Signaling to heme oxygenase-1 and its anti-inflammatory therapeutic potential

Paine, Ananta; Eiz‐Vesper, Britta; Blasczyk, Rainer; Immenschuh, Stephan

doi:10.1016/j.bcp.2010.07.014

Cited by 641 publications

(527 citation statements)

References 132 publications

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“…In addition, HSPs have been shown to inhibit multiple pro-apoptotic signaling events (Jaattela et al 1998;Beere et al 2000;Pandey et al 2000a, b;Concannon et al 2001Concannon et al , 2003Tsuchiya et al 2003;Stankiewicz et al 2005;Rodina et al 2007;Jiang et al 2009;Evans et al 2010;Pasupuleti et al 2010). HO-1 is a heat shock-inducible protein that lacks intrinsic chaperone activity; however, it inhibits oxidative stress, inflammation, and apoptosis in multiple tissue types (Kirkby and Adin 2006;Ryter et al 2006;Gozzelino et al 2010;Paine et al 2010;Blancou et al 2011). Our data indicate that HO-1 induction confers significant protection against cisplatininduced hair cell death.…”

Section: Discussionmentioning

confidence: 58%

Heat Shock Protein-Mediated Protection Against Cisplatin-Induced Hair Cell Death

Baker

Roy

Brandon

et al. 2014

JARO

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Cisplatin is a highly successful and widely used chemotherapy for the treatment of various solid malignancies in both adult and pediatric patients. Side effects of cisplatin treatment include nephrotoxicity and ototoxicity. Cisplatin ototoxicity results from damage to and death of cells in the inner ear, including sensory hair cells. We showed previously that heat shock inhibits cisplatin-induced hair cell death in whole-organ cultures of utricles from adult mice. Since heat shock protein 70 (HSP70) is the most upregulated HSP in response to heat shock, we investigated the role of HSP70 as a potential protectant against cisplatin-induced hair cell death. Our data using utricles from HSP70 −/− mice indicate that HSP70 is necessary for the protective effect of heat shock against cisplatin-induced hair cell death. In addition, constitutive expression of inducible HSP70 offered modest protection against cisplatin-induced hair cell death. We also examined a second heat-inducible protein, heme oxygenase-1 (HO-1, also called HSP32). HO-1 is an enzyme responsible for the catabolism of free heme. We previously showed that induction of HO-1 using cobalt protoporphyrin IX (CoPPIX) inhibits aminoglycoside-induced hair cell death. Here, we show that HO-1 also offers significant protection against cisplatin-induced hair cell death. HO-1 induction occurred primarily in resident macrophages, with no detectable expression in hair cells or supporting cells. Depletion of macrophages from utricles abolished the protective effect of HO-1 induction. Together, our data indicate that HSP induction protects against cisplatin-induced hair cell death, and they suggest that resident macrophages mediate the protective effect of HO-1 induction.

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Section: Discussionmentioning

confidence: 58%

Heat Shock Protein-Mediated Protection Against Cisplatin-Induced Hair Cell Death

Baker

Roy

Brandon

et al. 2014

JARO

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“…A growing number of studies have shown that HO-1 is a crucial antioxidant enzyme (Ryter and Tyrrell, 2000) and plays a signifi cant role in the regulation of infl ammation (Paine et al, 2010). Further, the anti-infl ammatory effects of various plantderived substances work through the induction of HO-1 (Hsu et al, 2008;Lee et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

“…HO-1, a highly inducible isoform, is Abstract widely known to possess potent anti-infl ammatory properties by reducing the production of pro-infl ammatory cytokine production, or stimulating the production of anti-infl ammatory cytokines, including interleukin-10 (Otterbein et al, 2003;Paine et al, 2010). Additionally, HO-1 over-expression protects against cytotoxicity induced by NO (Son et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Inhibition of Nitric Oxide Production by Ethyl Digallates Isolated from Galla Rhois in RAW 264.7 Macrophages

Park¹,

Hur²,

Lee³

et al. 2011

Biomolecules and Therapeutics

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Galla Rhois and its components are known to possess anti-infl ammatory properties. In the present study, we prepared equilibrium mixture of ethyl m-digallate and ethyl p-digallate isomers (EDG) from Galla Rhois and examined its effect on nitric oxide (NO) production in murine macrophage cell line. Treatment of RAW264.7 macrophages with EDG signifi cantly inhibited NO production and inducible nitric oxide synthase (iNOS) expression stimulated by LPS, as assessed by Western blot and quantitative RT-PCR analyses. We also demonstrated that EDG treatment led to an increase in heme oxygenase-1 (HO-1) mRNA and protein expression. EDG treatment also enhanced expression level of nuclear factor-erythroid 2-related factor 2 (Nrf2) in nucleus, which is critical for transcriptional induction of HO-1. Treatment with SnPP (tin protoporphyrin IX), a selective HO-1 inhibitor, reversed EDG-mediated inhibition of nitrite production, suggesting that HO-1 plays an important role in the suppression of NO production by EDG. Taken together, these results indicate that EDG isolated from Galla Rhois suppresses LPS-stimulated NO production in RAW 264.7 macrophages via HO-1 induction.

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“…It also was recently reported that the HO-1 system provides a therapeutic effect in many experimental pathological conditions (Bonelli et al, 2012;Farombi and Surh, 2006;Luz et al, 2012). In oxidative injury and inflammation conditions, an increase in the synthesis of the HO-1 gene is linked to the transcription factors NFkB, Nrf2, and AP-1 (Paine et al, 2010;Srisook et al, 2005;Surh et al, 2009). Among the transcriptional factors, Nrf2 nuclear translocation requires the activation of several signal transduction pathways, such as mitogen-activated protein kinases (MAPKs), phosphatidylinositol 3-kinase (PI3K) and0 Akt (Martin et al, 2004).…”

Section: Introductionmentioning

confidence: 95%

Acteoside Improves Survival in Cecal Ligation an Puncture-Induced Septic Mice via Blocking of High Mobility Group Box 1 Release

Seo

Pak

et al. 2013

Molecules and Cells

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Acteoside, an active phenylethanoid glycoside, has been used traditionally as an anti-inflammatory agent. The molecular mechanism by which acteoside reduces inflammation was investigated in lipopolysaccharide (LPS)-induced Raw264.7 cells and in a mouse model of cecal ligation and puncture (CLP)-induced sepsis. In vitro, acteoside inhibits high mobility group box 1 (HMGB1) release and iNOS/NO production and induces heme oxygenase-1 (HO-1) expression in a concentration-dependent manner, while HO-1 siRNA antagonizes the inhibition of HMGB1 and NO. The effect of acteoside is inhibited by the p38 mitogen-activated protein kinase (MAPK) inhibitor SB203580 and Nfr2 siRNA, indicating that acteoside induces HO-1 via p38 MAPK and NF-E2-related factor 2 (Nrf2). In vivo, acteoside increases survival and decreases serum and lung HMGB1 levels in CLP-induced sepsis. Overall, these results that acteoside reduces HMGB1 release and may be beneficial for the treatment of sepsis.

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Signaling to heme oxygenase-1 and its anti-inflammatory therapeutic potential

Abstract: ABSTRACT

Cited by 641 publications

References 132 publications

Heat Shock Protein-Mediated Protection Against Cisplatin-Induced Hair Cell Death

Heat Shock Protein-Mediated Protection Against Cisplatin-Induced Hair Cell Death

Inhibition of Nitric Oxide Production by Ethyl Digallates Isolated from Galla Rhois in RAW 264.7 Macrophages

Acteoside Improves Survival in Cecal Ligation an Puncture-Induced Septic Mice via Blocking of High Mobility Group Box 1 Release

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