Heme oxygenase-1 in lung disease

Patty J. Lee; Madhu Sasidhar; Leo E. Otterbein; Jigme M. Sethi; Augustine M.K. Choi

Heme oxygenase-1 in lung disease

Patty J. Lee, Madhu Sasidhar, Leo E. Otterbein, Jigme M. Sethi, Augustine M.K. Choi

Research output: Chapter in Book/Report/Conference proceeding › Chapter

Abstract

Heme oxygenase (HO) was first described in 1968 by Raimo Tenhunen as the enzyme responsible for degrading heme, a highly conserved molecule that is essential for most forms of life (1). HO targets the α-methene bridge of the heme ring to catalyze the oxidative breakdown of heme into equimolar amounts of carbon monoxide (CO), biliverdin, and iron (Fe) (Fig. 1). In most mammals, biliverdin is subsequently reduced to bilirubin by biliverdin reductase. Under physiological conditions HO activity is highest in the spleen, where senescent erythrocytes are sequestered and destroyed, but this activity is observed in virtually all organ systems.

Original language	English (US)
Title of host publication	Disease Markers in Exhaled Breath
Publisher	CRC Press
Pages	117-131
Number of pages	15
ISBN (Electronic)	9780203909195
ISBN (Print)	9780824708177
State	Published - Jan 1 2002

ASJC Scopus subject areas

General Medicine

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AU - Sasidhar, Madhu

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AU - Sethi, Jigme M.

AU - Choi, Augustine M.K.

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N2 - Heme oxygenase (HO) was first described in 1968 by Raimo Tenhunen as the enzyme responsible for degrading heme, a highly conserved molecule that is essential for most forms of life (1). HO targets the α-methene bridge of the heme ring to catalyze the oxidative breakdown of heme into equimolar amounts of carbon monoxide (CO), biliverdin, and iron (Fe) (Fig. 1). In most mammals, biliverdin is subsequently reduced to bilirubin by biliverdin reductase. Under physiological conditions HO activity is highest in the spleen, where senescent erythrocytes are sequestered and destroyed, but this activity is observed in virtually all organ systems.

AB - Heme oxygenase (HO) was first described in 1968 by Raimo Tenhunen as the enzyme responsible for degrading heme, a highly conserved molecule that is essential for most forms of life (1). HO targets the α-methene bridge of the heme ring to catalyze the oxidative breakdown of heme into equimolar amounts of carbon monoxide (CO), biliverdin, and iron (Fe) (Fig. 1). In most mammals, biliverdin is subsequently reduced to bilirubin by biliverdin reductase. Under physiological conditions HO activity is highest in the spleen, where senescent erythrocytes are sequestered and destroyed, but this activity is observed in virtually all organ systems.

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Heme oxygenase-1 in lung disease

Abstract

ASJC Scopus subject areas

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