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Open AccessJournal ArticleDOI

Heme oxygenase-1 protein localizes to the nucleus and activates transcription factors important in oxidative stress.

TLDR
It is speculated that nuclear localization of HO-1 protein may serve to up-regulate genes that promote cytoprotection against oxidative stress after exposure to hypoxia and heme or heme/hemopexin.
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This article is published in Journal of Biological Chemistry.The article was published on 2007-07-13 and is currently open access. It has received 366 citations till now. The article focuses on the topics: Nuclear protein & Heme oxygenase.

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Citations
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Journal ArticleDOI

Mechanisms of Cell Protection by Heme Oxygenase-1

TL;DR: The mechanism underlying this cytoprotective effect relies on the ability of HO-1 to catabolize free heme and prevent it from sensitizing cells to undergo programmed cell death.
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.
Journal ArticleDOI

Heme oxygenase-1/carbon monoxide: from metabolism to molecular therapy.

TL;DR: Translational and clinical trials research will unveil whether the HO-1 system or any of its reaction products can be successfully applied as molecular medicine in human disease.
References
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Journal ArticleDOI

Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei

TL;DR: A procedure for preparing extracts from nuclei of human tissue culture cells that directs accurate transcription initiation in vitro from class II promoters, including tRNA and Ad 2 VA, is developed.
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Bilirubin is an antioxidant of possible physiological importance

TL;DR: The data support the idea of a "beneficial" role for bilirubin as a physiological, chain-breaking antioxidant.
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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.
Journal ArticleDOI

ATF6 Activated by Proteolysis Binds in the Presence of NF-Y (CBF) Directly to the cis-Acting Element Responsible for the Mammalian Unfolded Protein Response

TL;DR: It is concluded that specific and direct interactions between ATF6 and ERSE are critical for transcriptional induction not only of ER chaperones but also of CHOP and XBP-1.
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