Regulation of IL-1β-induced GM-CSF production in human airway smooth muscle cells by carbon monoxide

Song, Ruiping; Ning, Wen; Liu, Fang; Ameredes, Bill T.; Calhoun, William J.; Otterbein, Leo E.; Choi, Augustine M.K.

doi:10.1152/ajplung.00212.2002

Cited by 39 publications

(23 citation statements)

References 35 publications

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“…In this respect, our finding that HOCl stimulates the production of CO may be highly relevant, since CO inhibits lipopolysacharide-mediated production of pro-inflammatory cytokines while increasing the synthesis of the anti-inflammatory cytokine, interleukin-10 (35). In addition, CO has an inhibitory action on the formation of granulocyte-macrophage colony stimulating factor, which is known to promote the secretion of proinflammatory mediators and the differentiation of hematopoetic progenitor cells into macrophages and neutrophils (42). Similarly, the HO-1 product biliverdin was recently demonstrated to reduce the severity of the inflammatory response to polymicrobial sepsis by inhibiting the expression of interleukin-6 and stimulating the production of interleukin-10 (40).…”

Section: Discussionmentioning

confidence: 99%

Hypochlorous acid-induced heme oxygenase-1 gene expression promotes human endothelial cell survival

Wei

Liu

Peyton

et al. 2009

American Journal of Physiology-Cell Physiology

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Section: Discussionmentioning

confidence: 99%

Hypochlorous acid-induced heme oxygenase-1 gene expression promotes human endothelial cell survival

Wei

Liu

Peyton

et al. 2009

American Journal of Physiology-Cell Physiology

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“…CO has been shown to inhibit LPS-induced production of proinflammatory cytokines (TNF-a, IL-1b, MIP-1b, and IL-6), and increase production of the anti-inflammatory cytokine, IL-10 (4, 6, 14). CO also has an inhibitory effect on granulocyte-macrophage colony-stimulating factor, which is known to promote the secretion of proinflammatory mediators (4,37) and the differentiation of hematopoetic progenitor cells into macrophages and neutrophils (4). Administration of bilirubin was recently shown to blunt the inflammatory cascade in a model of rodent sepsis by decreasing IL-6 and monocyte chemoattractant protein-1, and increasing IL-10 (38).…”

Section: Discussionmentioning

confidence: 99%

High-Mobility Group Box 1 Contributes to Lethality of Endotoxemia in Heme Oxygenase-1–Deficient Mice

Takamiya

Hung

Hall

et al. 2009

Am J Respir Cell Mol Biol

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High-mobility group box 1 (HMGB1) is a nuclear protein that has been found to be a critical mediator of lethality in endotoxemia and sepsis. During the systemic inflammatory response, circulating levels of HMGB1 are increased, but in a delayed fashion compared with early inflammatory mediators. To counteract the inflammatory response of endotoxemia, a secondary anti-inflammatory response ensues in an attempt to prevent inflammation-induced tissue injury. One such cytoprotective gene that is induced during endotoxemia is heme oxygenase (HO)-1. HO-1, and its products of heme metabolism, possess anti-inflammatory and antioxidant properties to counter the damaging effects of endotoxemia. In the present study, we wanted to determine whether tissue and circulating levels of HMGB1 are increased further in the absence of HO-1 during endotoxemia, and whether this increase may contribute to the pathobiology of endotoxemia. Lung inflammation, HMGB1 protein levels, and expression of HMGB1 in inflammatory cells were increased in HO-1 2/2 mice compared with HO-1 1/1 mice. After the administration of LPS, tissue levels of HMGB1 were not increased further in HO-1 2/2 mice; however, circulating levels of HMGB1 were higher when compared with HO-1 1/1 mice. HO-1 2/2 mice treated with a carbon monoxide-releasing molecule or biliverdin showed a reduction in plasma HMGB1, which was associated with a marked improvement in survival. HO-1 2/2 mice given HMGB1-neutralizing antibody showed improvement in survival compared with control antibody. These data suggest that exaggerated circulating levels of HMGB1 contribute to endotoxin-induced mortality in the absence of HO-1.

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“…CO, one of the byproducts of the HO-1 pathway, has been shown to be anti-inflammatory and cytoprotective in various models of inflammation and tissue injury, including sepsis (4-6), asthma (17,18), chronic graft rejection (19), and ventilator-induced lung injury (20). The signaling pathways and transcription factors involved in CO-mediated anti-inflammatory and cytoprotective effects remain elusive.…”

Section: Discussionmentioning

confidence: 99%

CCAAT/Enhancer-Binding Protein Mediates Carbon Monoxide–Induced Suppression of Cyclooxygenase-2

Suh

Yang

et al. 2006

Am J Respir Cell Mol Biol

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101

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Cyclooxygenase-2 (COX-2) is a key enzyme involved in the inflammatory process that is rapidly induced in macrophages in response to LPS. Carbon monoxide (CO), a byproduct of heme oxygnease-1, can suppress proinflammatory response in various in vitro and in vivo models of inflammation. This study was undertaken to examine whether CO can regulate (and if so, to delineate the mechanism by which CO regulates) LPS-induced COX-2 expression in macrophages. RAW 264.7 murine macrophages were stimulated with LPS (0-10 ng/ml) with or without CO (500 ppm). Northern and Western blot analysis was done. Progstaglandin E 2 and nitrite concentration was measured from cell culture supernatant. Electrophoretic mobility shift assay was performed to assess nuclear factor binding. CO downregulated LPS-induced COX-2 mRNA and protein expression. CO also inhibited LPS-induced prostaglandin E 2 secretion (P Ͻ 0.05). CO also decreased LPS-induced CCAAT/enhancer-binding protein (C/EBP) ␤ and ␦ protein expression in LPS-treated RAW 264.7 cells. Gel shift analysis revealed that CO treatment decreased LPSinduced activation of protein binding to C/EBP consensus oligonucleotides of murine cyclooxygenase-2 promoter. CO also decreased LPS-induced nitric oxide synthase-2 protein expression and nitrite production, and decreased LPS-induced activation of protein binding to C/EBP consensus oligonucleotides of murine nitric oxide synthase-2 promoter. CO may act as an important regulator of inflammation by virtue of its ability to regulate C/EBPs. Keywords: heme oxygenase; lipopolysaccharides; nitric oxide synthase Heme oxygenase-1 (HO-1) is a microsomal enzyme responsible for degradation of heme, generating biliverdin, iron, and carbon monoxide (CO) (1). HO-1 can be induced by a wide variety of stimuli, and the enzyme is involved in cellular and tissue defense against oxidative stress possessing potent anti-inflammatory properties (2, 3). There is growing interest in the role of CO in the anti-inflammatory and cytoprotective function of HO-1 (4-7), but the pathways involved in the anti-inflammatory effect of CO are poorly understood. CO can modulate mitogen-activated protein kinase (5) and guanylate cyclase/3Ј,5Ј-guanylate cyclic monophospate (cGMP) pathway (8) to inhibit secretion of proinflammatory cytokines. CO also modulates several transcription factors, including NF-B (4, 6) and activating protein-1 (4), which are involved in inflammation. But whether other pathways or molecules are involved in the anti-inflammatory effect of CO is not known.

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Regulation of IL-1β-induced GM-CSF production in human airway smooth muscle cells by carbon monoxide

Cited by 39 publications

References 35 publications

Hypochlorous acid-induced heme oxygenase-1 gene expression promotes human endothelial cell survival

Hypochlorous acid-induced heme oxygenase-1 gene expression promotes human endothelial cell survival

High-Mobility Group Box 1 Contributes to Lethality of Endotoxemia in Heme Oxygenase-1–Deficient Mice

CCAAT/Enhancer-Binding Protein Mediates Carbon Monoxide–Induced Suppression of Cyclooxygenase-2

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