MAP kinase phosphatase 1 controls innate immune responses and suppresses endotoxic shock
Open accessAbstract
Septic shock is a leading cause of morbidity and mortality. However, genetic factors predisposing to septic shock are not fully understood. Excessive production of proinflammatory cytokines, particularly tumor necrosis factor (TNF)-alpha, and the resultant severe hypotension play a central role in the pathophysiological process. Mitogen-activated protein (MAP) kinase cascades are crucial in the biosynthesis of proinflammatory cytokines. MAP kinase phosphatase (MKP)-1 is an archetypal member of the dual specificity protein phosphatase family that dephosphorylates MAP kinase. Thus, we hypothesize that knockout of the Mkp-1 gene results in prolonged MAP kinase activation, augmented cytokine production, and increased susceptibility to endotoxic shock. Here, we show that knockout of Mkp-1 substantially sensitizes mice to endotoxic shock induced by lipopolysaccharide (LPS) challenge. We demonstrate that upon LPS challenge, Mkp-1-/- cells exhibit prolonged p38 and c-Jun NH2-terminal kinase activation as well as enhanced TNF-alpha and interleukin (IL)-6 production compared with wild-type cells. After LPS challenge, Mkp-1 knockout mice produce dramatically more TNF-alpha, IL-6, and IL-10 than do wild-type mice. Consequently, Mkp-1 knockout mice develop severe hypotension and multiple organ failure, and exhibit a remarkable increase in mortality. Our studies demonstrate that MKP-1 is a pivotal feedback control regulator of the innate immune responses and plays a critical role in suppressing endotoxin shock.
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GR-mediated transactivation typically induces expression of signaling inhibitors such as IκBα, MPK-1, IL-10, Annexin A1, GILZ, and SOCS proteins, which interfere with immune signaling pathways such as those triggered by Toll-like receptors.
“GR-mediated transactivation typically induces the expression of potent signaling inhibitors (e.g., IκBα, MPK-1, IL-10, Annexin A1, GILZ, and SOCS proteins), which strongly interfere with salient immune signaling pathways such as those triggered by the Toll-like receptors (TLR) (82–85).”
From The HPA – Immune Axis and the Immunomodulatory Actions of Glucocorticoids in the Brain (2014) · cites this paper as [85]
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“Peritoneal macrophages from dusp1-null mice have prolonged phosphorylated p38MAPK and JNK in response to LPS compared with wild-type mice (146).”
Behl, T., Rana, T., Alotaibi, G., Shamsuzzaman, M., Naqvi, M., Sehgal, A., Singh, S., Sharma, N., Almoshari, Y., Abdellatif, A. A. H., et al. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112545 · Cited by 230 · see citing works
Ying, H., Kang, Y., Zhang, H., Zhao, D., Xia, J., Lü, Z., Wang, H., Xu, F., & Shi, L. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1402088 · Cited by 216 · see citing works
“Because the phosphatase Dusp1 has been proposed to negatively regulate JNK activation and have a protective effect on acute lung injury (35, 36), we then investigated the possible involvement of Dusp1 in miR-127 regulatory loop.”
BackgroundWu, J., Flach, R. J. R., Anderson, E. J., Hong, E., Lee, M., Choi, C. S., Neufer, P. D., Shulman, G. I., Kim, J. K., & Bennett, A. M. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.05.010 · Cited by 212 · see citing works
Barbour, M., Plevin, R., & Jiang, H.-R. (2016) · Scientific Reports · doi:10.1038/srep38999 · Cited by 206 · see citing works
Nonreceptor Protein-Tyrosine Phosphatases in Immune Cell Signaling
Pao, L. I., Badour, K., Siminovitch, K., & Neel, B. G. (2007) · Annual Review of Immunology · doi:10.1146/annurev.immunol.23.021704.115647 · Cited by 200 · see citing works
Acetylation of mitogen-activated protein kinase phosphatase-1 inhibits Toll-like receptor signaling
Cao, W., Bao, C., Padalko, E. Y., & Lowenstein, C. J. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20071728 · Cited by 190 · see citing works
Regulatory mechanisms of mitogen-activated kinase signaling
Zhang, Y., & Dong, C. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7012-3 · Cited by 187 · see citing works
Induction of IRAK-M Is Associated with Lipopolysaccharide Tolerance in a Human Endotoxemia Model
Veer, C. V. ′., van den Pangaart, P. S., van Zoelen, M. A. D., de Kruif, M. D., Birjmohun, R. S., Stroes, E. S. G., de Vos, A. F., & van der Poll, T. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.10.7110 · Cited by 176 · see citing works
Restraint of inflammatory signaling by interdependent strata of negative regulatory pathways
Murray, P. J., & Smale, S. T. (2012) · Nature Immunology · doi:10.1038/ni.2391 · Cited by 170 · see citing works
Dual-specificity phosphatase 1: a critical regulator of innate immune responses
Abraham, S., & Clark, A. R. (2006) · Biochemical Society Transactions · doi:10.1042/bst0341018 · Cited by 169 · see citing works
Tiedje, C., Díaz‐Muñoz, M. D., Trulley, P., Ahlfors, H., Laaß, K., Blackshear, P. J., Turner, M., & Gaestel, M. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw474 · Cited by 168 · see citing works
“…feedback inhibitors, such as TTP, dual specificity phosphatase 1 (Dusp1), immediate early response 3 (Ier3) and tumor necrosis factor alpha-induced protein 3 (Tnfaip3 / A20), has been demonstrated by genetic deletions, which led to deregulated inflammatory responses and macrophage death (14–21).”
Shimazu, T., Villena, J., Tohno, M., Fujie, H., Hosoya, S., Shimosato, T., Aso, H., Suda, Y., Kawai, Y., Saito, T., et al. (2011) · Infection and Immunity · doi:10.1128/iai.05729-11 · Cited by 161 · see citing works
“An MKP-1 deficiency leads to hyperresponsiveness to LPS stimulation in innate immune cells (50).”
BackgroundMacrophage Proinflammatory Activation and Deactivation
Valledor, A. F., Comalada, M., Santamaria‐Babí, L. F., Lloberas, J., & Celada, A. (2010) · Advances in immunology · doi:10.1016/b978-0-12-380995-7.00001-x · Cited by 159 · see citing works
Bachstetter, A. D., & Eldik, L. J. V. (2010) · PubMed Central · Cited by 155 · see citing works
Bognar, E., Sárszegi, Z., Szabó, A., Debreceni, B., Kálmán, N., Tucsek, Z., Sümegi, B., & Gallyas, F. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065355 · Cited by 154 · see citing works
“Phosphorylation and thereby activation of the studied MAPKs were increased by LPS, which was attenuated by malvidin (Fig.5).”
BackgroundInfluentialKaminska, B., Mota, M., & Pizzi, M. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.10.026 · Cited by 153 · see citing works
Dual-Specificity Phosphatases in Immunity and Infection: An Update
Lang, R., & Raffi, F. A. M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20112710 · Cited by 153 · see citing works
Kleiman, A., Hübner, S., Parkitna, J. M. R., Neumann, A., Hofer, S., Weigand, M. A., Bauer, M., Schmid, W., Schütz, G., Libert, C., et al. (2012) · The FASEB Journal · doi:10.1096/fj.11-192112 · Cited by 152 · see citing works
“Among the genes that failed to be induced in GRdim cells by GCs, we found some coding for putative anti-inflammatory factors, such as DUSP-1 (26) and krüppel-like factor 2 (KLF2; ref.”
BackgroundResultInfluentialScheiber, J., Chen, B., Milik, M., Sukuru, S. C. K., Bender, A., Mikhailov, D., Whitebread, S., Hamon, J., Azzaoui, K., Urbán, L., et al. (2009) · Journal of Chemical Information and Modeling · doi:10.1021/ci800344p · Cited by 152 · see citing works
The phosphoproteome of toll‐like receptor‐activated macrophages
Weintz, G., Olsen, J. V., Frühauf, K., Niedzielska, M., Amit, I., Jantsch, J., Mages, J., Frech, C., Dölken, L., Mann, M., et al. (2010) · Molecular Systems Biology · doi:10.1038/msb.2010.29 · Cited by 152 · see citing works
“…is brought about by members of the MAPK phosphatase family, for example, by Dual specificity phosphatase 1 (DUSP1), that is induced by LPS in macrophages and prevents excessive cytokine production by deactivating p38 MAPK (Chi et al, 2006; Hammer et al, 2006; Salojin et al, 2006; Zhao et al, 2006).”
MicroRNA-101 targets MAPK phosphatase-1 to regulate the activation of MAPKs in macrophages
Zhu, Q.-Y., Liu, Q., Chen, J.-X., Lan, K., & Ge, B.-X. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000798 · Cited by 137 · see citing works
“MKP-1 expression itself is induced rapidly by stimulation with LPS and other microbial components, leading to feedback control of deactivation of MAPKs (17).”
BackgroundRegulation of innate immune response by MAP kinase phosphatase-1
Wang, X., & Liu, Y. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.03.013 · Cited by 149 · see citing works
Dual-specificity MAP kinase phosphatases in health and disease
Seternes, O. M., Kidger, A. M., & Keyse, S. M. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.09.002 · Cited by 148 · see citing works
TLR4 signaling in effector CD4+ T cells regulates TCR activation and experimental colitis in mice
González-Navajas, J. M., Fine, S., Law, J. K., Datta, S. K., Nguyen, K. P., Yu, M., Corr, M., Katakura, K., Eckmann, L., Lee, J., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci40055 · Cited by 143 · see citing works
“Indeed, glucocorticoids or IL-10 induce MKP-1 expression (37–39), while IFN-γ attenuates it and therefore enhances MAPK activation (40).”
BackgroundMitogen-activated protein kinase phosphatase (MKP)-1 in immunology, physiology, and disease
Wancket, L. M., Frazier, W. J., & Liu, Y. (2011) · Life Sciences · doi:10.1016/j.lfs.2011.11.017 · Cited by 134 · see citing works
“hanced cytokine production (Chi et al., 2006; Hammer et al., 2006; Salojin et al., 2006; Zhao et al., 2006) and increased mortality compared to similarly treated wildtype mice.”
BackgroundResultInfluentialThe negative regulation of Toll‐like receptor and associated pathways
Lang, T., & Mansell, A. S. (2007) · Immunology and Cell Biology · doi:10.1038/sj.icb.7100094 · Cited by 133 · see citing works
Chinenov, Y., & Rogatsky, I. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2007.04.014 · Cited by 133 · see citing works
Role of Dual-Specificity Phosphatase 1 in Glucocorticoid-Driven Anti-inflammatory Responses
Hoppstädter, J., & Ammit, A. J. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01446 · Cited by 131 · see citing works
“In accordance, depletion of DUSP1 led to the excessive release of inflammatory cytokines, such as TNF-α, IL-6, CCL3, and CCL4, and increased LPS-induced mortality (14, 15, 39, 42).”
BackgroundAnnexin-1 Regulates Macrophage IL-6 and TNF via Glucocorticoid-Induced Leucine Zipper
Yang, Y. H., Aeberli, D., Dacumos, A., Xue, J. R., & Morand, E. F. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0804000 · Cited by 130 · see citing works
Shipp, L. E., Lee, J. V., Yu, C.-Y., Pufall, M. A., Zhang, P., Scott, D. K., & Wang, J.-C. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013754 · Cited by 121 · see citing works
“Macrophages isolated from mice lacking DUSP1 gene (Dusp1) have prolonged activation of JNK and p38 MAPK, resulting in overexpression of inflammatory genes [13,14].”
BackgroundButchar, J. P., Cremer, T. J., Clay, C. D., Gavrilin, M. A., Wewers, M. D., Marsh, C. B., Schlesinger, L. S., & Tridandapani, S. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002924 · Cited by 119 · see citing works
“Further, a negative regulator of TLR pathway activity, MKP1 (DUSP1) [48], was increased (Figure 4C), although the 3.69-fold increase with Schu S4 did not reach statistical significance (p = 0.057, Figure 3A).”
BackgroundInfluentialTumour Immunogenicity, Antigen Presentation, and Immunological Barriers in Cancer Immunotherapy
Escors, D. (2014) · New Journal of Science · doi:10.1155/2014/734515 · Cited by 114 · see citing works
“[209] Q.”
BackgroundNardo, D. D., Nardo, C. M. D., Nguyen, T. U., Hamilton, J. A., & Scholz, G. M. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901031 · Cited by 105 · see citing works
“MKP-1 plays a key role in attenuating JNK and p38 MAPK activity following their TLR-mediated activation (51, 52), while MKP-5 appears to selectively target activated JNK (50).”
BackgroundKesarwani, M., Kincaid, Z., Gomaa, A. R., Huber, E., Rohrabaugh, S., Siddiqui, Z., Bouso, M. F., Latif, T., Xu, M., Komurov, K., et al. (2017) · Nature Medicine · doi:10.1038/nm.4310 · Cited by 98 · see citing works
“Likewise, studies from mice lacking Dusp1 revealed that it preferentially targets p38 and JNK 28,45 .”
Selective Roles of MAPKs during the Macrophage Response to IFN-γ
Valledor, A. F., Sànchez‐Tilló, E., Arpa, L., Park, J. M., Caelles, C., Lloberas, J., & Celada, A. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.7.4523 · Cited by 97 · see citing works
“Other macrophage activating agents, such as LPS, induce strong levels of expression of MKP-1 (37) which contribute to attenuate proinflammatory responses mediated by LPS-induced MAPK activation (38, 39).”
BackgroundProtein tyrosine phosphatases: dual‐specificity phosphatases in health and disease
Pulido, R., & van Huijsduijnen, R. H. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06250.x · Cited by 97 · see citing works
The p38 MAPK Pathway in Rheumatoid Arthritis: A Sideways Look
Clark, A. R., & Dean, J. L. (2012) · The Open Rheumatology Journal · doi:10.2174/1874312901206010209 · Cited by 96 · see citing works
“IL-10 may enhance or prolong DUSP1 expression in order to impair p38 MAPK signaling [63], whilst interferon may inhibit DUSP1 expression to enhance p38 MAPK signaling [64].”
BackgroundFürst, R., Schroeder, T., Eilken, H. M., Bubik, M. F., Kiemer, A. K., Stefan Zahler, A., & Vollmar, A. M. (2006) · The FASEB Journal · doi:10.1096/fj.06-6752com · Cited by 95 · see citing works
“Interestingly, recent reports show that MAPK phosphatases are important for the control of innate immune response processes (6, 7).”
BackgroundRole of Dual Specificity Phosphatases in Biological Responses to Glucocorticoids
Clark, A. R., Martins, J. R. S., & Tchen, C. R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r700053200 · Cited by 94 · see citing works
Jeong, Y., Du, R., Zhu, X., Yin, S., Wang, J., Cui, H., Cao, W., & Lowenstein, C. J. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.1013565 · Cited by 93 · see citing works
“MKP-1 null cells exhibited prolonged p38 activation and elevated IL-6 secretion compared with WT cells [18].”
A genome-wide analysis of LPS tolerance in macrophages
Mages, J., Dietrich, H., & Lang, R. (2007) · Immunobiology · doi:10.1016/j.imbio.2007.09.015 · Cited by 93 · see citing works
Frazier, W. J., Wang, X., Wancket, L. M., Li, X., Meng, X., Nelin, L. D., Cato, A. C. B., & Liu, Y. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0804343 · Cited by 93 · see citing works
“coli strain was the source of LPS used in previous studies in our laboratory (22, 23).”
BackgroundMethodInfluentialSignal integration, crosstalk mechanisms and networks in the function of inflammatory cytokines
Schmitz, M. L., Weber, A., Roxlau, T., Gaestel, M., & Kracht, M. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.06.019 · Cited by 92 · see citing works
MAP Kinase Phosphatase-2 Plays a Critical Role in Response to Infection by Leishmania mexicana
Al-Mutairi, M. S., Cadalbert, L. C., McGachy, H. A., Shweash, M., Schroeder, J., Kurnik‐Łucka, M., Sloss, C. M., Bryant, C. E., Alexander, J. K., & Plevin, R. J. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001192 · Cited by 89 · see citing works
“[5] and PAC-1 [6] have been shown to both enhance and reduce LPS mediated cellular responses respectively, whilst MKP-5 is thought to regulate adaptive immunity via effects upon T-cells [7].”
Bruton’s Tyrosine Kinase Is Required for TLR-Induced IL-10 Production
Schmidt, N. W., Thieu, V. T., Mann, B. A., Ahyi, A.-N. N., & Kaplan, M. H. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.10.7203 · Cited by 88 · see citing works
Redox signaling in the pancreas in health and disease
Sastre, J., Pérez, S., Sabater-Orti, L., & Rius‐Pérez, S. (2024) · Physiological Reviews · doi:10.1152/physrev.00044.2023 · Cited by 92 · see citing works
Knockout of Mkp-1 Enhances the Host Inflammatory Responses to Gram-Positive Bacteria
Wang, X., Meng, X., Kuhlman, J. R., Nelin, L. D., Nicol, K. K., English, B. K., & Liu, Y. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.8.5312 · Cited by 87 · see citing works
“We and other laboratories have recently shown that in primary macrophages stimulated with LPS, MKP-1 is the primary phosphatase responsible for the dephosphorylation of p38 and JNK (29, 30, 32).”
BackgroundMethodInfluentialMKP-1 Is Necessary for T Cell Activation and Function
Zhang, Y., Reynolds, J. M., Chang, S. H., Martín‐Orozco, N., Chung, Y., Nurieva, R., & Dong, C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.052472 · Cited by 87 · see citing works
Redox signaling and histone acetylation in acute pancreatitis
Escobar, J., Pereda, J., López‐Rodas, G., & Sastre, J. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.11.009 · Cited by 84 · see citing works
Issa, R., Xie, S., Khorasani, N. M., Sukkar, M. B., Adcock, I. M., Lee, K., & Chung, K. F. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.11.7366 · Cited by 85 · see citing works
“(32) demonstrated that these murine cells produce more TNF- , IL-6, and IL-10 when challenged with LPS compared with wild-type macrophages.”
BackgroundKlebsiella pneumoniae subverts the activation of inflammatory responses in a NOD1-dependent manner
Regueiro, V., Moranta, D., Frank, C. G., Larrarte, E., Margareto, J., March, C., Garmendia, J., & Bengoechea, J. A. (2010) · Cellular Microbiology · doi:10.1111/j.1462-5822.2010.01526.x · Cited by 82 · see citing works
“In vitro and in vivo studies suggest that CYLD and MKP-1 may protect the host from an overwhelming inflammatory response by terminating the activation of NF-kBand MAPKs-dependent signalling pathways respectively (Chi et al., 2006; Zhao et al., 2006; Lim et al., 2007; 2008; Liu et al., 2007).”
BackgroundShah, S., King, E. M., Chandrasekhar, A., & Newton, R. C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.540799 · Cited by 81 · see citing works
“This is consistent with feedback control by DUSP1 for multiple genes (20, 21), including, in A549 cells, CSF2, IL6, IL8, and PTGS2 (40).”
ResultDiversity and specificity of the mitogen-activated protein kinase phosphatase-1 functions
Lawan, A., Shi, H., Gatzke, F., & Bennett, A. M. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1041-2 · Cited by 81 · see citing works
“Using mkp-1 mice as a model system, work form this laboratory [27] along with three others [58– 60], demonstrated that MKP-1 is a negative regulator of MAPK-mediated inflammatory responses in macrophages and dendritic cells.”
BackgroundMethodFeedback control of MKP-1 expression by p38
Hu, J., Chen, T., Zhuang, Z., Kong, L., Yu, M., Liu, Y., Zang, J., & Ge, B. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.07.010 · Cited by 81 · see citing works
Triptolide induces anti-inflammatory cellular responses.
Matta, R., Wang, X., Ge, H., Ray, W., Nelin, L. D., & Liu, Y. (2009) · PubMed Central · Cited by 80 · see citing works
Maier, J. V., Brema, S., Tuckermann, J. P., Herzer, U., Klein, M., Stassen, M., Moorthy, A., & Cato, A. C. B. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0067 · Cited by 80 · see citing works
Yan, J., Meng, X., Wancket, L. M., Lintner, K. E., Nelin, L. D., Chen, B., Francis, K. P., Smith, C. V., Rogers, L. K., & Liu, Y. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1102683 · Cited by 80 · see citing works
“To assess organ pathology, the tissue sections were stained with H&E and examined for histological abnormalities as previously described (30).”
MethodAcetylation of MKP-1 and the Control of Inflammation
Chi, H., & Flavell, R. A. (2008) · Science Signaling · doi:10.1126/scisignal.141pe44 · Cited by 79 · see citing works
“Conversely, proinflammatory stimuli such as interferon γ (IFN-γ) attenuate MKP-1 expression to facilitate their positive effects on MAPK activation (13).”
BackgroundStaples, C. J., Owens, D. M., Maier, J. V., Cato, A. C. B., & Keyse, S. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.117911 · Cited by 78 · see citing works
Medina, E. A., Morris, I. R., & Berton, M. T. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0903790 · Cited by 79 · see citing works
Wei, X., Tang, C., Lu, X., Liu, R., Zhou, M., He, D., Zheng, D., Sun, C., & Wu, Z. (2015) · Oncotarget · doi:10.18632/oncotarget.4089 · Cited by 78 · see citing works
“Moreover, DUSP1 knockout mice produce substantially greater quantities of inflammatory cytokines and have greater mortality from endotoxic shock [14].”
BackgroundKrishnan, G., & Chatterjee, N. (2012) · Glia · doi:10.1002/glia.22380 · Cited by 77 · see citing works
“Earlier studies (Chi et al., 2006; Salojin et al., 2006; Zhao et al., 2006) in other cells have indicated AEA action on the MAPK cascade.”
Background
- Authors
- Zhao, Q., Wang, X., Nelin, L. D., Yao, Y., Matta, R., Manson, M. E., Baliga, R. S., Meng, X., Smith, C. V., Bauer, J. A., Chang, C.-H., & Liu, Y.
- Affiliations
- 1Children's Research Institute, Columbus Children's Hospital, Department of Pediatrics,
- Indiana University Indianapolis (US)
- The Ohio State University (US)
- Venue
- The Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 2005-12-27
- Volume
- 203
- Issue
- 1
- Pages
- 131-140
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC2118076
- OpenAlex
- W2169259339
- Cited by
- 370
- References
- 49
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 5 · 2023: 4 · 2022: 8 · 2021: 11 · 2020: 8 · 2019: 9 · 2018: 6 · 2017: 16 · 2016: 16 · 2015: 29 · 2014: 18 · 2013: 16 · 2012: 37
- FWCI
- 10.33
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Experimental Medicine (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL063067, R01HL063067)
- National Institute of General Medical Sciences (R01GM044263, GM044263)
- National Institute of Allergy and Infectious Diseases (AI045811, R01AI057798, AI057798, R21AI057798, R01AI045811)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Health Sciences › Medicine › Epidemiology › Sepsis Diagnosis and Treatment
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- MAP kinase phosphatase-1, MKP-1, endotoxic shock, septic shock, lipopolysaccharide, innate immunity, p38 MAPK, c-Jun N-terminal kinase, TNF-α, interleukin-6, IL-10, hypotension, multiple organ failure, cytokine production
- MeSH terms
- Animals, Cells, Cultured, Dendritic Cells, Immunity, Innate, Lipopolysaccharides, Mice, Transgenic, Phosphoprotein Phosphatases, Shock, Septic, Spleen, Cytokines, Protein Tyrosine Phosphatases, Macrophages, Peritoneal, Immediate-Early Proteins, Cell Cycle Proteins, Mitogen-Activated Protein Kinases, Mice, Dual Specificity Phosphatase 1, Protein Phosphatase 1
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