Mycoplasma fermentans MALP-2 Induces Heme Oxygenase-1 Expression via Mitogen-Activated Protein Kinases and Nrf2 Pathways To Modulate Cyclooxygenase 2 Expression in Human Monocytes

Ma, Xiaotong; You, Xiaoxing; Zeng, Yanhua; He, Jun; Liu, Liangzhuan; Deng, Zhongliang; Jiang, Chao; Wu, Haiying; Zhu, Chen; Yu, Min; Wu, Yimou

doi:10.1128/cvi.00716-12

Cited by 13 publications

(17 citation statements)

References 51 publications

(62 reference statements)

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“…This preferential responsiveness toward MALP-2 could be caused by the high expression of TLR-2 on monocytes [35]. It is known that MALP-2 can induce COX-2 expression in monocytes with ensuing PGE2 production [24,25]. PGE2 is a potent suppressor of NK cell activity [28,29].…”

Section: Discussionmentioning

confidence: 98%

“…In murine models, TLR-2 agonists can enhance NK cell activity indirectly by activating dendritic cells [22,23]. Moreover, the effect of MALP-2 on monocytes/ macrophages has been studied in some detail [12,16,24]. Several molecules are induced in monocytes/macrophages during MALP-2 stimulation, and COX-2 is one of these molecules [24][25][26].…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, the effect of MALP-2 on monocytes/ macrophages has been studied in some detail [12,16,24]. Several molecules are induced in monocytes/macrophages during MALP-2 stimulation, and COX-2 is one of these molecules [24][25][26]. COX-2 is well known as the rate-limiting enzyme for NK cell suppressive PGE2 production [27][28][29].…”

Section: Introductionmentioning

confidence: 99%

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The TLR-2/TLR-6 agonist macrophage-activating lipopeptide-2 augments human NK cell cytotoxicity when PGE2 production by monocytes is inhibited by a COX-2 blocker

Müller

Tufa

Chatterjee

et al. 2015

Cancer Immunol Immunother

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Macrophage-activating lipopeptide-2 (MALP-2) is a potent inducer of proinflammatory cytokine secretion by macrophages, monocytes, and dendritic cells. MALP-2 was reported to be involved in natural killer (NK) cell activation and ensuing tumor rejection. However, the mechanism of MALP-2-mediated NK cell activation remained unclear. Therefore, we studied the effects of MALP-2 on cultured human NK cells. We found that MALP-2 had no direct effect on NK cells. Instead, MALP-2 acted on monocytes and triggered the release of different molecules such as interleukin (IL)-1β, IL-6, IL-10, IL-12, IL-15, interferon gamma-induced protein (IP-10), and prostaglandin (PG)-E2. Our data show that monocyte-derived IP-10 could significantly induce NK cell cytotoxicity as long as the immunosuppression by PGE2 is specifically inhibited by cyclooxygenase (COX)-2 blockade. In summary, our results show that MALP-2-mediated stimulation of monocytes results in the production of several mediators which, depending on the prevailing conditions, affect the activity of NK cells in various ways. Hence, MALP-2 administration with concurrent blocking of COX-2 can be considered as a promising approach in MALP-2-based adjuvant tumor therapies.

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Section: Discussionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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The TLR-2/TLR-6 agonist macrophage-activating lipopeptide-2 augments human NK cell cytotoxicity when PGE2 production by monocytes is inhibited by a COX-2 blocker

Müller

Tufa

Chatterjee

et al. 2015

Cancer Immunol Immunother

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“…The primary antibodies used were rabbit anti-human BMAL1 polyclonal antibody (sc-48790, 1:1000; Santa Cruz Biotechnology, Dallas. TX, USA) 27) , mouse anti-human PER2 monoclonal antibody (sc-377290, 1:1000; Santa Cruz Biotechnology) 28) , mouse anti-human REV-ERBα monoclonal antibody (sc-393215, 1:1000; Santa Cruz Biotechnology) 29) , rabbit anti-human TBP polyclonal antibody (22006-1-AP, 1:2000; Proteintech) 30) , anti-β-actin mouse monoclonal antibody (sc-47778, 1:1000; Santa Cruz Biotechnology) 31) . The immunoreactive signals were visualized with chemiluminescent detection using the AE-9300 Ez-Capture MG (ATTO, Tokyo, Japan).…”

Section: Western Blotting Analysismentioning

confidence: 99%

Role of Circadian Clock Genes in Sudden Cardiac Death: A Pilot Study

Tani

Ikeda

Oritani

et al. 2017

J. Hard Tissue Biology.

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The present study deals with the circadian expression of clock genes in acute cardiac death to examine any correlation between clock gene expression and catecholamines. A total of 36 subjects, who died of acute ischemic heart disease (AIHD, n = 10), acute myocardial infarction (AMI, n = 11), and recurrent myocardial infarction (RMI, n = 15) and underwent autopsy within 2 days after death, were included in this study. The mRNA expression levels of the clock genes BMAL1, PER2, and REV-ERBα were determined in the post-mortem heart tissue. Catecholamine levels in blood obtained from the right heart were measured. Furthermore, the cellular localization of clock proteins was assessed by immunohistochemistry, and protein levels in the heart tissue were also measured by Western blotting. In our cases of AIHD death, BMAL1 and PER2 exhibited trimodal expression patterns; however, the trimodal expression pattern of PER2 was antiphasic to that of BMAL1. PER2 expression correlated with adrenaline and noradrenaline levels. In deaths from AMI, BMAL1 and PER2 exhibited antiphasic trimodal and bimodal expressions, respectively, and BMAL1 expression correlated with adrenaline and noradrenaline levels. In RMI, both BMAL1 and PER2 exhibited antiphasic unimodal expression patterns, which were not correlated with adrenaline and noradrenaline levels. REV-ERBα expression varied, and no correlations were found between dopamine levels and clock gene expression in any group. We concluded that catecholamine levels are decreased in AIHD and raised in AMI as a function of BMAL1 expression and that BMAL1 and PER2 modulate and suppress catecholamine levels respectively.

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“…Within mammalian cells, biliverdin reductase converts biliverdin to bilirubin. Pathogen-associated molecular patterns (PAMPs) such as lipopolysaccharide (LPS), lipoteichoic acid, and peptidoglycan, as well as several proinflammatory cytokines, can induce HO-1 expression (12). Upregulated HO-1 expression can lead to adaptive immune responses that protect cells from immunopathogenesis or stress damage (12,13).…”

mentioning

confidence: 99%

Bacteroides fragilis Enterotoxin Upregulates Heme Oxygenase-1 in Intestinal Epithelial Cells via a Mitogen-Activated Protein Kinase- and NF-κB-Dependent Pathway, Leading to Modulation of Apoptosis

Rho

Jeon

et al. 2016

Infect Immun

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Enterotoxigenic Bacteroides fragilis (ETBF) is associated with noninvasive diarrheal diseases (1, 2), inflammatory bowel diseases (1), and colorectal cancers (3-5). B. fragilis enterotoxin (BFT), a virulence factor of ETBF, is responsible for these diseases (1). BFT interacts with a single layer of intestinal epithelial cells and can provoke signals that induce mucosal inflammation (1, 6-9).In mammalian cells, two genetically distinct isozymes of heme oxygenase (HO) have been clearly identified. HO-1 is inducible, whereas HO-2 is constitutively expressed. HO-1 catalyzes the degradation of free heme into carbon monoxide, biliverdin, and free iron (10, 11). Within mammalian cells, biliverdin reductase converts biliverdin to bilirubin. Pathogen-associated molecular patterns (PAMPs) such as lipopolysaccharide (LPS), lipoteichoic acid, and peptidoglycan, as well as several proinflammatory cytokines, can induce HO-1 expression (12). Upregulated HO-1 expression can lead to adaptive immune responses that protect cells from immunopathogenesis or stress damage (12, 13). In addition, HO-1 expression is involved in clearance of pathogenic bacteria and downregulation of inflammatory responses. For example, HO-1 deficiency not only results in inadequate pathogen clearance (14) but also promotes the development of necrotizing enterocolitis-like intestinal injury in mice (15). HO-1 and HO-1-induced carbon monoxide can ameliorate intestinal inflammation through promotion of bacterial clearance (16). The HO-1/carbon monoxide pathway also suppresses Toll-like receptor 4 (TLR4) signaling, leading to downregulation of proinflammatory signaling induced by stimulation with LPS (17). Based on these findings, we hypothesized that the induction of HO-1 may regulate inflammatory responses induced by BFT. However, there are no reports regarding BFT-induced HO-1 expression.Signals from transcription factors, including nuclear factor-B (NF-B), activator protein-1 (AP-1), and NF-E2-related factor 2 (Nrf2, or nuclear factor [erythroid-derived 2]-like 2 [NFE2L2]), regulate the expression of HO-1 (11). Stimulation of intestinal epithelial cells with BFT can activate NF-B and AP-1 signaling (6)(7)(8)(9)(18)(19)(20). We have previously demonstrated that exposure of intestinal epithelial cells to BFT results in delayed apoptosis, suggesting that protection of cells after BFT stimulation is related to the generation of signals that activate or suppress mucosal inflammation (21). These observations raise the possibility that signaling molecules that regulate HO-1 expression may be activated in BFTexposed cells. However, there is no evidence that BFT-induced signaling results in HO-1 induction in intestinal epithelial cells. We therefore investigated HO-1 induction in response to stimulation of intestinal epithelial cells with BFT. We found that a signaling pathway involving p38 mitogen-activated protein kinases (MAPKs)-IB kinase (IKK)-NF-B in intestinal epithelial cells is required for HO-1 induction following exposure to BFT.

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Mycoplasma fermentans MALP-2 Induces Heme Oxygenase-1 Expression via Mitogen-Activated Protein Kinases and Nrf2 Pathways To Modulate Cyclooxygenase 2 Expression in Human Monocytes

Cited by 13 publications

References 51 publications

The TLR-2/TLR-6 agonist macrophage-activating lipopeptide-2 augments human NK cell cytotoxicity when PGE2 production by monocytes is inhibited by a COX-2 blocker

The TLR-2/TLR-6 agonist macrophage-activating lipopeptide-2 augments human NK cell cytotoxicity when PGE2 production by monocytes is inhibited by a COX-2 blocker

Role of Circadian Clock Genes in Sudden Cardiac Death: A Pilot Study

Bacteroides fragilis Enterotoxin Upregulates Heme Oxygenase-1 in Intestinal Epithelial Cells via a Mitogen-Activated Protein Kinase- and NF-κB-Dependent Pathway, Leading to Modulation of Apoptosis

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