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Circulation Research. 2001;89:105-107

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(Circulation Research. 2001;89:105.)
© 2001 American Heart Association, Inc.


Editorial

Heme Oxygenase-1 Protects the Heart

Augustine M.K. Choi

From the Division of Pulmonary, Allergy and Critical Care Medicine, University of Pittsburgh School of Medicine, Pittsburgh, Pa.

Correspondence to Augustine M.K. Choi, MD, Division of Pulmonary, Allergy and Critical Care Medicine, University of Pittsburgh School of Medicine, MUH 628 NW, Pittsburgh, PA 15213. E-mail choiam@msx.upmc.edu


Key Words: carbon monoxide • bilirubin • ferritin

The seminal discovery of nitric oxide (NO) in the 1980s unraveled the novel concept that an endogenous production of a gaseous substance such as NO can impart diverse and critical functional effects on a wide spectrum of biological and pathological processes. Intense investigations in the chemistry and biology of NO have led to numerous fruitful discoveries, enhancing our understanding of many disease processes including cardiovascular disorders. Interestingly, though, we have known for a longer period of time that there exists another gaseous molecule, carbon monoxide (CO), which can be generated endogenously. The heme oxygenase (HO) enzyme system generates the majority of endogenous CO.1,2 Since the biochemical isolation of the HO enzyme in 1968, much of the focus of HO research has been in the study of HO in heme metabolism based on the known fact that the HO enzyme serves as the rate-limiting enzyme in the degradation of heme. However, in recent years, as a result of the emerging role of HO in a variety of biological processes, interest in HO has continued to grow beyond its role in heme metabolism and has expanded into many scientific disciplines. The recent characterization of the HO enzyme system in yeast, prokaryotic bacterial system, and plants further highlights the functional importance of a highly conserved enzyme throughout the evolution of living organisms.

HO catalyzes the first and rate-limiting step in the degradation of heme to yield equimolar quantities of biliverdin IXa, CO, and iron1,2 (Figure). Biliverdin is subsequently converted to bilirubin . . . [Full Text of this Article]




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