Understanding the processes governing the ability of the heart to repair and regenerate after injury is crucial for developing translational medical solutions. New avenues of exploration include cardiac cell therapy and cellular reprogramming targeting cell death and regeneration. An attractive possibility is the exploitation of cytoprotective genes that exist solely for self-preservation proce...

The development of heme oxygenase (HO) inhibitors, especially those that are isozyme-selective, promises powerful pharmacological tools to elucidate the regulatory characteristics of the HO system. It is already known that HO has cytoprotective properties and may play a role in several disease states, making it an enticing therapeutic target. Traditionally, the metalloporphyrins have been used ...

The presence of heme oxygenase and NADPH cytochrome P-450 (c) reductase, the latter an integral component of heme oxygenase and cytochrome P-450-dependent drug metabolizing enzymes, was demonstrated in human corneal epithelium. We reported for the first time that human corneal epithelium contains heme oxygenase activity as high as 20% of that reported for the human liver. Using immunological te...

5-Aminolevulinic acid (ALA) is the rate-limiting intermediate in heme biosynthesis vertebrate species; a reaction catalyzed by mitochondrial ALA synthase 1 (ALAS1) enzyme. Previously we reported that knockdown of ubiquitously expressed ALAS1 gene mice disrupts normal glucose metabolism, attenuates function and results prediabetic like phenotype when animals pass 20-weeks age (Saitoh et al., 201...

The data have been obtained from the Heme Oxygenase Database (HemeOxDB) and refined according to the 2D-QSAR requirements. These data provide information about a set of more than 380 Heme Oxygenase-1 (HO-1) inhibitors. The development of the 2D-QSAR model has been undertaken with the use of CORAL software using SMILES, molecular graphs and hybrid descriptors (SMILES and graph together). The 2D-...

The enzyme heme oxygenase, which exists in inducible (HO-1) and constitutive (HO-2) isoforms, catalyzes the degradation of heme to biliverdin and CO in mammalian tissues. CO has been implicated in the control of vascular tone in a manner similar to that for NO. In the present study, we investigated the contribution of the heme oxygenase/CO pathway to the modulation of acute hypertensive respons...

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...

The heat shock protein heme oxygenase-1 (HO-1) is regulated by a variety of physiological and pharmacological factors. In skeletal muscle tissue, HO-1 has been shown to be induced only by exercise and electrical stimulation in vivo. Both hemin and sodium nitroprusside (SNP) are potent inducers of HO-1 in other tissues. In this study, we examined the effects of these two agents on HO-1 induction...

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...