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Catalytic inactive heme oxygenase-1 protein regulates its own expression in oxidative stress.

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TLDR
Feed-forward autoregulation of HO-1 in oxidative stress is documented and it is suggested thatHO-1 protein has a role in the induction process and may also serve to up-regulate other genes to promote cytoprotection and to modulate cell proliferation.
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This article is published in Free Radical Biology and Medicine.The article was published on 2008-03-01 and is currently open access. It has received 67 citations till now. The article focuses on the topics: Heme oxygenase & Heme.

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Journal ArticleDOI

Heme oxygenase-1, oxidation, inflammation, and atherosclerosis.

TL;DR: Findings suggest that a potential intervention on HO-1 or its byproducts may need to take into account any potential alteration in the status of Nrf2 activation, as well as the potential pathways and mechanisms mediating vascular protection.
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Heme oxygenase-1 and neurodegeneration: expanding frontiers of engagement.

TL;DR: In ‘stressed’ astroglia, HO‐1 hyperactivity promotes mitochondrial sequestration of non‐transferrin iron and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergetic failure amply documented in Alzheimer disease, Parkinson disease and other aging‐related neurodegenerative disorders.
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Insight into oxidative stress in varicocele-associated male infertility: part 1

TL;DR: Measurement of the reactive oxygen species and other markers of oxidative stress, including the levels of the antioxidant enzymes catalase and superoxide dismutase, can provide valuable information on the extent of oxidative Stress and might guide therapeutic management strategies.
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Nuclear Heme Oxygenase-1 (HO-1) Modulates Subcellular Distribution and Activation of Nrf2, Impacting Metabolic and Anti-oxidant Defenses

TL;DR: In oxidative stress, nuclear HO-1 interacts with Nrf2 and stabilizes it from glycogen synthase kinase 3β (GSK3β)-mediated phosphorylation coupled with ubiquitin-proteasomal degradation, thereby prolonging its accumulation in the nucleus.
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Heme oxygenase-1, a critical arbitrator of cell death pathways in lung injury and disease.

TL;DR: Enhanced HO-1 expression or the pharmacological application of HO end-products affords protection in preclinical models of tissue injury, including experimental and transplant-associated ischemia/reperfusion injury, promising potential future therapeutic applications.
References
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Journal ArticleDOI

Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response

TL;DR: In this article, the lumenal domains of transmembrane protein kinases (PERK and IRE1) were found to be functionally interchangeable in mediating an ER stress response and that in unstressed cells, both L1 and L2 domains formed a stable complex with the ER chaperone BiP.

Dynamic interaction of BiP and ER stress transducers in the unfolded

TL;DR: It is shown that the lumenal domains of these two proteins are functionally interchangeable in mediating an ER stress response and that, in unstressed cells, both lumenAL domains form a stable complex with the ER chaperone BiP.
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Carbon monoxide has anti-inflammatory effects involving the mitogen-activated protein kinase pathway

TL;DR: It is demonstrated here that carbon monoxide, a by-product of heme catabolism by heme oxygenase, mediates potent anti-inflammatory effects and may have an important protective function in inflammatory disease states and thus has potential therapeutic uses.
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Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite.

TL;DR: The observation of a high level of induction of the enzyme in cells from an organ not involved in hemoglobin breakdown strongly supports the proposal that the induction of heme oxygenase may be a general response to oxidant stress and constitutes an important cellular defense mechanism against oxidative damage.
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Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene.

TL;DR: Results implicate Nrf2 in the induction of the HO-1 gene but suggest that the NRF2 partner in this function is a factor other than p18 or Jun proteins.
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