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Heme oxygenase in the retina in diabetes
Current Eye Research, 2003Heme oxygenase (HO) isoforms, HO-1, and HO-2, are responsible for heme breakdown to iron and carbon monoxide (CO). HO may respond to oxidative stress and may modulate the expression of vasoactive factors like nitric oxide (NO). Since diabetes induced oxidative stress may change HO, the present study examined whether diabetes is associated with HO ...
Subrata Chakabarti +3 more
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Current Opinion in Chemical Biology, 2002
Our understanding of the biological significance and chemical properties of non-heme iron oxygenases has increased dramatically in recent years. New group members have emerged from genome sequences and biochemical analyses. Spectroscopic and crystallographic studies have provided critical insights into catalysis.
Matthew J. Ryle, Robert P. Hausinger
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Our understanding of the biological significance and chemical properties of non-heme iron oxygenases has increased dramatically in recent years. New group members have emerged from genome sequences and biochemical analyses. Spectroscopic and crystallographic studies have provided critical insights into catalysis.
Matthew J. Ryle, Robert P. Hausinger
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Different Faces of the Heme-Heme Oxygenase System in Inflammation [PDF]
Pharmacological Reviews, 2003 The heme-heme oxygenase system has recently been recognized to possess important regulatory properties. It is tightly involved in both physiological as well as pathophysiological processes, such as cytoprotection, apoptosis, and inflammation. Heme functions as a double-edged sword.
Wagener, F.A.D.T.G. +6 more
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Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications.
Physiological Reviews, 2006The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2), catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (i.e., biliverdin and bilirubin) and thus constitute a major intracellular ...
S. Ryter, J. Alam, A. Choi
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The mechanism of heme oxygenase
Current Opinion in Chemical Biology, 2000Major advances have been made in determining the structure of heme oxygenase and the relationship between its structure and catalytic activity. The nature of the first step in the reaction sequence, heme alpha-meso-hydroxylation, is now clear, although the mechanisms that control the alpha-regiospecificity remain elusive. Hypothetical mechanisms can be
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, 2002 Oxidative stresses such as oxidant stimuli, inflammation, exposure to xenobiotics, and ionizing irradiation elicit various tissue injuries and provoke cellular responses, principally involving transcriptional activation of genes encoding proteins which participate in the defense reactions (Camhi et al., 1995).
Reiko Akagi +4 more
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Heme Oxygenase and Atherosclerosis [PDF]
, 2002 Atherosclerosis is characterized by the accumulation of lipids and fibrous elements in large and medium-sized elastic and muscular arteries. It may result in the obstruction of blood flow which can result in ischemia of the heart, brain, or extremities.1,2 For many decades, it was considered a degenerative disease; currently it is better understood as ...
Aldons J. Lusis +2 more
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Heme oxygenase and renal disease
Current Hypertension Reports, 2009The cellular content of heme, derived from the breakdown of heme proteins, is regulated via the heme oxygenase (HO) enzyme system. HO catalyzes the rate-limiting step in heme degradation resulting in the formation of iron, carbon monoxide, and biliverdin.
Anupam Agarwal, Tambi Jarmi
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Heme oxygenase-1: unleashing the protective properties of heme [PDF]
Trends in Immunology, 2003 Heme oxygenase (HO)-1 catabolizes heme into three products: carbon monoxide (CO), biliverdin (which is rapidly converted to bilirubin) and free iron (which leads to the induction of ferritin, an iron-binding protein). HO-1 serves as a "protective" gene by virtue of the anti-inflammatory, anti-apoptotic and anti-proliferative actions of one or more of ...
Fritz H. Bach +3 more
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Current Pharmaceutical Design, 2008
Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin. In the recent years, HO-1 expression has been reported as an important protective endogenous mechanism against physical, chemical and biological stress.
María Luisa Ferrándiz, Isabel Devesa
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Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin. In the recent years, HO-1 expression has been reported as an important protective endogenous mechanism against physical, chemical and biological stress.
María Luisa Ferrándiz, Isabel Devesa
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