Up-regulation of heme-binding protein 23 (HBP23) gene expression by lipopolysaccharide is mediated via a nitric oxide-dependent signaling pathway in rat Kupffer cells

Immenschuh, Stephan; Stritzke, Janina; Iwahara, Shin-ichiro; Ramadori, Giuliano

doi:10.1002/hep.510300142

Cited by 43 publications

(29 citation statements)

References 60 publications

(68 reference statements)

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“…An effect of cytokines (IFN-γ) on expression of peroxiredoxins has been shown only in rat Kupffer cells [37]. We show that cytokines up-regulate Prxs in INS-1 cells as well as in isolated pancreatic islets.…”

Section: Discussionmentioning

confidence: 70%

“…An influence of substances, which directly release nitric oxide on peroxiredoxin expression has already been reported. A dose-dependent increase of peroxiredoxin I mRNA amount in rat Kupffer cells were found after exposure to both the nitric oxide (NO)-donor SNAP and the peroxynitrite donor SIN-1 [37].…”

Section: Discussionmentioning

confidence: 99%

“…Prx I is a physiological inhibitor of cAbl kinase activity [34]. It is induced by oxidative stress in peritoneal macrophages exposed to heavy metals, oxidized low-density lipoproteins or heme [30,35,36,37].…”

mentioning

confidence: 99%

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Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

et al. 2002

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Aims/hypothesis. Insulin-producing beta cells are destroyed by oxidative and nitrosative stress during the pathogenesis of Type I (insulin-dependent) diabetes mellitus. These cells are more sensitive than others due to their deficiency of well known antioxidant enzymes like superoxide dismutase, glutathione peroxidase and catalase. However the peroxiredoxins discovered in the past decade form a large family of highly conserved thioredoxin-dependent peroxide reductases, which are present in most tissues. We investigated whether peroxiredoxins I and II are present in pancreatic beta cells and if they are inducible by oxidative and nitrosative stress. Methods. To detect these enzymes in insulin-producing beta cells we used semiquantitative RT-PCR, western blots and immunohistochemistry. The expression of peroxiredoxins I and II was analysed after treatment with cytokines, hydrogen peroxide, alloxan or streptozotocin in the rat insulinoma cells INS-1 using RT-PCR and western blots. Results. We show that peroxiredoxins I and II are present in the cytoplasm of pancreatic islet cells as well as in insulinoma cell lines βTC6-F7 and INS-1. Peroxiredoxins I and II were up-regulated by all stress agents used. Conclusion/interpretation. Beta cells, undersupplied with well characterized antioxidant enzymes, possess an additional antioxidant system which is inducible by oxidative as well as nitrosative stress. [Diabetologia (2002) 45:867-876]

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Section: Discussionmentioning

confidence: 70%

Section: Discussionmentioning

confidence: 99%

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Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

et al. 2002

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“…Comparable results were obtained in mice liver (Rizzardini et al 1993), rat Kuppfer cells (Immenschuh et al 1999), macrophages (Srisook & Cha 2004), and rat glial cells (Kitamura et al 1998). As was also demonstrated in other tissues or cell types, the induction of this enzymatic activity is probably involved in the development of cytoprotective mechanisms triggered by both injury and infection (Ryter & Tyrrell 2000).…”

Section: Discussionmentioning

confidence: 71%

“…Many reports have previously indicated that NO donors increase HO activity and induce the expression of HO-1 in different cell types (Otterbein & Choi 2000). In this sense, (Immenschuh et al 1999) have shown that HO-1 induction by LPS is mediated by NO. The attenuation of HO activity by NOS inhibitors has also been demonstrated both in vitro and in vivo models (Datta & Lianos 1999, Datta et al 2002.…”

Section: Discussionmentioning

confidence: 92%

Induction of nitric oxide synthase and heme oxygenase activities by endotoxin in the rat adrenal cortex: involvement of both signaling systems in the modulation of ACTH-dependent steroid production

Grion¹,

Repetto²,

Pomeraniec³

et al. 2007

Journal of Endocrinology

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The present study was designed to investigate the effect of lipopolysaccharide (LPS) on the expression levels and activities of the nitric oxide synthase (NOS) and heme oxygenase (HO) systems in the rat adrenal gland. Both enzymatic activities were significantly increased in this tissue after in vivo treatment with LPS. The concurrent induction of the HO-1, NOS-1, and NOS-2 gene products was also detected as both mRNAs and protein levels were augmented by this treatment in a time-dependent way. A significant interaction between both signaling systems was also demonstrated as in vivo blockage of NOS activity with N(G)-nitro-L-arginine methyl ester (L-NAME) resulted in a significant reduction in HO expression and activity levels, while an increase in NOS activity was observed when HO was inhibited by Sn-protoporphyrin IX (Sn-PPIX). As both NOS and HO activities have been previously involved in the modulation of adrenal steroidogenesis, we investigated the participation of these signaling systems in the adrenal response to LPS. Our results showed that acute stimulation of steroid production by ACTH was significantly increased when either NOS or HO activities were inhibited. We conclude that adrenal NOS and HO can be induced by a non-lethal dose of endotoxin supporting a modulatory role for these activities in the adrenal response to immune challenges.

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Nitric oxide and prostaglandin E₂ participate in lipopolysaccharide/interferon‐γ‐induced heme oxygenase 1 and prevent RAW264.7 macrophages from UV‐irradiation‐induced cell death

Chen

Shen

Lee

et al. 2002

J of Cellular Biochemistry

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Induction of heme oxygenase (HO)-1 during inflammation has been demonstrated in many cell types, but the contribution of inflammatory molecules nitric oxide (NO) and prostaglandin E(2) (PGE(2)) has remained unresolved. Here we show that NO donors including sodium nitroprusside (SNP) and spermine nonoate (SP-NO), and PGE(2) significantly stimulate HO-1 expression in RAW264.7 macrophages, associated with alternative induction on NO and PGE(2) in medium, respectively. NO donors also show the inductive effect on cyclo-oxygenase 2 protein and PGE(2) production. In the presence of lipopolysaccharide and interferon-gamma (LPS/IFN-gamma), HO-1 protein was induced slightly but significantly, and SNP, SP-NO, and PGE(2) enhanced HO-1 protein induced by LPS/IFN-gamma. L-Arginine analogs N-nitro-L-arginine methyl ester (L-NAME) and N-nitro-L-arginine (NLA) significantly block HO-1 protein induced by LPS/IFN-gamma associated with a decrease in NO (not PGE(2)) production. And, NSAIDs aspirin and diclofenase dose dependently inhibited LPS/IFN-gamma-induced HO-1 protein accompanied by suppression of PGE(2) (not NO) production. PD98059 (a specific inhibitor of MEKK), but not SB203580 (a specific inhibitor of p38 kinase), attenuated PGE(2) (not SP-NO) induced HO-1 protein. Under UVC (100 J/m(2)) and UVB (50 J/m(2)) irradiation, PGE(2) or SP-NO treatment prevents cells from UVC or UVB-induced cell death, and HO-1 inhibitor tin protoporphyrin (SnPP) reverses the preventive effects of PGE(2) and SP-NO. The protective activity induced by PGE(2) on UVC or UVB irradiation-induced cell death was blocked by MAPK inhibitor PD98059 (not SB203580). These results demonstrated that inflammatory molecules NO and PGE(2) were potent inducers of HO-1 gene, and protected cells from UV-irradiation-induced cell death through HO-1 induction.

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Up-regulation of heme-binding protein 23 (HBP23) gene expression by lipopolysaccharide is mediated via a nitric oxide-dependent signaling pathway in rat Kupffer cells

Cited by 43 publications

References 60 publications

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

Induction of nitric oxide synthase and heme oxygenase activities by endotoxin in the rat adrenal cortex: involvement of both signaling systems in the modulation of ACTH-dependent steroid production

Nitric oxide and prostaglandin E₂ participate in lipopolysaccharide/interferon‐γ‐induced heme oxygenase 1 and prevent RAW264.7 macrophages from UV‐irradiation‐induced cell death

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Up-regulation of heme-binding protein 23 (HBP23) gene expression by lipopolysaccharide is mediated via a nitric oxide-dependent signaling pathway in rat Kupffer cells

Cited by 43 publications

References 60 publications

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

Induction of nitric oxide synthase and heme oxygenase activities by endotoxin in the rat adrenal cortex: involvement of both signaling systems in the modulation of ACTH-dependent steroid production

Nitric oxide and prostaglandin E2 participate in lipopolysaccharide/interferon‐γ‐induced heme oxygenase 1 and prevent RAW264.7 macrophages from UV‐irradiation‐induced cell death

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Nitric oxide and prostaglandin E₂ participate in lipopolysaccharide/interferon‐γ‐induced heme oxygenase 1 and prevent RAW264.7 macrophages from UV‐irradiation‐induced cell death