Expression of the antioxidant stress protein heme oxygenase-1 (HO-1) in human leukocytes

1999 ◽  
Vol 26 (1-2) ◽  
pp. 184-192 ◽  
Author(s):  
Andreas Michael Niess ◽  
Frank Passek ◽  
Ingrid Lorenz ◽  
Elisabeth Marion Schneider ◽  
Hans-Hermann Dickhuth ◽  
...  
Keyword(s):  
Heme Oxygenase ◽  
Stress Protein ◽  
Heme Oxygenase 1 ◽  
Human Leukocytes ◽  
Antioxidant Stress

Induction of HSP 32 gene in hypoxic cardiomyocytes is attenuated by treatment withN-acetyl-l-cysteine

1998 ◽  
Vol 274 (3) ◽  
pp. H965-H973 ◽  
Author(s):  
D. R. Borger ◽  
D. A. Essig
Keyword(s):  
Heme Oxygenase ◽  
Stress Proteins ◽  
Stress Protein ◽  
Heme Oxygenase 1 ◽  
Low Oxygen ◽  
Neonatal Cardiomyocytes ◽  
Ambient Oxygen ◽  
Mrna Content ◽  
Mrna And Protein Expression ◽  
Heat Stress Protein

Increased synthesis of stress proteins may enhance myocardial viability during periods of low oxygen delivery. Our purpose was to determine if the oxidative stress protein heme oxygenase-1 [heat stress protein 32 (HSP 32)] was induced in hypoxic cardiomyocytes and whether this induction might be mediated by a redox-sensitive mechanism. Primary rat neonatal cardiomyocytes, cultured to express a tissuelike phenotype, responded to 12 h of hypoxia (<0.5% ambient oxygen) with an approximately fivefold (range 3- to 7.5-fold; P < 0.05) increase in HSP 32 mRNA and a threefold ( P < 0.05) increase in HSP 32 protein content. Exposure to 80 μM H2O2for 3 h increased HSP 32 mRNA content to a similar extent. Expression of heme oxygenase-2 mRNA was unaffected by H2O2or hypoxic treatments. Inclusion of 20 mM N-acetyl-l-cysteine in the medium during hypoxia reduced the increase in HSP 32 mRNA and protein expression by 25–50% compared with hypoxia alone. The data suggest that induction of HSP 32 protein may lead to an improved antioxidant defense in cardiomyocytes during hypoxia and that a redox-sensitive pathway mediates at least a portion of the hypoxic induction of the HSP 32gene.

Heme oxygenase-1 mediates the anti-inflammatory actions of 2′-hydroxychalcone in RAW 264.7 murine macrophages

2006 ◽  
Vol 290 (4) ◽  
pp. C1092-C1099 ◽  
Author(s):  
Hadil Abuarqoub ◽  
Roberta Foresti ◽  
Colin J. Green ◽  
Roberto Motterlini
Keyword(s):  
Heme Oxygenase ◽  
Stress Protein ◽  
Protoporphyrin Ix ◽  
Heme Oxygenase 1 ◽  
Raw 264.7 ◽  
Oxygenase Activity ◽  
Tnf Α ◽  
Anti Inflammatory ◽  
Oxide Synthase ◽  
Interfering Rna

Chalcones are a group of plant-derived polyphenolic compounds that belong to the flavonoids family, and possess a wide variety of cytoprotective and modulatory functions. Chalcones exert their cytoprotective actions via activation of specific transcriptional factors and upregulation of endogenous defensive pathways, such as phase II enzymes and the stress protein heme oxygenase-1 (HO-1). In this study, we investigated the anti-inflammatory action of 2′-hydroxychalcone (2-HC) in a model of lipopolysaccharide (LPS)-induced inflammation in RAW 264.7 macrophages and examined the role of HO-1 in this process. Our results demonstrate that 2-HC potently induces HO-1 expression and markedly reduces LPS-mediated nitrite and TNF-α production. These effects are accompanied by inhibition of inducible nitric oxide synthase protein expression and abolished by blockade of heme oxygenase activity with either tin protoporphyrin IX or HO-1 small interfering RNA. By using a pharmacological approach and siRNA technology, we also found that phosphatidylinositol 3-kinase is a major cellular mediator in 2-HC-induced HO-1 expression. These findings strongly suggest that 2-HC exerts anti-inflammatory actions via activation of the HO-1 pathway and help to elucidate the mechanisms underlying the potential therapeutic value of chalcones.

scholarly journals Ozonation of Human Blood Induces a Remarkable Upregulation of Heme Oxygenase-1 and Heat Stress Protein-70

2007 ◽  
Vol 2007 ◽  
pp. 1-6 ◽  
Author(s):  
Velio Bocci ◽  
Carlo Aldinucci ◽  
Francesca Mosci ◽  
Fabio Carraro ◽  
Giuseppe Valacchi
Keyword(s):  
Human Plasma ◽  
Heme Oxygenase ◽  
Vascular Endothelial Cells ◽  
Stress Protein ◽  
Heme Oxygenase 1 ◽  
Immune Reactivity ◽  
Vascular Endothelial ◽  
Hsp 70 ◽  
Heat Stress Protein ◽  
Dose Dependent

Heme oxygenase-I (HO-1) has emerged as one of the most protective enzymes and its pleiotropic activities have been demonstrated in a variety of human pathologies. Unpublished observations have shown that HO-1 is induced after the infusion of ozonated blood into the respective donors, and many other experimental observations have demonstrated the efficacy of oxidizing agents. It appeared worthwhile to evaluate whether we could better define the activity of potential inducers such as hydrogen peroxide and ozonated human plasma. Human vascular endothelial cells at confluence were challenged with different concentrations of these inducers and the simultaneous production of nitric oxide (NO); and HO-1 was measured by either measuring nitrite, or bilirubin formation, or/and the immune reactivity of the protein by Western blot using a rabbit antihuman HO-1 and Hsp-70. The results show that production of both NO and HO-1 is fairly dose dependent but is particularly elevated using human plasma after transient exposure to a medium ozone concentration. At this concentration, there is also induction of Hsp-70. The results clarify another positive effect achievable by the use of ozone therapy.

A Precursor of the Nitric Oxide Donor SIN-1 Modulates the Stress Protein Heme Oxygenase-1 in Rat Liver

1996 ◽  
Vol 225 (1) ◽  
pp. 167-172 ◽  
Author(s):  
Roberto Motterlini ◽  
Ana Hidalgo ◽  
Ivan Sammut ◽  
Ketan A. Shah ◽  
Saleem Mohammed ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Heme Oxygenase ◽  
Rat Liver ◽  
Stress Protein ◽  
Nitric Oxide Donor ◽  
Heme Oxygenase 1
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