Regulation of innate immune response by MAP kinase phosphatase-1

Wang, Xianxi; Liu, Yusen

doi:10.1016/j.cellsig.2007.03.013

Cited by 138 publications

(125 citation statements)

References 88 publications

(143 reference statements)

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“…The role of p38 MAPK and its isoforms in HCC cell growth have not yet been established. It has been shown that p38 MAPK induces MKP-1, a major negative regulator for ERK (26). This study also showed that phosphorylated HSP27 activated p38 MAPK and subsequently induced phosphorylated MKP-1 (Fig.…”

Section: Discussionsupporting

confidence: 67%

“…This is probably the first report showing such a positive feedback from phosphorylated HSP27 to p38 MAPK. The activation of p38 MAPK is reported to induce MKP-1, a phosphatase that inactivates ERK (26). The effect of phosphorylated HSP27 was analyzed on an active form of MKP-1, phosphorylated MKP-1 (27).…”

Section: Phosphorylated Hsp27 Inhibited Prolonged Activation Of Erk Smentioning

confidence: 99%

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Phosphorylated Heat Shock Protein 27 Represses Growth of Hepatocellular Carcinoma via Inhibition of Extracellular Signal-regulated Kinase

Matsushima‐Nishiwaki

Takai

Adachi

et al. 2008

Journal of Biological Chemistry

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Heat shock protein 27, one of the low molecular weight stress proteins, is recognized as a molecular chaperone; however, other functions have not yet been well established. Phosphorylated heat shock protein 27 levels inversely correlate with the progression of human hepatocellular carcinoma. This study shows that phosphorylated heat shock protein 27 interferes with cell growth of the hepatocellular carcinoma-derived HuH7 cells in the presence of the proinflammatory cytokine, tumor necrosis factor-␣, via inhibition of the sustained activation of the extracellular signal-regulated kinase signal pathway. The activities of Raf/extracellular signal-regulated kinase and subsequent activator protein-1 transactivation and the induction levels of cyclin D1 were lower in HuH7 cells transfected with phosphorylated heat shock protein 27 than those with unphosphorylated heat shock protein 27. Moreover, phosphorylated heat shock protein 27 up-regulated the levels of p38 mitogen-activated protein kinase and mitogen-activated protein kinase phosphatase-1, an inhibitory protein of extracellular signal-regulated kinase. These results indicate that phosphorylated heat shock protein 27 might suppress the extracellular signal-regulated kinase activity in the hepatocellular carcinoma cells via two separate pathways in an inflammatory state. The extracellular signal-regulated kinase activity is inversely correlated with phosphorylated heat shock protein 27 at serine 15 and also in human hepatocellular carcinoma tissues in vivo. Because the extracellular signal-regulated kinase signal pathway is a major proliferation signal of hepatocellular carcinoma, activator protein-1 activation is an early event in hepatocarcinogenesis. These findings strongly suggest that the control of the phosphorylated heat shock protein 27 levels could be a new therapeutic strategy especially to counter the recurrence of hepatocellular carcinoma.The mammalian small stress protein, heat shock protein (HSP) 2 27, is a widely expressed 27-kDa protein, and it is one of 10 members of the human low molecular weight HSP family. HSPs are classified into high molecular weight HSPs such as HSP70 and HSP90, and low molecular weight HSPs with molecular masses from 10 to 30 kDa based on their apparent molecular sizes. Low molecular weight HSPs have significant similarities in terms of amino acid sequences, known as the ␣-crystallin domain and WDPF motif (1, 2). The high molecular weight HSPs act as molecular chaperones in protein folding, oligomerization, and translocation (1). Although the functions of low molecular weight HSPs are not as well characterized as those of the high molecular weight HSPs, it is recognized that they may have chaperone activities (1). The functions of HSP27 are regulated by post-translational modifications such as phosphorylation (3, 4). Mouse HSP27 is phosphorylated at two sites (Ser-15 and Ser-82), whereas human HSP27 is phosphorylated at three sites (Ser-15, Ser-78, and Ser-82) (3). Ser-78 and Ser-82 of HSP27 are adjacent to the amino-termin...

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Section: Discussionsupporting

confidence: 67%

Section: Phosphorylated Hsp27 Inhibited Prolonged Activation Of Erk Smentioning

confidence: 99%

Phosphorylated Heat Shock Protein 27 Represses Growth of Hepatocellular Carcinoma via Inhibition of Extracellular Signal-regulated Kinase

Matsushima‐Nishiwaki

Takai

Adachi

et al. 2008

Journal of Biological Chemistry

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“…It is possible that regulation of SARM by B. pseudomallei may be only partially involved in inhibition of gene expression downstream of the MyD88-independent pathway. Recent evidence demonstrates that SARM directly interacts with TRIF (5); therefore, it is possible that other negative regulators of TLR signaling downstream of TRIF, such as MAP kinase phosphatase 1 (MKP-1) or signal regulatory protein ␣ (SIRP␣), which negatively regulate phosphorylation of p38 and TBK-1, respectively (14,33), may also participate in B. pseudomallei infection. The involvement of these molecules is under investigation by our group.…”

Section: Discussionmentioning

confidence: 99%

Burkholderia pseudomallei-Induced Expression of a Negative Regulator, Sterile-α and Armadillo Motif-Containing Protein, in Mouse Macrophages: a Possible Mechanism for Suppression of the MyD88-Independent Pathway

2011

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Burkholderia pseudomallei, a causative agent of melioidosis, is a Gram-negative facultative intracellular bacterium that can survive and multiply in macrophages. Previously, we demonstrated that B. pseudomallei failed to activate gene expression downstream of the MyD88-independent pathway, particularly the expression of beta interferon (IFN-␤) and inducible nitric oxide synthase (iNOS), leading to the inability of macrophages to kill this bacterium. In the present report, we extended our study to show that B. pseudomallei was able to activate sterile-␣ and Armadillo motif (SARM)-containing protein, a known negative regulator of the MyD88-independent pathway. Both live B. pseudomallei and heat-killed B. pseudomallei were able to upregulate SARM expression in a time-dependent manner in mouse macrophage cell line RAW 264.7. The expression of SARM required bacterial internalization, as it could be inhibited by cytochalasin D. In addition, the intracellular survival of B. pseudomallei was suppressed in SARM-deficient macrophages. Increased expression of IFN-␤ and iNOS and degradation of I B␣ correlated with enhanced macrophage killing capability. These results demonstrated that B. pseudomallei modulated macrophage defense mechanisms by upregulating SARM, thus leading to the suppression of IFN-␤ and iNOS needed for bacterial elimination.

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“…Resting macrophages always express low MKP-1 expression, which allows for inflammatory responses after PAMP stimulation. After PAMP stimulation, MKP-1 mRNA expression increases by 10-100-fold between 15 to 60 min to suppress excessive inflammation (29).…”

Section: Discussionmentioning

confidence: 99%

Mitogen-activated protein kinase phosphatase-1 expression in macrophages is controlled by lymphocytes during macrophage activation

Luo

Yang

Yao³

et al. 2011

Int J Mol Med

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Abstract. The viewpoints on the control of innate immune cells by the adaptive immune system during sepsis remain controversial. Mitogen-activated protein kinase phosphatase-1 (MKP-1) is essential to the negative control of innate immunity and suppresses the activation of macrophages by inhibiting activated mitogen-activated protein kinase (MAPK). The purpose of the current study was to observe inflammatory response and macrophage activation in mice with severe combined immunodeficiency (SCID) with endotoxemia and to determine the role of MKP-1 in the control of macrophage activation by the adaptive immune system. Endotoxemia was induced in wild-type and SCID mice by an intraperitoneal injection of lipopolysaccharide (LPS), and all of the SCID mice died. SCID mice produced more inflammatory cytokines than BALB/c mice systemically and locally. TNF-α mRNA expression was higher and MKP-1 mRNA expression was lower in peritoneal macrophages (PMa) from SCID mice compared to PMa from wild-type mice after and even before LPS injection. Thioglycollate-stimulated PMa from wild-type mice were stimulated with LPS in vitro in the presence or absence of pan-T cells. The levels of TNF-α and IL-6 were higher in the supernatants from PMa cultured alone compared to PMa co-cultured with pan-T cells, and PMa MKP-1 mRNA and protein expression were higher when PMa were co-cultured with pan-T cells. Therefore, pan-T cells can up-regulate MKP-1 expression in macrophages and inhibit the secretion of inflammatory cytokines secretion by macrophages. In SCID mice, lymphocyte deficiency, especially T cell deficiency, causes insufficient MKP-1 expression in macrophages, which can be responsible for the severe inflammation and bad prognosis of septic SCID mice. MKP-1 plays an important role in the control of macrophage activation by the adaptive immune system.

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Regulation of innate immune response by MAP kinase phosphatase-1

Cited by 138 publications

References 88 publications

Phosphorylated Heat Shock Protein 27 Represses Growth of Hepatocellular Carcinoma via Inhibition of Extracellular Signal-regulated Kinase

Phosphorylated Heat Shock Protein 27 Represses Growth of Hepatocellular Carcinoma via Inhibition of Extracellular Signal-regulated Kinase

Burkholderia pseudomallei-Induced Expression of a Negative Regulator, Sterile-α and Armadillo Motif-Containing Protein, in Mouse Macrophages: a Possible Mechanism for Suppression of the MyD88-Independent Pathway

Mitogen-activated protein kinase phosphatase-1 expression in macrophages is controlled by lymphocytes during macrophage activation

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