CGS 26303 Upregulates mRNA Expression of Heme Oxygenase-1 in Brain Tissue of Rats Subjected to Experimental Subarachnoid Hemorrhage

2004 ◽  
Vol 44 (Supplement 1) ◽  
pp. S474-S478 ◽  
Author(s):  
Chun-Po Yen ◽  
Shih-Chieh Chen ◽  
Tze-Kan Lin ◽  
Shu-Chuan Wu ◽  
Chao-Yuah Chang ◽  
...  
Keyword(s):  
Subarachnoid Hemorrhage ◽  
Mrna Expression ◽  
Brain Tissue ◽  
Heme Oxygenase ◽  
Heme Oxygenase 1 ◽  
Experimental Subarachnoid Hemorrhage

Heme-oxygenase-1 induction in glia throughout rat brain following experimental subarachnoid hemorrhage

1996 ◽  
Vol 713 (1-2) ◽  
pp. 211-222 ◽  
Author(s):  
Paul Matz ◽  
Christopher Turner ◽  
Philip R. Weinstein ◽  
Stephen M. Massa ◽  
S.Scott Panter ◽  
...  
Keyword(s):  
Subarachnoid Hemorrhage ◽  
Rat Brain ◽  
Heme Oxygenase ◽  
Heme Oxygenase 1 ◽  
Experimental Subarachnoid Hemorrhage

scholarly journals Heme Oxygenase-1 and Ferritin are Increased in Cerebral Arteries after Subarachnoid Hemorrhage in Monkeys

2000 ◽  
Vol 20 (7) ◽  
pp. 1066-1076 ◽  
Author(s):  
Shigeki Ono ◽  
Zhen-Du Zhang ◽  
Linda S. Marton ◽  
Baktiar Yamini ◽  
Emily Windmeyer ◽  
...  
Keyword(s):  
Subarachnoid Hemorrhage ◽  
Brain Tissue ◽  
Heme Oxygenase ◽  
Cerebral Arteries ◽  
Heme Oxygenase 1 ◽  
Messenger Ribonucleic Acid ◽  
Control Side ◽  
Key Factor ◽  
Polymerase Chain ◽  
And Control

Hemoglobin is a key factor in the production of cerebral vasospasm. Metabolism of hemoglobin involves breakdown of heme by heme oxygenase (HO) and sequestration of the released iron in ferritin. We determined whether subarachnoid hemorrhage induces these proteins in cerebral arteries and, if so, in which cells they are produced. Whether the changes correlated with vasospasm also was investigated. Subarachnoid hemorrhage was created in monkeys, and vasospasm was assessed by angiography in cohorts of animals killed 3, 7, or 14 days after the hemorrhage. Ferritin and HO-1 messenger ribonucleic acid (mRNA) and protein were measured by competitive reverse transcription-polymerase chain reaction and Western blotting in hemorrhage-side and control-side cerebral arteries and brain tissue. The location of these proteins was determined by immunohistochemistry. There was significant vasospasm 3 and 7 days but not 14 days after subarachnoid hemorrhage. There were no significant changes in mRNA for HO-1 or ferritin in cerebral arteries or brain tissue at any time. There was a significant increase in HO-1 and ferritin protein in hemorrhage-side compared with control-side cerebral arteries at 3, 7, and 14 days. The increase in HO-1 protein was maximal at 3 days, whereas the increase in ferritin protein was maximal at 7 days. There was no detectable increase in HO-1 or ferritin protein in brain tissue at any time. Immunohistochemistry localized HO-1 protein and ferritin to cells in the adventitia of the arterial wall. We show that subarachnoid hemorrhage is associated with a significant increase in HO-1 and ferritin proteins in cerebral arteries that begins at least as early as 3 days after the hemorrhage and that persists for up to 14 days.

Heme Oxygenase-1 mRNA Expression in Egyptian Patients With Chronic Liver Disease

2012 ◽  
Vol 12 (4) ◽  
pp. 278-285 ◽  
Author(s):  
Sahar Saad El-Din Bessa ◽  
Ehab Mostafa Mohamed Ali ◽  
Abeer El-Sayed Abd El-Wahab ◽  
Sherif Abd El-Monem Nor El-Din
Keyword(s):  
Liver Disease ◽  
Mrna Expression ◽  
Chronic Liver Disease ◽  
Heme Oxygenase ◽  
Chronic Liver ◽  
Heme Oxygenase 1 ◽  
Egyptian Patients

Heme Oxygenase-1 mRNA Expression in Chronic Hepatitis B

2005 ◽  
Vol 100 ◽  
pp. S130
Author(s):  
J. Y. Lee ◽  
M. K. Jang ◽  
J. H. Lee ◽  
H. Y. Kim ◽  
J. Y. Yoo
Keyword(s):  
Chronic Hepatitis ◽  
Hepatitis B ◽  
Mrna Expression ◽  
Chronic Hepatitis B ◽  
Heme Oxygenase ◽  
Heme Oxygenase 1

Heme Oxygenase-1 mRNA Expression in the Lung during Murine Traumatic Shock: Effect of rsPSGL.1g

2002 ◽  
Vol 96 (Sup 2) ◽  
pp. A420
Author(s):  
Alexander G. Minchenko ◽  
Irina L. Opentanova ◽  
Valerie E. Armstead
Keyword(s):  
Mrna Expression ◽  
Heme Oxygenase ◽  
Traumatic Shock ◽  
Heme Oxygenase 1 ◽  
Shock Effect

scholarly journals Adiponectin Inhibits LPS-Induced HMGB1 Release through an AMP Kinase and Heme Oxygenase-1-Dependent Pathway in RAW 264 Macrophage Cells

2016 ◽  
Vol 2016 ◽  
pp. 1-9 ◽  
Author(s):  
Mohamed Elfeky ◽  
Ryuji Kaede ◽  
Yuko Okamatsu-Ogura ◽  
Kazuhiro Kimura
Keyword(s):  
Mrna Expression ◽  
Heme Oxygenase ◽  
High Mobility ◽  
Heme Oxygenase 1 ◽  
Amp Kinase ◽  
High Mobility Group Protein ◽  
Macrophage Cells ◽  
Compound C ◽  
Tlr4 Mrna ◽  
Anti Inflammatory

High mobility group protein B1 (HMGB1) is a late inflammatory mediator that exaggerates septic symptoms. Adiponectin, an adipokine, has potent anti-inflammatory properties. However, possible effects of adiponectin on lipopolysaccharide- (LPS-) induced HMGB1 release are unknown. The aim of this study was to investigate effects of full length adiponectin on HMGB1 release in LPS-stimulated RAW 264 macrophage cells. Treatment of the cells with LPS alone significantly induced HMGB1 release associated with HMGB1 translocation from the nucleus to the cytosol. However, prior treatment with adiponectin suppressed LPS-induced HMGB1 release and translocation. The anti-inflammatory cytokine interleukin- (IL-) 10 similarly suppressed LPS-induced HMGB1 release. Adiponectin treatment decreased toll-like receptor 4 (TLR4) mRNA expression and increased heme oxygenase- (HO-) 1 mRNA expression without inducing IL-10 mRNA, while IL-10 treatment decreased TLR2 and HMGB1 mRNA expression and increased the expression of IL-10 and HO-1 mRNA. Treatment with the HO-1 inhibitor ZnPP completely prevented the suppression of HMGB1 release by adiponectin but only partially inhibited that induced by IL-10. Treatment with compound C, an AMP kinase (AMPK) inhibitor, abolished the increase in HO-1 expression and the suppression of HMGB1 release mediated by adiponectin. In conclusion, our results indicate that adiponectin suppresses HMGB1 release by LPS through an AMPK-mediated and HO-1-dependent IL-10-independent pathway.

scholarly journals Expression of ACE2 in the Intact and Acutely Injured Kidney

Kidney360 ◽  
2021 ◽  
pp. 10.34067/KID.0001562021
Author(s):  
Karl A. Nath ◽  
Raman Deep Singh ◽  
Joseph P. Grande ◽  
Vesna D. Garovic ◽  
Anthony J. Croatt ◽  
...  
Keyword(s):  
Protein Expression ◽  
Mrna Expression ◽  
Heme Oxygenase ◽  
Urinary Tract Obstruction ◽  
Kidney Injury ◽  
Heme Oxygenase 1 ◽  
Renal Tubular Epithelium ◽  
Mrna And Protein Expression ◽  
Intact Kidney ◽  
Renal Tubular

Background. The actions of angiotensin-converting enzyme 2 (ACE2) oppose those of the renin-angiotensin-aldosterone system. Evidence supports ACE2 as a cytoprotectant in some tissues. This study examined ACE2 expression in models of acute kidney injury (AKI). Methods. ACE2 mRNA and protein expression, ACE2 activity, and ACE2 expression by immunofluorescence were assessed following ischemic AKI in mice. Renal ACE2 mRNA expression was evaluated in lipopolysaccharide-induced AKI in wildtype (C57BL/6J) mice, in heme oxygenase-1+/+ and heme oxygenase-1-/- mice, and following unilateral urinary tract obstruction (UUO) in wildtype mice. The effect of sex and age on renal ACE2 protein expression was also assessed. Results. In ischemic AKI, ACE2 mRNA and protein expression and ACE2 activity were reduced as compared with such indices in the intact kidney. In ischemic AKI, ACE2, which, in health, is prominently expressed in the renal tubular epithelium, especially in proximal tubules, exhibited decreased expression in these segments. Decreased ACE2 expression in AKI did not reflect reduced GFR per se as ACE2 mRNA expression was unaltered after UUO. Lipopolysaccharide induced renal ACE2 mRNA expression in wildtype mice, but this effect of lipopolysaccharide did not occur in heme oxygenase-1 deficient mice. In the intact kidney, renal ACE2 protein expression decreased in female mice as compared with male mice, but was unaltered with age. Conclusion. We conclude that renal ACE2 expression is decreased in ischemic AKI, one characterized by markedly reduced GFR and abundant cell death, but is upregulated in lipopolysaccharide-induced AKI; this latter effect requires heme oxygenase-1. Determining the significance of ACE2 expression in models of AKI merits further study. We also suggest that understanding the mechanism underlying ACE2 downregulation in AKI may offer insights relevant to COVID-19: ACE2 is downregulated after ACE2 mediates SARS-CoV-2 cellular entry; such downregulation promotes inflammation in COVID-19; and AKI commonly occurs and determines outcomes in COVID-19.

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