10
Views
1
CrossRef citations to date
0
Altmetric
REVIEW ARTICLES

Mitogen-activated protein kinase phosphatase-1 and septic shock

&
Pages 66-78 | Published online: 11 Jul 2009

References

  • Angus DC, Linde-Zwirble WT, Lidicker J, Clermont G, Carcillo J, Pinsky MR. Epidemiology of severe sepsis in the United States: analysis of incidence, outcome, and associated costs of care. Crit Care Med 2001; 29: 1303–10
  • Martin GS, Mannino DM, Eaton S, Moss M. The epidemiology of sepsis in the United States from 1979 through 2000. N Engl J Med 2003; 348: 1546–54
  • Wang JE, Dahle MK, Yndestad A, Bauer I, McDonald MC, Aukrust P, et al. Peptidoglycan of Staphylococcus aureus causes inflammation and organ injury in the rat. Crit Care Med 2004; 32: 546–52
  • Centers for Disease Control (CDC). Increase in National Hospital Discharge Survey rates for septicemia—United States, 1979–1987. MMWR Morb Mortal Wkly Rep 1990;39:31–4.
  • Watson RS, Carcillo JA. Scope and epidemiology of pediatric sepsis. Pediatr Crit Care Med 2005; 6: S3–5
  • Watson RS, Carcillo JA, Linde-Zwirble WT, Clermont G, Lidicker J, Angus DC. The epidemiology of severe sepsis in children in the United States. Am J Respir Crit Care Med 2003; 167: 695–701
  • Schrag SJ, Zywicki S, Farley MM, Reingold AL, Harrison LH, Lefkowitz LB, et al. Group B streptococcal disease in the era of intrapartum antibiotic prophylaxis. N Engl J Med 2000; 342: 15–20
  • Pearlman M. Prevention of early-onset group B streptococcal disease in newborns. Obstet Gynecol 2003; 102: 414–5
  • Hoffman JA, Mason EO, Schutze GE, Tan TQ, Barson WJ, Givner LB, et al. Streptococcus pneumoniae infections in the neonate. Pediatrics 2003; 112: 1095–102
  • Cohen J. The immunopathogenesis of sepsis. Nature 2002; 420: 885–91
  • Parrillo JE. Pathogenetic mechanisms of septic shock. N Engl J Med 1993; 328: 1471–7
  • Ceneviva G, Paschall JA, Maffei F, Carcillo JA. Hemodynamic support in fluid-refractory pediatric septic shock. Pediatrics 1998; 102: e19
  • Kumar A, Brar R, Wang P, Dee L, Skorupa G, Khadour F, et al. Role of nitric oxide and cGMP in human septic serum-induced depression of cardiac myocyte contractility. Am J Physiol 1999; 276: R265–76
  • Levi M. Disseminated intravascular coagulation: what's new?. Crit Care Clin 2005; 21: 449–67
  • Beutler B, Kruys V. Lipopolysaccharide signal transduction, regulation of tumor necrosis factor biosynthesis, and signaling by tumor necrosis factor itself. J Cardiovasc Pharmacol 1995; 25(Suppl 2)S1–8
  • Akira S. Mammalian Toll-like receptors. Curr Opin Immunol 2003; 15: 5–11
  • Janeway CAJ, Travers P, Walport M, Shlomchik MJ. Immunobiology: the immune system in health and disease5th ed. Garland Publishing, New York 2001
  • Ono K, Han J. The p38 signal transduction pathway: activation and function. Cell Signal 2000; 12: 1–13
  • Dong C, Davis RJ, Flavell RA. MAP kinases in the immune response. Annu Rev Immunol 2002; 20: 55–72
  • Keyse SM. Protein phosphatases and the regulation of mitogen-activated protein kinase signalling. Curr Opin Cell Biol 2000; 12: 186–92
  • Zhao Q, Wang X, Nelin LD, Yao Y, Matta R, Manson ME, et al. MAP kinase phosphatase 1 controls innate immune responses and suppresses endotoxic shock. J Exp Med 2006; 203: 131–40
  • Hammer M, Mages J, Dietrich H, Servatius A, Howells N, Cato AC, et al. Dual specificity phosphatase 1 (DUSP1) regulates a subset of LPS-induced genes and protects mice from lethal endotoxin shock. J Exp Med 2006; 203: 15–20
  • Salojin KV, Owusu IB, Millerchip KA, Potter M, Platt KA, Oravecz T. Essential role of MAPK phosphatase-1 in the negative control of innate immune responses. J Immunol 2006; 176: 1899–907
  • Chi H, Barry SP, Roth RJ, Wu JJ, Jones EA, Bennett AM, et al. Dynamic regulation of pro- and anti-inflammatory cytokines by MAPK phosphatase 1 (MKP-1) in innate immune responses. Proc Natl Acad Sci U S A 2006; 103: 2274–9
  • Whitmarsh AJ, Davis RJ. Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways. J Mol Med 1996; 74: 589–607
  • Carballo E, Lai WS, Blackshear PJ. Feedback inhibition of macrophage tumor necrosis factor-{alpha} production by tristetraprolin. Science 1998; 281: 1001–5
  • Mahtani KR, Brook M, Dean JL, Sully G, Saklatvala J, Clark AR. Mitogen-activated protein kinase p38 controls the expression and posttranslational modification of tristetraprolin, a regulator of tumor necrosis factor alpha mRNA stability. Mol Cell Biol 2001; 21: 6461–9
  • Stoecklin G, Stubbs T, Kedersha N, Wax S, Rigby WF, Blackwell TK, et al. MK2-induced tristetraprolin:14-3-3 complexes prevent stress granule association and ARE-mRNA decay. EMBO J 2004; 23: 1313–24
  • Lai WS, Parker JS, Grissom SF, Stumpo DJ, Blackshear PJ. Novel mRNA targets for tristetraprolin (TTP) identified by global analysis of stabilized transcripts in TTP-deficient fibroblasts. Mol Cell Biol 2006; 26: 9196–208
  • Lau LF, Nathans D. Identification of a set of genes expressed during the G0/G1 transition of cultured mouse cells. EMBO J 1985; 4: 3145–51
  • Charles CH, Abler AS, Lau LF. cDNA sequence of a growth factor-inducible immediate early gene and characterization of its encoded protein. Oncogene 1992; 7: 187–90
  • Keyse SM, Emslie EA. Oxidative stress and heat shock induce a human gene encoding a protein-tyrosine phosphatase. Nature 1992; 359: 644–7
  • Charles CH, Sun H, Lau LF, Tonks NK. The growth factor-inducible immediate-early gene 3CH134 encodes a protein-tyrosine-phosphatase. Proc Natl Acad Sci U S A 1993; 90: 5292–6
  • Alessi DR, Smythe C, Keyse SM. The human CL100 gene encodes a Tyr/Thr-protein phosphatase which potently and specifically inactivates MAP kinase and suppresses its activation by oncogenic ras in Xenopus oocyte extracts. Oncogene 1993; 8: 2015–20
  • Zheng CF, Guan KL. Dephosphorylation and inactivation of the mitogen-activated protein kinase by a mitogen-induced Thr/Tyr protein phosphatase. J Biol Chem 1993; 268: 16116–9
  • Sun H, Charles CH, Lau LF, Tonks NK. MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell 1993; 75: 487–93
  • Liu Y, Gorospe M, Yang C, Holbrook NJ. Role of mitogen-activated protein kinase phosphatase during the cellular response to genotoxic stress. Inhibition of c-Jun N-terminal kinase activity and AP-1-dependent gene activation. J Biol Chem 1995; 270: 8377–80
  • Raingeaud J, Gupta S, Rogers JS, Dickens M, Han J, Ulevitch RJ, et al. Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J Biol Chem 1995; 270: 7420–6
  • Franklin CC, Kraft AS. Conditional expression of the mitogen-activated protein kinase (MAPK) phosphatase MKP-1 preferentially inhibits p38 MAPK and stress-activated protein kinase in U937 cells. J Biol Chem 1997; 272: 16917–23
  • Laderoute KR, Mendonca HL, Calaoagan JM, Knapp AM, Giaccia AJ, Stork PJ. Mitogen-activated protein kinase phosphatase-1 (MKP-1) expression is induced by low oxygen conditions found in solid tumor microenvironments. A candidate MKP for the inactivation of hypoxia- inducible stress-activated protein kinase/c-Jun N-terminal protein kinase activity. J Biol Chem 1999; 274: 12890–7
  • Brondello JM, Pouyssegur J, McKenzie FR. Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation. Science 1999; 286: 2514–7
  • Sohaskey ML, Ferrell JE, Jr. Activation of p42 mitogen-activated protein kinase (MAPK), but not c-Jun NH(2)-terminal kinase, induces phosphorylation and stabilization of MAPK phosphatase XCL100 in Xenopus oocytes. Mol Biol Cell 2002; 13: 454–68
  • Hutter D, Chen P, Barnes J, Liu Y. Catalytic activation of mitogen-activated protein (MAP) kinase phosphatase-1 by binding to p38 MAP kinase: critical role of the p38 C-terminal domain in its negative regulation. Biochem J 2000; 352: 155–63
  • Slack DN, Seternes OM, Gabrielsen M, Keyse SM. Distinct binding determinants for erk2/p38alpha and jnk map kinases mediate catalytic activation and substrate selectivity of map kinase phosphatase-1. J Biol Chem 2001; 276: 16491–500
  • Stewart AE, Dowd S, Keyse SM, McDonald NQ. Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation. Nat Struct Biol 1999; 6: 174–81
  • Schwan WR, Kugler S, Schuller S, Kopecko DJ, Goebel W. Detection and characterization by differential PCR of host eukaryotic cell genes differentially transcribed following uptake of intracellular bacteria. Infect Immun 1996; 64: 91–9
  • Kugler S, Schuller S, Goebel W. Involvement of MAP-kinases and -phosphatases in uptake and intracellular replication of Listeria monocytogenes in J774 macrophage cells. FEMS Microbiol Lett 1997; 157: 131–6
  • Valledor AF, Xaus J, Comalada M, Soler C, Celada A. Protein kinase C epsilon is required for the induction of mitogen-activated protein kinase phosphatase-1 in lipopolysaccharide-stimulated macrophages. J Immunol 2000; 164: 29–37
  • Chen P, Li J, Barnes J, Kokkonen GC, Lee JC, Liu Y. Restraint of proinflammatory cytokine biosynthesis by mitogen-activated protein kinase phosphatase-1 in lipopolysaccharide-stimulated macrophages. J Immunol 2002; 169: 6408–16
  • Shepherd EG, Zhao Q, Welty SE, Hansen TN, Smith CV, Liu Y. The function of mitogen-activated protein kinase phosphatase-1 in peptidoglycan-stimulated macrophages. J Biol Chem 2004; 279: 54023–31
  • Zhao Q, Shepherd EG, Manson ME, Nelin LD, Sorokin A, Liu Y. The role of mitogen-activated protein kinase phosphatase-1 in the response of alveolar macrophages to lipopolysaccharide: attenuation of proinflammatory cytokine biosynthesis via feedback control of p38. J Biol Chem 2005; 280: 8101–8
  • Howard M, Muchamuel T, Andrade S, Menon S. Interleukin 10 protects mice from lethal endotoxemia. J Exp Med 1993; 177: 1205–8
  • Gerard C, Bruyns C, Marchant A, Abramowicz D, Vandenabeele P, Delvaux A, et al. Interleukin 10 reduces the release of tumor necrosis factor and prevents lethality in experimental endotoxemia. J Exp Med 1993; 177: 547–50
  • Hammer M, Mages J, Dietrich H, Schmitz F, Striebel F, Murray PJ, et al. Control of dual-specificity phosphatase-1 expression in activated macrophages by IL-10. Eur J Immunol 2005; 35: 2991–3001
  • Jacobs D, Glossip D, Xing H, Muslin AJ, Kornfeld K. Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase. Genes Dev 1999; 13: 163–75
  • Swantek JL, Cobb MH, Geppert TD. Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) is required for lipopolysaccharide stimulation of tumor necrosis factor alpha (TNF-alpha) translation: glucocorticoids inhibit TNF-alpha translation by blocking JNK/SAPK. Mol Cell Biol 1997; 17: 6274–82
  • Lasa M, Mahtani KR, Finch A, Brewer G, Saklatvala J, Clark AR. Regulation of cyclooxygenase 2 mRNA stability by the mitogen-activated protein kinase p38 signaling cascade. Mol Cell Biol 2000; 20: 4265–74
  • Lasa M, Brook M, Saklatvala J, Clark AR. Dexamethasone destabilizes cyclooxygenase 2 mRNA by inhibiting mitogen-activated protein kinase p38. Mol Cell Biol 2001; 21: 771–80
  • Lasa M, Abraham SM, Boucheron C, Saklatvala J, Clark AR. Dexamethasone causes sustained expression of mitogen-activated protein kinase (MAPK) phosphatase 1 and phosphatase-mediated inhibition of MAPK p38. Mol Cell Biol 2002; 22: 7802–11
  • Kassel O, Sancono A, Kratzschmar J, Kreft B, Stassen M, Cato AC. Glucocorticoids inhibit MAP kinase via increased expression and decreased degradation of MKP-1. EMBO J 2001; 20: 7108–16
  • Abraham SM, Lawrence T, Kleiman A, Warden P, Medghalchi M, Tuckermann J, et al. Antiinflammatory effects of dexamethasone are partly dependent on induction of dual specificity phosphatase 1. J Exp Med 2006; 203: 1883–9
  • Collart MA, Belin D, Vassalli JD, de Kossodo S, Vassalli P. Gamma interferon enhances macrophage transcription of the tumor necrosis factor/cachectin, interleukin 1, and urokinase genes, which are controlled by short-lived repressors. J Exp Med 1986; 164: 2113–8
  • Gordon S. The macrophage. Bioessays 1995; 17: 977–86
  • Calandra T, Echtenacher B, Roy DL, Pugin J, Metz CN, Hultner L, et al. Protection from septic shock by neutralization of macrophage migration inhibitory factor. Nat Med 2000; 6: 164–70
  • Roger T, David J, Glauser MP, Calandra T. MIF regulates innate immune responses through modulation of Toll-like receptor 4. Nature 2001; 414: 920–4
  • Calandra T, Bernhagen J, Metz CN, Spiegel LA, Bacher M, Donnelly T, et al. MIF as a glucocorticoid-induced modulator of cytokine production. Nature 1995; 377: 68–71
  • Roger T, Chanson AL, Knaup-Reymond M, Calandra T. Macrophage migration inhibitory factor promotes innate immune responses by suppressing glucocorticoid-induced expression of mitogen-activated protein kinase phosphatase-1. Eur J Immunol 2005; 35: 3405–13
  • Volk HD, Reinke P, Krausch D, Zuckermann H, Asadullah K, Muller JM, et al. Monocyte deactivation—rationale for a new therapeutic strategy in sepsis. Intensive Care Med 1996; 22(Suppl 4)S474–81
  • West MA, Heagy W. Endotoxin tolerance: a review. Crit Care Med 2002; 30: S64–73
  • Cross AS. Endotoxin tolerance—current concepts in historical perspective. J Endotoxin Res 2002; 8: 83–98
  • Nimah M, Zhao B, Denenberg AG, Bueno O, Molkentin J, Wong HR, et al. Contribution of MKP-1 regulation of p38 to endotoxin tolerance. Shock 2005; 23: 80–7
  • Docke WD, Randow F, Syrbe U, Krausch D, Asadullah K, Reinke P, et al. Monocyte deactivation in septic patients: restoration by IFN-gamma treatment. Nat Med 1997; 3: 678–81
  • Volk HD, Thieme M, Heym S, Docke WD, Ruppe U, Tausch W, et al. Alterations in function and phenotype of monocytes from patients with septic disease—predictive value and new therapeutic strategies. Behring Inst Mitt 1991; 88: 208–15
  • Muller Kobold AC, Tulleken JE, Zijlstra JG, Sluiter W, Hermans J, Kallenberg CG, et al. Leukocyte activation in sepsis; correlations with disease state and mortality. Intensive Care Med 2000; 26: 883–92
  • Allen ML, Peters MJ, Goldman A, Elliott M, James I, Callard R, et al. Early postoperative monocyte deactivation predicts systemic inflammation and prolonged stay in pediatric cardiac intensive care. Crit Care Med 2002; 30: 1140–5
  • Sanlorenzo L, Zhao B, Spight D, Denenberg AG, Page K, Wong HR, et al. Heat shock inhibition of lipopolysaccharide-mediated tumor necrosis factor expression is associated with nuclear induction of MKP-1 and inhibition of mitogen-activated protein kinase activation. Crit Care Med 2004; 32: 2284–92
  • Wong HR, Dunsmore KE, Page K, Shanley TP. Heat shock-mediated regulation of MKP-1. Am J Physiol Cell Physiol 2005; 289: C1152–8
  • Aneja R, Odoms K, Dunsmore K, Shanley TP, Wong HR. Extracellular heat shock protein-70 induces endotoxin tolerance in THP-1 cells. J Immunol 2006; 177: 7184–92
  • Dehoux MS, Hernot S, Asehnoune K, Boutten A, Paquin S, Lecon-Malas V, et al. Cardiopulmonary bypass decreases cytokine production in lipopolysaccharide-stimulated whole blood cells: roles of interleukin-10 and the extracorporeal circuit. Crit Care Med 2000; 28: 1721–7
  • Allen ML, Hoschtitzky JA, Peters MJ, Elliott M, Goldman A, James I, et al. Interleukin-10 and its role in clinical immunoparalysis following pediatric cardiac surgery. Crit Care Med 2006; 34: 2658–65
  • Fan H, Cook JA. Molecular mechanisms of endotoxin tolerance. J Endotoxin Res 2004; 10: 71–84
  • Nomura F, Akashi S, Sakao Y, Sato S, Kawai T, Matsumoto M, et al. Cutting edge: endotoxin tolerance in mouse peritoneal macrophages correlates with down-regulation of surface toll-like receptor 4 expression. J Immunol 2000; 164: 3476–9

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.