Heme oxygenase (HO)-1 catalyzes the oxidative cleavage of heme to yield equimolar
amounts of biliverdin, iron, and carbon monoxide. HO-1 is a stress response protein, the …

Increases in cell death by programmed (ie, apoptosis, autophagy) or nonprogrammed
mechanisms (ie, necrosis) occur during tissue injury and may contribute to the etiology of …

Abstract Heme oxygenase-1 (HO-1), an inducible stress protein, confers cytoprotection
against oxidative stress in vitro and in vivo. In addition to its physiological role in heme …

Abstract Heme oxygenase-1 (HO-1) is an inducible enzyme that catalyzes oxidative
degradation of heme to form biliverdin, carbon monoxide (CO), and free iron. Biliverdin is …

Heme oxygenase-1 (HO-1) catalyzes the degradation of heme and forms antioxidant bile
pigments as well as the signaling molecule carbon monoxide. HO-1 is inducible in response …

Heme oxygenase (HO) catalyzes the rate-limiting step in the degradation of heme to
biliverdin, which is reduced by biliverdin reductase to bilirubin. Heme oxygenase-1 (HO-1) is …

Heme oxygenase 1 (HO-1) inhibits apoptosis by regulating cellular prooxidant iron. We now
show that there is an additional mechanism by which HO-1 inhibits apoptosis, namely by …

Heme oxygenase catalyzes the rate-limiting step in heme degradation in order to generate
biliverdin, carbon monoxide (CO), and iron. The inducible form of the enzyme, heme …

Accumulating evidence suggests that oxidative stress plays a central role in the
pathogenesis of many pulmonary diseases including adult respiratory distress syndrome …

Heme oxygenase (HO) breaks down heme, the iron-containing, oxygen-carrying constituent
of red blood cells, yielding biliverdin, iron (II) ions, and carbon monoxide (CO). Among the …