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Hamster heme oxygenase 1,HO-1 ELISA Kit, Species Hamster, Sample Type serum, plasma

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[#CSB-E14111Ha] Hamster heme oxygenase 1,HO-1 ELISA Kit, Species Hamster, Sample Type serum, plasma


CSB-E14111Ha | Hamster heme oxygenase 1,HO-1 ELISA Kit, Species Hamster, Sample Type serum, plasma, 96T
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(1) Antioxidant and cytoprotective effects of morin against hydrogen peroxide-induced oxidative stress are associated with the induction of Nrf-2‑mediated HO-1 expression in V79-4 Chinese hamster lung fibroblasts.[TOP]

Pubmed ID :28204816
Publication Date : //
Natural phytochemicals of plant origin, including flavonoids, have been found to be potent antioxidants providing beneficial effects against oxidative stress-related diseases. The present study was carried out to investigate the antioxidant properties of morin, a flavonoid originally isolated from the flowering plants of the Moraceae family. Superoxide dismutase (SOD)‑like activity and 2,2'‑azino‑bis‑(3‑ethylbenzothiazoline‑6‑sulfonic acid) (ABTS•+) radical scavenging activity were determined. We also investigated the cytoprotective effects of morin against hydrogen peroxide (H2O2)‑induced DNA damage and apoptosis in V79‑4 Chinese hamster lung fibroblasts. Our results demonstrated that morin had strong scavenging effects against ABTS•+ radicals with enhanced SOD activity, which varied in a dose-dependent manner. Morin was found to reduce H2O2‑induced intracellular reactive oxygen species generation and nuclear DNA damage, and it recovered cell viability damaged by H2O2 via inhibition of mitochondrial dysfunction‑mediated apoptosis. Notably, the treatment of V79‑4 cells with morin markedly enhanced the expression of heme oxygenase‑1 (HO‑1) but not quinone oxidoreductase-1, which was associated with the increased expression and phosphorylation of nuclear factor-erythroid 2-related factor 2 (Nrf2) and the downregulation of Kelch‑like ECH‑associated protein 1 expression. Based on our findings, we conclude that morin effectively ameliorated oxidative stress‑induced DNA damage through intrinsic free radical scavenging activity and activation of the Nrf2/HO-1 pathway.

Authors : Lee Moon Hee, Cha Hee-Jae, Choi Eun Ok, Han Min Ho, Kim Sung Ok, Kim Gi-Young, Hong Su Hyun, Park Cheol, Moon Sung-Kwon, Jeong Soon-Jeong, Jeong Moon-Jin, Kim Wun-Jae, Choi Yung Hyun,

(2) Effect of 7, 8-dihydroxyflavone on the up-regulation of Nrf2-mediated heme oxygenase-1 expression in hamster lung fibroblasts.[TOP]

Pubmed ID :24610348
Publication Date : //
The cytoprotective mechanism of 7, 8-dihydroxyflavone (DHF) against oxidative stress-induced cell damage with respect to its stimulatory effect on the expression of heme oxygenase-1 (HO-1), a potent antioxidant enzyme, was investigated in the present study. Up-regulation of HO-1 expression by DHF was both dose and time dependent in lung fibroblast V79-4 cells. DHF also increased the protein expression level of the transcription factor nuclear factor erythroid-2-related factor 2 (Nrf2), and induced the translocation of Nrf2 from the cytosol into the nucleus, leading to elevated HO-1 expression. The siNrf2 RNA-transfection attenuated HO-1 expression induced by DHF treatment. In addition, DHF induced the activation of extracellular signal-regulated kinase (ERK), while U0126 (a specific pharmacological inhibitor of ERK kinase) abrogated DHF-activated Nrf2 and HO-1 expression. This suggests that DHF increased the levels of Nrf2 and HO-1 via ERK-dependent pathways. Furthermore, DHF significantly prevented the reduction of cell viability in response to oxidative stress; however, U0126 attenuated the protective effect of DHF. Taken together, these results demonstrate that DHF protected cells from oxidative stress via the activation of an ERK/Nrf2/HO-1 signaling pathway.

Authors : Ryu Min Ju, Kang Kyoung Ah, Piao Mei Jing, Kim Ki Cheon, Zheng Jian, Yao Cheng Wen, Cha Ji Won, Hyun Chang Lim, Chung Ha Sook, Park Jong Cook, Cho Suk Ju, Hyun Jin Won,

(3) PECAM-1-dependent heme oxygenase-1 regulation via an Nrf2-mediated pathway in endothelial cells.[TOP]

Pubmed ID :24500083
Publication Date : //
The antioxidant enzyme heme oxygenase (HO)-1, which catalyses the first and rate-limiting step of heme degradation, has major anti-inflammatory and immunomodulatory effects via its cell-type-specific functions in the endothelium. In the current study, we investigated whether the key endothelial adhesion and signalling receptor PECAM-1 (CD31) might be involved in the regulation of HO-1 gene expression in human endothelial cells (ECs). To this end PECAM-1 expression was down-regulated in human umbilical vein ECs (HUVECs) by an adenoviral vector-based knockdown approach. PECAM-1 knockdown markedly induced HO-1, but not the constitutive HO isoform HO-2. Nuclear translocation of the transcription factor NF-E2-related factor-2 (Nrf2), which is a master regulator of the inducible antioxidant cell response, and intracellular levels of reactive oxygen species (ROS) were increased in PECAM-1-deficient HUVECs, respectively. PECAM-1-dependent HO-1 regulation was also examined in PECAM-1 over-expressing Chinese hamster ovary and murine L-cells. Endogenous HO-1 gene expression and reporter gene activity of transiently transfected luciferase HO-1 promoter constructs with Nrf2 target sequences were decreased in PECAM-1 over-expressing cells. Moreover, a regulatory role of ROS for HO-1 regulation in these cells is demonstrated by studies with the antioxidant N-acetylcysteine and exogenous hydrogenperoxide. Finally, direct interaction of PECAM-1 with a native complex of its binding partner NB1 (CD177) and serine proteinase 3 (PR3) from human neutrophils, markedly induced HO-1 expression in HUVECs. Taken together, we demonstrate a functional link between HO-1 gene expression and PECAM-1 in human ECs, which might play a critical role in the regulation of inflammation.

Authors : Saragih Hendry, Zilian Eva, Jaimes Yarúa, Paine Ananta, Figueiredo Constanca, Eiz-Vesper Britta, Blasczyk Rainer, Larmann Jan, Theilmeier Gregor, Burg-Roderfeld Monika, Andrei-Selmer Luminita-Cornelia, Becker Jan Ulrich, Santoso Sentot, Immenschuh Stephan,

(4) Modulation of Nrf2-dependent gene transcription by bilberry anthocyanins in vivo.[TOP]

Pubmed ID :23349102
Publication Date : //
In a human pilot intervention study (healthy + ileostomy probands), the questions were addressed whether in vivo consumption of an anthocyanin-rich bilberry (Vaccinium myrtillius L.) pomace extract (BE) affects (i) the transcription of Nrf2-dependent genes in peripheral blood mononuclear cells (PBMC), indicative for systemic effects, and (ii) the level of oxidative DNA damage in these cells. In healthy test subjects transcripts of NAD(P)H quinone oxidoreductase 1 (NQO1) were significantly elevated throughout the observation period (1-8 h), whereas transcription of heme oxygenase 1 (HO-1) and Nrf2 was significantly decreased. NQO1 and HO-1 transcription remained unchanged in the ileostomy probands, whereas Nrf2-transcription was suppressed in both groups. Decrease in oxidative DNA damage was observed 2 h after BE consumption again only in healthy subjects. In vitro studies using a reporter gene approach (CHO) and qPCR (HT29) indicate that not the intact anthocyanins/anthocyanidins are the activating constituents but the intestinal degradation product phloroglucinol aldehyde (PGA). Taken together, consumption of anthocyanin-rich BE was found to modulate Nrf2-dependent gene expression in PBMCs indicative for systemic activity. Limitation of the effect to healthy test subjects suggests a role of colonic processes for bioactivity, supported by the results on Nrf2-activating properties of the intestinal anthocyanin degradation product PGA.

Authors : Kropat Christopher, Mueller Dolores, Boettler Ute, Zimmermann Kristin, Heiss Elke H, Dirsch Verena M, Rogoll Dorothee, Melcher Ralph, Richling Elke, Marko Doris,

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(7) Up-regulation of Nrf2-mediated heme oxygenase-1 expression by eckol, a phlorotannin compound, through activation of Erk and PI3K/Akt.[TOP]

Pubmed ID :19931411
Publication Date : //
The aim of the present study was to examine the cytoprotective effect of eckol, a phlorotannin found in Ecklonia cava and to elucidate underlying mechanisms. Heme oxygenase-1 (HO-1) is an important antioxidant enzyme that plays a role in cytoprotection against oxidative stress. Eckol-induced HO-1 expression both at the level of mRNA and protein in Chinese hamster lung fibroblast (V79-4) cells, resulting in increased HO-1 activity. The transcription factor NF-E2-related factor 2 (Nrf2) is a critical regulator of HO-1, achieved by binding to the antioxidant response element (ARE). Eckol treatment resulted in the enhanced level of phosphorylated form, nuclear translocation, ARE-binding, and transcriptional activity of Nrf2. Extracellular regulated kinase (Erk) and phosphatidylinositol 3-kinase (PI3K)/protein kinase B (PKB, Akt) contributed to ARE-driven HO-1 expression. Eckol activated both Erk and Akt, and treatments with U0126 (an Erk kinase inhibitor), LY294002 (a PI3K inhibitor), specific Erk1 siRNA, and Akt siRNA suppressed the eckol-induced activation of Nrf2, resulting in a decrease in HO-1 expression. ZnPP (a HO-1 inhibitor), HO-1 siRNA, and Nrf2 siRNA markedly abolished the cytoprotective effect of eckol against hydrogen peroxide-induced cell damage. Likewise, U0126 and LY294002 inhibited the eckol-induced cytoprotective effect against oxidative cell damage. These studies demonstrate that eckol attenuates oxidative stress by activating Nrf2-mediated HO-1 induction via Erk and PI3K/Akt signaling.

Authors : Kim Ki Cheon, Kang Kyoung Ah, Zhang Rui, Piao Mei Jing, Kim Gi Young, Kang Mi Young, Lee Su Jae, Lee Nam Ho, Surh Young-Joon, Hyun Jin Won,

(8) Neutrophil gelatinase-associated lipocalin induces the expression of heme oxygenase-1 and superoxide dismutase 1, 2.[TOP]

Pubmed ID :19904630
Publication Date : //
Lipocalin-2 (Lcn2, NGAL) is a member of the lipocalin super family with diverse function such as the induction of apoptosis, the suppression of bacterial growth, and modulation of inflammatory response. Much interest has recently been focused on the physiological/pathological role of the lipocalin-2 that is considered to be a novel protective factor against oxidative stress. However, its precise biological roles in this protection are not fully understood. In this report we intended to test the effect of lipocalin-2 on the expression of heme oxygenase ((1, 2)) and superoxide dismutase ((1, 2)) which are two strong antioxidants. NGAL was cloned to pcDNA3.1 plasmid by using genetic engineering method. The recombinant vector was transfected to CHO and HEK293T to establish stable cell expressing NGAL and the expression of HO-1, 2 and SOD(1, 2) were compared with appropriate controls by RT-PCR and western blot. On the other hand, expression of NGAL was suppressed by siRNA transfection in order to study the effect of lipocalin-2 on mentioned genes/proteins. The results showed that the expression of HO-1 and SOD(1, 2) enzymes were higher in cells expressing recombinant lipocalin-2 compared with the control cells. Although the expression of HO-1 was lower in NGAL silencing cells, the expression of SOD(1) and SOD(2) were higher. Our data suggest that NGAL is a potent inducer of HO-1 and somewhat SOD(1) and SOD(2) and it appears that part of antioxidant property of NGAL could be attributed to the induction of HO-1 and SOD(1, 2).

Authors : Bahmani Parisa, Halabian Raheleh, Rouhbakhsh Mehdi, Roushandeh Amaneh Mohammadi, Masroori Nasser, Ebrahimi Majid, Samadikuchaksaraei Ali, Shokrgozar Mohammad Ali, Roudkenar Mehryar Habibi,

(9) Lipocalin 2 regulation by thermal stresses: protective role of Lcn2/NGAL against cold and heat stresses.[TOP]

Pubmed ID :19732769
Publication Date : //
Environmental temperature variations are the most common stresses experienced by a wide range of organisms. Lipocalin 2 (Lcn2/NGAL) is expressed in various normal and pathologic conditions. However, its precise functions have not been fully determined. Here we report the induction of Lcn2 by thermal stresses in vivo, and its role following exposure to cold and heat stresses in vitro. Induction of Lcn2 in liver, heart and kidney was detected by RT-PCR, Western blot and immunohistochemistry following exposure of mice to heat and cold stresses. When CHO and HEK293T cells overexpressing NGAL were exposed to cold stress, cell proliferation was higher compared to controls. Down-regulatrion of NGAL by siRNA in A549 cells resulted in less proliferation when exposed to cold stress compared to control cells. The number of apoptotic cells and expression of pro-apoptotic proteins were lower in the NGAL overexpressing CHO and HEK293T cells, but were higher in the siRNA-transfected A549 cells compared to controls, indicating that NGAL protects cells against cold stress. Following exposure of the cells to heat stress, ectopic expression of NGAL protected cells while addition of exogenous recombinant NGAL to the cell culture medium exacerbated the toxicity of heat stress specially when there was low or no endogenous expression of NGAL. It had a dual effect on apoptosis following heat stress. NGAL also increased the expression of HO-1. Lcn2/NGAL may have the potential to improve cell proliferation and preservation particularly to prevent cold ischemia injury of transplanted organs or for treatment of some cancers by hyperthermia.

Authors : Roudkenar Mehryar Habibi, Halabian Raheleh, Roushandeh Amaneh Mohammadi, Nourani Mohammad Reza, Masroori Nasser, Ebrahimi Majid, Nikogoftar Mahin, Rouhbakhsh Mehdi, Bahmani Parisa, Najafabadi Ali Jahanian, Shokrgozar Mohammad Ali,

(10) Triphlorethol-A induces heme oxygenase-1 via activation of ERK and NF-E2 related factor 2 transcription factor.[TOP]

Pubmed ID :17467702
Publication Date : //
Triphlorethol-A, phlorotannin found in Ecklonia cava, induced heme oxygenase-1 (HO-1) expression at mRNA and protein levels, leading to increased HO-1 activity. Transcription factor NF-E2 related factor 2 (Nrf2) regulates antioxidant response element (ARE) of phase 2 detoxifying and antioxidant enzymes. Triphlorethol-A increased nuclear translocation, ARE binding, and transcriptional activity of Nrf2. Triphlorethol-A exhibited activation of ERK and U0126, inhibitor of ERK kinase, suppressed triphlorethol-A induced activation of Nrf2, finally decreased HO-1 protein level. Taken together, these data suggest that triphlorethol-A augments cellular antioxidant defense capacity through induction of HO-1 via ERK-Nrf2-ARE signaling pathway, thereby protecting cells from oxidative stress.

Authors : Kang Kyoung Ah, Lee Kyoung Hwa, Park Jae Woo, Lee Nam Ho, Na Hye Kyung, Surh Young Joon, You Ho Jin, Chung Myung Hee, Hyun Jin Won,