stress protein HERP. J Biol Chem 285 (2010), 6960–6969 20054003 1:CAS:528:DC%2BC3cXisFaltbc%3D 10.1074/jbc.M109.056614.
96. Modlin, I.M., Kidd, M., Farhadi, J., Bayliss and Starling and the nascence of endocrinology. Regul Pept 93 (2000), 109–123 11033058 1:CAS:528:DC%2BD3cXntF2hur8%3D 10.1016/S0167-0115(00)00182-8.
97. Munakata, T., Semba, U., Shibuya, Y., Kuwano, K., Akagi, M., Arai, S., Induction of interferon-gamma production by human natural killer cells stimulated by hydrogen peroxide. J Immunol 134 (1985), 2449–2455 3919096 1:CAS:528:DyaL2MXhs1GjtLk%3D.
98. Murapa, P., Ward, M.R., Gandhapudi, S.K., Woodward, J.G., D'Orazio, S.E., Heat shock factor 1 protects mice from rapid death during Listeria monocytogenes infection by regulating expression of tumor necrosis factor alpha during fever. Infect Immun 79 (2011), 177–184 20956571 1:CAS:528:DC%2BC3MXisVegtL4%3D 10.1128/IAI.00742-09.
99. Nace, G., Evankovich, J., Eid, R., Tsung, A., Dendritic cells and damage-associated molecular patterns: endogenous danger signals linking innate and adaptive immunity. J Innate Immun 4 (2012), 6–15 22086146 1:CAS:528:DC%2BC3MXhs1WgsL3P 10.1159/000334245.
100. Nagarsekar, A., Hasday, J.D., Singh, I.S., CXC chemokines: a new family of heat-shock proteins?. Immunol Investig 34 (2005), 381–398 1:CAS:528:DC%2BD2MXpslyktrk%3D 10.1081/IMM-200067648.
101. Navarro-Millán, I., Curtis, J.R., Newest clinical trial results with antitumor necrosis factor and nonantitumor necrosis factor biologics for rheumatoid arthritis. Curr Opin Rheumatol 25 (2013), 384–390 23511719 10.1097/BOR.0b013e32835fc62e 1:CAS:528:DC%2BC3sXks1OntLc%3D.
102. Nicoletti-Carvalho, J.E., Nogueira, T.C., Gorjão, R., Bromati, C.R., Yamanaka, T.S., Boschero, A.C., Velloso, L.A., Curi, R., Anhê, G.F., Bordin, S., UPR-mediated TRIB3 expression correlates with reduced AKT phosphorylation and inability of interleukin 6 to overcome palmitate-induced apoptosis in RINm5F cells. J Endocrinol 206 (2010), 183–193 20488947 1:CAS:528:DC%2BC3cXhtVCjtrfM 10.1677/JOE-09-0356.
103. Noonan, E.J., Place, R.F., Rasoulpour, R.J., Giardina, C., Hightower, L.E., Cell number-dependent regulation of Hsp70B' expression: evidence of an extracellular regulator. J Cell Physiol 210 (2007), 201–211 17044073 1:CAS:528:DC%2BD28XhtlWktrnK 10.1002/jcp.20875.
104. Nowis, D., McConnell, E.J., Dierlam, L., Palamarchuk, A., Lass, A., Wójcik, C., TNF potentiates anticancer activity of bortezomib (Velcade) through reduced expression of proteasome subunits and dysregulation of unfolded protein response. Int J Cancer 121 (2007), 431–441 17373661 1:CAS:528:DC%2BD2sXmslOltLg%3D 10.1002/ijc.22695.
105. Ochs, S., 2005, Cambridge University Press, Cambridge.
106. Okamura, M., Takano, Y., Hiramatsu, N., Hayakawa, K., Yao, J., Paton, A.W., Paton, J.C., Kitamura, M., Suppression of cytokine responses by indomethacin in podocytes: a mechanism through induction of unfolded protein response. Am J Physiol Ren Physiol 295 (2008), F1495–F1503 1:CAS:528:DC%2BD1cXhsVWkurzM 10.1152/ajprenal.00602.2007.
107. Oliveira-Marques, V., Marinho, H.S., Cyrne, L., Antunes, F., Role of hydrogen peroxide in NF-kappaB activation: from inducer to modulator. Antioxid Redox Signal. 11 (2009), 2223–2243 19496701 1:CAS:528:DC%2BD1MXpvFaqsrs%3D 10.1089/ars.2009.2601.
108. Ooie, T., Takahashi, N., Saikawa, T., Nawata, T., Arikawa, M., Single oral dose of geranylgeranylacetone induces heat-shock protein 72 and renders protection against ischemia/reperfusion injury in rat heart. Circulation 104 (2001), 1837–1843 11591623 1:CAS:528:DC%2BD3MXotlWiu78%3D 10.1161/hc3901.095771.
109. Ortis, F., Cardozo, A.K., Crispim, D., Störling, J., Mandrup-Poulsen, T., Eizirik, D.L., Cytokine-induced proapoptotic gene expression in insulin-producing cells is related to rapid, sustained, and nonoscillatory nuclear factor-kappaB activation. Mol Endocrinol 20 (2006), 1867–1879 16556731 1:CAS:528:DC%2BD28XnvFajs7c%3D 10.1210/me.2005-0268.
110. Ozaki, K., Leonard, W.J., Cytokine and cytokine receptor pleiotropy and redundancy. J Biol Chem 277 (2002), 29355–29358 12072446 1:CAS:528:DC%2BD38XmsVKisbo%3D 10.1074/jbc.R200003200.
111. Pahl, H.L., Baeuerle, P.A., A novel signal transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-kappa B. EMBO J 14 (1995), 2580–2588 7781611 1:CAS:528:DyaK2MXmsVOjsL0%3D.
112. Panayi, G.S., Corrigall, V.M., BiP, an anti-inflammatory ER protein, is a potential new therapy for the treatment of rheumatoid arthritis. Novartis Found Symp 291 (2008), 212–216 18575276 1:CAS:528:DC%2BD1cXps1Kis7o%3D 10.1002/9780470754030.ch16.
113. Panayi, G.S., Corrigall, V.M., Henderson, B., Stress cytokines: pivotal proteins in immune regulatory networks; opinion. Curr Opin Immunol 16 (2004), 531–534 15245751 1:CAS:528:DC%2BD2cXlsFyrur4%3D 10.1016/j.coi.2004.05.017.
114. Parcellier, A., Schmitt, E., Gurbuxani, S., Seigneurin-Berny, D., Pance, A., Chantôme, A., Plenchette, S., Khochbin, S., Solary, E., Garrido, C., HSP27 is a ubiquitin-binding protein involved in I-kappaBalpha proteasomal degradation. Mol Cell Biol 23 (2003), 5790–5802 12897149 1:CAS:528:DC%2BD3sXmt1SrtLs%3D 10.1128/MCB.23.16.5790-5802.2003.
115. Park, K.J., Gaynor, R.B., Kwak, Y.T., Heat shock protein 27 association with the I kappa B kinase complex regulates tumor necrosis factor alpha-induced NF-kappa B activation. J Biol Chem 278 (2003), 35272–35278 12829720 1:CAS:528:DC%2BD3sXntVWqur8%3D 10.1074/jbc.M305095200.
116. Peetermans, W.E., Raats, C.J., Langermans, J.A., van Furth, R., Mycobacterial heat-shock protein 65 induces proinflammatory cytokines but does not activate human mononuclear phagocytes. Scand J Immunol 39 (1994), 613–617 8009177 1:CAS:528:DyaK2cXltVKgurw%3D 10.1111/j.1365-3083.1994.tb03421.x.
117. Pereira, E.R., Liao, N., Neale, G.A., Hendershot, L.M., Transcriptional and post-transcriptional regulation of proangiogenic factors by the unfolded protein response. PLoS One, 5, 2010, e12521 20824063 10.1371/journal.pone.0012521 1:CAS:528:DC%2BC3cXhtFCksr%2FO.
118. Petho, G., Reeh, P.W., Sensory and signaling mechanisms of bradykinin, eicosanoids, platelet-activating factor, and nitric oxide in peripheral nociceptors. Physiol Rev 92 (2012), 1699–1775 23073630 1:CAS:528:DC%2BC38Xhsl2lsbnE 10.1152/physrev.00048.2010.
119. Piguet, P.F., Grau, G.E., Vesin, C., Loetscher, H., Gentz, R., Lesslauer, W., Evolution of collagen arthritis in mice is arrested by treatment with anti-tumour necrosis factor (TNF) antibody or a recombinant soluble TNF receptor. Immunology 77 (1992), 510–514 1337334 1:CAS:528:DyaK3sXhtVShs7w%3D.
120. Pirot, P., Eizirik, D.L., Cardozo, A.K., Interferon-gamma potentiates endoplasmic reticulum stress-induced death by reducing pancreatic beta cell defence mechanisms. Diabetologia 49 (2006), 1229–1236 16604358 1:CAS:528:DC%2BD28Xktlalu74%3D 10.1007/s00125-006-0214-7.
121. Railson, J.E., Lawrence, K., Buddle, J.C., Pennica, D., Latchman, D.S., Heat shock protein-56 is induced by cardiotrophin-1 and mediates its hypertrophic effect. J Mol Cell Cardiol 33:6 (2001), 1209–1221.
122. Rice, J.W., Veal, J.M., Fadden, R.P., Barabasz, A.F., Partridge, J.M., Barta, T.E., Dubois, L.G., Huang, K.H., Mabbett, S.R., Silinski, M.A., Steed, P.M., Hall, S.E., Small molecule inhibitors of Hsp90 potently affect inflammatory disease pathways and exhibit activity in models of rheumatoid arthritis. Arthritis Rheum 58 (2008), 3765–3775 19035474 1:CAS:528:DC%2BD1MXmt1ymtQ%3D%3D 10.1002/art.24047.
123. Riddell, J.R., Wang, X.Y., Minderman, H., Gollnick, S.O., Peroxiredoxin 1 stimulates secretion of proinflammatory cytokines by binding to TLR4. J Immunol 184 (2010), 1022–1030 20018613 1:CAS:528:DC%2BC3cXhslChsg%3D%3D 10.4049/jimmunol.0901945.
124. Ropeleski, M.J., Tang, J., Walsh-Reitz, M.M., Musch, M.W., Chang, E.B., Interleukin-11-induced heat shock protein 25 confers intestinal epithelial-specific cytoprotection from oxidant stress. Gastroenterology 124:5 (2003), 1358–1368.
125. Rousseau, S., Dolado, I., Beardmore, V., Shpiro, N., Marquez, R., Nebreda, A.R., Arthur, J.S., Case, L.M., Tessier-Lavigne, M., Gaestel, M., Cuenda, A., Cohen, P., CXCL12 and C5a trigger cell migration via a PAK1/2-p38alpha MAPK-MAPKAP-K2-HSP27 pathway. Cell Signal 18 (2006), 1897–1905 16574378 1:CAS:528:DC%2BD28XhtVGjtbbK 10.1016/j.cellsig.2006.02.006.
126. Roussel, B.D., Irving, J.A., Ekeowa, U.I., Belorgey, D., Haq, I., Ordóñez, A., Kruppa, A.J., Duvoix, A., Rashid, S.T., Crowther, D.C., Marciniak, S.J., Lomas, D.A., Unravelling the twists and turns of the serpinopathies. FEBS J 278 (2011), 3859–3867 21624056 1:CAS:528:DC%2BC3MXhtlGks77M 10.1111/j.1742-4658.2011.08201.x.
127. Saini, V., Romero, J., Marchese, A., Majetschak, M., Ubiquitin receptor binding and signaling in primary human leukocytes. Commun Integr Biol 3 (2010), 608–610 21331255 10.4161/cib.3.6.13375.
128. Salminen, A., Paimela, T., Suuronen, T., Kaarniranta, K., Innate immunity meets with cellular stress at the IKK complex: regulation of the IKK complex by HSP70 and HSP90. Immunol Lett 117 (2008), 9–15 18282612 1:CAS:528:DC%2BD1cXjtlWgtro%3D 10.1016/j.imlet.2007.12.017.
129. Sasaki, H., Sato, T., Yamauchi, N., Okamoto, T., Kobayashi, D., Iyama, S., Kato, J., Matsunaga, T., Takimoto, R., Takayama, T., Kogawa, K., Watanabe, N., Niitsu, Y., Induction of heat shock protein 47 synthesis by TGF-beta and IL-1 beta via enhancement of the heat shock element binding activity of heat shock transcription factor 1. J Immunol 168:10 (2002), 5178–5183.
130. Satoh, J., Kim, S.U., Cytokines and growth factors induce HSP27 phosphorylation in human astrocytes. J Neuropathol Exp Neurol 54 (1995), 504–512 7541446 1:CAS:528:DyaK2MXnt1Cgt7s%3D 10.1097/00005072-199507000-00004.
131. Schmidt, J.A., Abdulla, E., Down-regulation of IL-1 beta biosynthesis by inducers of the heat-shock response. J Immunol 141 (1988), 2027–2034 3139749 1:CAS:528:DyaL1cXls1ylurw%3D.
132. Schönthal, A.H., Direct non-cyclooxygenase-2 targets of celecoxib and their potential relevance for cancer therapy. Br J Cancer 97 (2007), 1465–1468 17955049 10.1038/sj.bjc.6604049 1:CAS:528:DC%2BD2sXhtlKmt7jM.
133. Schreck, R., Rieber, P., Baeuerle, P.A., Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1. EMBO J 10 (1991), 2247–2258 2065663 1:CAS:528:DyaK3MXkvVOjurY%3D.
134. Scott-Phillips, T.C., Defining biological communication. J Evol Biol 21 (2008), 387–395 18205776 1:STN:280:DC%2BD1c7htFOisg%3D%3D 10.1111/j.1420-9101.2007.01497.x.
135. Serpier, H., Gillery, P., Salmon-Ehr, V., Garnotel, R., Georges, N., Kalis, B., Maquart, F.X., Antagonistic effects of interferon-gamma and interleukin-4 on fibroblast cultures. J Invest Dermatol 109 (1997), 158–162 9242501 1:CAS:528:DyaK2sXltlKjur4%3D 10.1111/1523-1747.ep12319207.
136. Shapiro, L., Dinarello, C.A., Osmotic regulation of cytokine synthesis in vitro. Proc Natl Acad Sci U S A 92 (1995), 12230–12234 8618875 1:CAS:528:DyaK28Xhtl2gsQ%3D%3D 10.1073/pnas.92.26.12230.
137. Sharma, M., Chemokines and their receptors: orchestrating a fine balance between health and disease. Crit Rev Biotechnol 30 (2010), 1–22 19780653 1:CAS:528:DC%2BC3cXitVOmsrY%3D 10.3109/07388550903187418.
138. Shim, Y.J., Kang, B.H., Choi, B.K., Park, I.S., Min, B.H., Clusterin induces the secretion of TNF-α and the chemotactic migration of macrophages. Biochem Biophys Res Commun 422 (2012), 200–205 22575505 1:CAS:528:DC%2BC38XntFaisbs%3D 10.1016/j.bbrc.2012.04.162.
139. Shimp, S.K. 3rd, Parson, C.D., Regna, N.L., Thomas, A.N., Chafin, C.B., Reilly, C.M., Nichole Rylander, M., HSP90 inhibition by 17-DMAG reduces inflammation in J774 macrophages through suppression of Akt and nuclear factor-κB pathways. Inflamm Res 61 (2012), 521–533 22327510 1:CAS:528:DC%2BC38XlslaisL0%3D 10.1007/s00011-012-0442-x.
140. Singh, I.S., Gupta, A., Nagarsekar, A., Cooper, Z., Manka, C., Hester, L., Benjamin, I.J., He, J.R., Hasday, J.D., Heat shock co-activates interleukin-8 transcription. Am J Respir Cell Mol Biol 39 (2008), 235–242 18367728 1:CAS:528:DC%2BD1cXpsFOntL4%3D 10.1165/rcmb.2007-0294OC.
141. Sironi, M., Breviario, F., Proserpio, P., Biondi, A., Vecchi, A., Van Damme, J., Dejana, E., Mantovani, A., IL-1 stimulates IL-6 production in endothelial cells. J Immunol 142 (1989), 549–553 2783442 1:CAS:528:DyaL1MXntlKmsw%3D%3D.
142. Snyder, Y.M., Guthrie, L., Evans, G.F., Zuckerman, S.H., Transcriptional inhibition of endotoxin-induced monokine synthesis following heat shock in murine peritoneal macrophages. J Leukoc Biol 51 (1992), 181–187 1431555 1:STN:280:DyaK3s%2FlslSlsw%3D%3D.
143. Sonderegger, S., Yap, J., Menkhorst, E., Weston, G., Stanton, P.G., Dimitriadis, E., Interleukin (IL)11 mediates protein secretion and modification in human extravillous trophoblasts. Hum Reprod 26:10 (2011), 2841–2849.
144. Splettstoesser, W.D., Schuff-Werner, P., Oxidative stress in macrophages—“the enemy within”. Micros Res Tech 57 (2002), 441–445 1:CAS:528:DC%2BD38XlslOitLc%3D 10.1002/jemt.10098.
145. Stephanou, A., Amin, V., Isenberg, D.A., Akira, S., Kishimoto, T., Latchman, D.S., Interleukin 6 activates heat-shock protein 90 beta gene expression. Biochem J 321:Pt 1 (1997), 103–106.
146. Stephanou, A., Brar, B., Heads, R., Knight, R.D., Marber, M.S., Pennica, D., Latchman, D.S., Cardiotrophin-1 induces heat shock protein accumulation in cultured cardiac cells and protects them from stressful stimuli. J Mol Cell Cardiol 30 (1998), 849–855 9602434 1:CAS:528:DyaK1cXjtl2it7o%3D 10.1006/jmcc.1998.0651.
147. Tagaya, Y., Maeda, Y., Mitsui, A., Kondo, N., Matsui, H., Hamuro, J., Brown, N., Arai, K., Yokota, T., Wakasugi, H., ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction. EMBO J 8 (1989), 757–764 2785919 1:CAS:528:DyaK3cXlvVWg.
148. Takano, Y., Hiramatsu, N., Okamura, M., Hayakawa, K., Shimada, T., Kasai, A., Yokouchi, M., Shitamura, A., Yao, J., Paton, A.W., Paton, J.C., Kitamura, M., Suppression of cytokine response by GATA inhibitor K-7174 via unfolded protein response. Biochem Biophys Res Commun 360 (2007), 470–475 17604001 1:CAS:528:DC%2BD2sXnslSqurk%3D 10.1016/j.bbrc.2007.06.082.
149. Takenaka, I.M., Hightower, L.E., Transforming growth factor-beta 1 rapidly induces Hsp70 and Hsp90 molecular chaperones in cultured chicken embryo cells. J Cell Physiol 152 (1992), 568–577 1506415 1:CAS:528:DyaK38XlvVyltrg%3D 10.1002/jcp.1041520317.
150. Takii, R., Inouye, S., Fujimoto, M., Nakamura, T., Shinkawa, T., Prakasam, R., Tan, K., Hayashida, N., Ichikawa, H., Hai, T., Nakai, A., Heat shock transcription factor 1 inhibits expression of IL-6 through activating transcription factor 3. J Immunol 184 (2010), 1041–1048 20018623 1:CAS:528:DC%2BC3cXhslChsA%3D%3D 10.4049/jimmunol.0902579.
151. Teshigawara, K., Maeda, M., Nishino, K., Nikaido, T., Uchiyama, T., Tsudo, M., Wano, Y., Yodoi, J., Adult T leukemia cells produce a lymphokine that augments interleukin 2 receptor expression. J Mol Cell Immunol 2 (1985), 17–26 2978223 1:CAS:528:DyaL2MXkt1Squr8%3D.
152. Teshima, S., Rokutan, K., Takahashi, M., Nikawa, T., Kishi, K., Induction of heat shock proteins and their possible roles in macrophages during activation by macrophage colony-stimulating factor. Biochem J 315 (1996), 497–504 8615820 1:CAS:528:DyaK28Xis1emtbk%3D.
153. Tomasovic, S.P., Barta, M., Klostergaard, J., Temporal dependence of hyperthermic augmentation of macrophage-TNF production and tumor cell-TNF sensitization. Int J Hyperthermia 5 (1989), 625–639 2671183 1:CAS:528:DyaL1MXmtFejtLY%3D 10.3109/02656738909140486.
154. Tukaj, S., Kotlarz, A., Jozwik, A., Smolenska, Z., Bryl, E., Witkowski, J.M., Lipinska, B., Hsp40 proteins modulate humoral and cellular immune response in rheumatoid arthritis patients. Cell Stress Chaperones 15 (2010), 555–566 20127215 1:CAS:528:DC%2BC3cXpvV2jtrc%3D 10.1007/s12192-010-0168-z.
155. Turner, M.J., Sowders, D.P., DeLay, M.L., Mohapatra, R., Bai, S., Smith, J.A., Brandewie, J.R., Taurog, J.D., Colbert, R.A., HLA-B27 misfolding in transgenic rats is associated with activation of the unfolded protein response. J Immunol 175 (2005), 2438–2448 16081815 1:CAS:528:DC%2BD2MXntVSqsr8%3D.
156. van de Veerdonk, F.L., Stoeckman, A.K., Wu, G., Boeckermann, A.N., Azam, T., Netea, M.G., Joosten, L.A., van der Meer, J.W., Hao, R., Kalabokis, V., Dinarello, C.A., IL-38 binds to the IL-36 receptor and has biological effects on immune cells similar to IL-36 receptor antagonist. Proc Natl Acad Sci U S A 109 (2012), 3001–3005 22315422 10.1073/pnas.1121534109.
157. van Eden, W., Spiering, R., Broere, F., van der Zee, R., A case of mistaken identity: HSPs are no DAMPs but DAMPERs. Cell Stress Chaperones 17 (2012), 281–292 22139593 10.1007/s12192-011-0311-5.
158. Vanags, D., Williams, B., Johnson, B., Hall, S., Nash, P., Taylor, A., Weiss, J., Feeney, D., Therapeutic efficacy and safety of chaperonin 10 in patients with rheumatoid arthritis: a double-blind randomised trial. Lancet 368 (2006), 855–863 16950363 1:CAS:528:DC%2BD28Xptlyku7Y%3D 10.1016/S0140-6736(06)69210-6.
159. Verhasselt, V., Goldman, M., Willems, F., Oxidative stress up-regulates IL-8 and TNF-alpha synthesis by human dendritic cells. Eur J Immunol 28 (1998), 3886–3890 9842932 1:CAS:528:DyaK1cXnsFKjsb4%3D 10.1002/(SICI)1521-4141(199811)28:11%3C3886::AID-IMMU3886%3E3.0.CO;2-M.
160. Verma, G., Datta, M., IL-1beta induces ER stress in a JNK dependent manner that determines cell death in human pancreatic epithelial MIA PaCa-2 cells. Apoptosis 15:7 (2010), 864–876.
161. Walter, P., Ron, D., The unfolded protein response: from stress pathway to homeostatic regulation. Science 334 (2011), 1081–1086 22116877 1:CAS:528:DC%2BC3MXhsV2mu7jL 10.1126/science.1209038.
162. Wang, W., Zhang, M., Xiao, Z.Z., Sun, L., Cynoglossus semilaevis ISG15: a secreted cytokine-like protein that stimulates antiviral immune response in a LRGG motif-dependent manner. PLoS One, 7, 2012, e44884 23028660 1:CAS:528:DC%2BC38XhsVWlsbrM 10.1371/journal.pone.0044884.
163. Wang, Y., Alam, G.N., Ning, Y., Visioli, F., Dong, Z., Nör, J.E., Polverini, P.J., The unfolded protein response induces the angiogenic switch in human tumor cells through the PERK/ATF4 pathway. Cancer Res 72 (2012), 5396–5406 22915762 1:CAS:528:DC%2BC38XhsFWrs7nI 10.1158/0008-5472.CAN-12-0474.
164. Wax, S., Piecyk, M., Maritim, B., Anderson, P., Geldanamycin inhibits the production of inflammatory cytokines in activated macrophages by reducing the stability and translation of cytokine transcripts. Arthritis Rheum 48 (2003), 541–550 12571865 1:CAS:528:DC%2BD3sXhslKktbo%3D 10.1002/art.10780.
165. Wilson, M., 2008, Blackwell, Oxford.
166. Wilson HM, Barker RN (2013) Cytokines. doi: 10.1002/9780470015902.a0000929.pub3.
167. Wilson, M., Seymour, R., Henderson, B., Bacterial perturbation of cytokine networks. Infect Immun 66 (1998), 2401–2409 9596695 1:CAS:528:DyaK1cXjs1eisb8%3D.
168. Xie, Y., Chen, C., Stevenson, M.A., Auron, P.E., Calderwood, S.K., Heat shock factor 1 represses transcription of the IL-1beta gene through physical interaction with the nuclear factor of interleukin 6. J Biol Chem 277 (2002), 11802–11810 11801594 1:CAS:528:DC%2BD38XivVeksL4%3D 10.1074/jbc.M109296200.
169. Xu, W., Yu, F., Yan, M., Lu, L., Zou, W., Sun, L., Zheng, Z., Liu, X., Geldanamycin, a heat shock protein 90-binding agent, disrupts Stat5 activation in IL-2-stimulated cells. J Cell Physiol 198 (2004), 188–196 14603521 1:CAS:528:DC%2BD3sXpvFCmtLo%3D 10.1002/jcp.10403.
170. Xue, X., Piao, J.H., Nakajima, A., Sakon-Komazawa, S., Kojima, Y., Mori, K., Yagita, H., Okumura, K., Harding, H., Nakano, H., Tumor necrosis factor alpha (TNFalpha) induces the unfolded protein response (UPR) in a reactive oxygen species (ROS)-dependent fashion, and the UPR counteracts ROS accumulation by TNFalpha. J Biol Chem 280 (2005), 33917–33925 16107336 1:CAS:528:DC%2BD2MXhtVKisbnI 10.1074/jbc.M505818200.
171. Yamamura, I., Hirata, H., Hosokawa, N., Nagata, K., Transcriptional activation of the mouse HSP47 gene in mouse osteoblast MC3T3-E1 cells by TGF-beta 1. Biochem Biophys Res Commun 244:1 (1998), 68–74.
172. Yu, A.L., Fuchshofer, R., Birke, M., Kampik, A., Bloemendal, H., Welge-Lüssen, U., Oxidative stress and TGF-beta2 increase heat shock protein 27 expression in human optic nerve head astrocytes. Invest Ophthalmol Vis Sci 49:12 (2008), 5403–5411.
173. Yurchenko, V., Constant, S., Eisenmesser, E., Bukrinsky, M., Cyclophilin-CD147 interactions: a new target for anti-inflammatory therapeutics. Clin Exp Immunol 160 (2010), 305–317 20345978 1:CAS:528:DC%2BC3cXotVaqu7k%3D 10.1111/j.1365-2249.2010.04115.x.
174. + regulatory T cell function via innate TLR2 signalling. J Clin Invest 116 (2006), 2022–2032 16767222 1:CAS:528:DC%2BD28XmvV2lu78%3D 10.1172/JCI28423.
175. Zeng, L., Liu, Y.P., Sha, H., Chen, H., Qi, L., Smith, J.A., XBP-1 couples endoplasmic reticulum stress to augmented IFN-beta induction via a cis-acting enhancer in macrophages. J Immunol 185 (2010), 2324–2330 20660350 1:CAS:528:DC%2BC3cXpslWmsr8%3D 10.4049/jimmunol.0903052.
176. Zeng, L., Lindstrom, M.J., Smith, J.A., Ankylosing spondylitis macrophage production of higher levels of interleukin-23 in response to lipopolysaccharide without induction of a significant unfolded protein response. Arthritis Rheum 63 (2011), 3807–3817 22127699 1:CAS:528:DC%2BC3MXhsFCqs7bE 10.1002/art.30593.
177. Zhang, K., Shen, X., Wu, J., Sakaki, K., Saunders, T., Rutkowski, D.T., Back, S.H., Kaufman, R.J., Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response. Cell 124 (2006), 587–599 16469704 1:CAS:528:DC%2BD28Xhslaqs7Y%3D 10.1016/j.cell.2005.11.040.
178. Zhang, L., Yang, M., Wang, Q., Liu, M., Liang, Q., Zhang, H., Xiao, X., HSF1 regulates expression of G-CSF through the binding element for NF-IL6/CCAAT enhancer binding protein beta. Mol Cell Biochem 352 (2011), 11–17 21455770 1:CAS:528:DC%2BC3MXmtFSlsbw%3D 10.1007/s11010-010-0624-1.
179. Zhao, Y., Huang, Z.J., Rahman, M., Luo, Q., Thorlacius, H., Radicicol, an Hsp90 inhibitor, inhibits intestinal inflammation and leakage in abdominal sepsis. J Surg Res 182 (2013), 312–318 23138048 1:CAS:528:DC%2BC38Xhs1aqtrjP 10.1016/j.jss.2012.10.038.