Developmental Biology of Heme Oxygenase
Clinics in Perinatology, 1990 The regulation of heme oxygenase activity in the developing neonate is essential to the control of bilirubin production as well as intracellular heme and hemoprotein metabolism. The coordinated activity of the microsomal enzymes, heme oxygenase and NADPH-cytochrome c (P450) reductase, and the cytosolic enzyme biliverdin reductase is responsible for the
David K. Stevenson, Pamela A. Rodgers
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Heme Oxygenase-1 Deficiency [PDF]
Indian Pediatrics, 2021 Manisha Madkaikar +2 more
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The N-end rule pathway is a sensor of heme [PDF]
, 2008 The conjugation of arginine, by arginyl-transferase, to N-terminal aspartate, glutamate or oxidized cysteine is a part of the N-end rule pathway of protein degradation.
A. Varshavsky +21 more
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Identification, heterologous expression and characterization of a dye-decolorizing peroxidase of Pleurotus sapidus [PDF]
, 2017 The coding sequence of a peroxidase from the secretome of Pleurotus sapidus was cloned from a cDNA library. Bioinformatic analyses revealed an open reading frame of 1551 bp corresponding to a primary translation product of 516 amino acids.
Lauber, Christiane +5 more
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Heme oxygenase-1 deficiency alters erythroblastic Island formation, steady-state erythropoiesis and red blood cell lifespan in mice [PDF]
, 2015 Heme oxygenase-1 is critical for iron recycling during red blood cell turnover, whereas its impact on steady-state erythropoiesis and red blood cell lifespan is not known.
Andrade, Osvaldo Cooley +13 more
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Journal of Biological Chemistry, 1969 Abstract This study characterizes microsomal heme oxygenase, a previously undescribed enzyme which catalyzes the oxidation of heme at the α-methene bridge to form biliverdin. This step is then coupled with soluble NADPH-dependent biliverdin reductase to form bilirubin; microsomal heme oxygenase is rate-limiting in this pathway.
Rudi Schmid +2 more
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Heme Oxygenase-1: A Metabolic Nike [PDF]
Antioxidants & Redox Signaling, 2014 Heme degradation, which was described more than 30 years ago, is still very actively explored with many novel discoveries on its role in various disease models every year.The heme oxygenases (HO) are metabolic enzymes that utilize NADPH and oxygen to break apart the heme moiety liberating biliverdin (BV), carbon monoxide (CO), and iron.
Wegiel, Barbara +4 more
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Phenolic metabolites of anthocyanins modulate mechanisms of endothelial function [PDF]
, 2015 Anthocyanins are reported to have vascular bioactivity, however their mechanisms of action are largely unknown. Evidence suggests that anthocyanins modulate endothelial function, potentially by increasing nitric oxide (NO) synthesis, or enhancing NO ...
Cassidy, Aedin +4 more
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The effects of Bilirubin and Bilirubin-di-taurate on ischemia reperfusion injruy in a rat model of kidney transplantation [PDF]
, 2011 Background: Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the conversion of heme into biliverdin, carbon monoxide (CO) and free iron. Biliverdin is then subsequently reduced to bilirubin by the enzyme bilverdin reductase.
Thomas, Michael
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The protective role of pregnane X receptor in lipopolysaccharide/D-galactosamine-induced acute liver injury. [PDF]
, 2010 The pregnane X receptor (PXR) is a nuclear receptor transcription factor regulating drug-metabolizing enzymes and transporters that facilitate xenobiotic and endobiotic detoxification.
Damjanov, Ivan +2 more
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