Heme oxygenase, an essential enzyme of heme catabolism, is inducible by its substrate heme, by heavy metals, and by various other substances. To study the molecular mechanisms of the induction of heme oxygenase, we isolated the heme oxygenase gene from a rat genomic DNA library using cloned cDNA as hybridization probes and determined its complete nucleotide sequence. The gene is composed of 683...

A full-length heme oxygenase gene from the gram-negative pathogen Neisseria meningitidis was cloned and expressed in Escherichia coli. Expression of the enzyme yielded soluble catalytically active protein and caused accumulation of biliverdin within the E. coli cells. The purified HemO forms a 1:1 complex with heme and has a heme protein spectrum similar to that previously reported for the puri...

Cytochrome P450 content and activities are increased in the kidneys of spontaneously hypertensive rats (SHR) as compared with those of normotensive, Wistar-Kyoto (WKY), control rats during the period of rapid elevation of blood pressure. We studied the effect of heme arginate, a potent inducer of heme oxygenase (EC 1.14.99.3), on microsomal cytochrome P450 levels and activities and blood pressu...

Purpose: Different studies suggest the defending role of bilirubin and “heme-oxygenase-1(HO-1)” in inflammatory illnesses, but there are limited that evaluate these two recovered patients. Methods: Therefore, current study evaluates HO-1 patients who suffered from glomerulonephritis (6 months ago) control group. Findings &Practical Implication: After obtaining informed consent, sample urine...

Nitric oxide and S-nitrosothiols modulate a variety of important physiological activities. In vascular cells, agents that release NO and donate nitrosonium cation (NO(+)), such as S-nitrosoglutathione, are potent inducers of the antioxidant protein heme oxygenase 1 (HO-1) (Foresti, R., Clark, J. E., Green, C. J., and Motterlini, R. (1997) J. Biol. Chem. 272, 18411-18417; Motterlini, R., Foresti...

Heme proteins such as myoglobin or hemoglobin, when released into the extracellular space, can instigate tissue toxicity. Myoglobin is directly implicated in the pathogenesis of renal failure in rhabdomyolysis. In the glycerol model of this syndrome, we demonstrate that the kidney responds to such inordinate amounts of heme proteins by inducing the heme-degradative enzyme, heme oxygenase, as we...

Neuronal nitric oxide synthase (nNOS) is composed of an oxygenase domain that binds heme, (6R)-tetrahydrobiopterin, and Arg, coupled to a reductase domain that binds FAD, FMN, and NADPH. Activity requires dimeric interaction between two oxygenase domains and calmodulin binding between the reductase and oxygenase domains, which triggers electron transfer between flavin and heme groups. We constr...

Heme oxygenase from Leptospira interrogans is an important virulence factor. During catalysis, redox equivalents are provided to this enzyme by the plastidic-type ferredoxin-NADP+ reductase also found in L. interrogans. This process may have evolved to aid this bacterial pathogen to obtain heme-iron from their host and enable successful colonization. Herein we report the crystal structure of th...

Hemin treatment of the Philadelphia chromosome positive leukemia cell line, K562, accentuates a number of erythroid phenotypic characteristics. The nature of this hemin effect was investigated by examining heme production and heme biosynthetic and catabolic enzyme activity in untreated and 0.05 mM hemin-treated cells. Activities of -aminolevulinic acid synthetase (ALAS). the rate limiting heme ...

The single nucleotide polymorphism rs2071746 and a (GT)n microsatellite within the human gene encoding heme oxygenase-1 (HMOX1) are associated with incidence or outcome in a variety of diseases. Most of these associations involve either release of heme or oxidative stress. Both polymorphisms are localized in the promoter region, but previously reported correlations with heme oxygenase-1 express...