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Heme Oxygenase-1 in Acute Lung Injury

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Molecular Biology of Acute Lung Injury

Part of the book series: Molecular and Cellular Biology of Critical Care Medicine ((MCCM,volume 1))

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Abstract

Heme oxygenase (HO) was first described, in 1968, as the enzyme responsible for the rate-limiting step in the catalytic breakdown of the heme moiety of hemoglobin, and understandably, initial work focused on the regulation and function of this enzyme in heme metabolism (1). That HO could be important for much more than the color changes of a bruise as heme was broken down through biliverdin to bilirubin, was not suspected until the work of Tyrrell and his colleagues. These researchers showed that HO-1 could be vigorously induced not just by heme, its natural substrate, but by a variety of agents that had as their common feature the ability to generate reactive oxidant species (ROS) (2). Examples of the broad spectrum of agents capable of inducing HO include lipopolysaccharide (LPS), phorbol esters, sodium arsenite, hydrogen peroxide, ultraviolet radiation, hyperthermia, hyperoxia, sulfhydryl reagents, heat shock, and heavy metals. This extraordinary variety of inducers is surprising for an enzyme subserving a seemingly housekeeping function of heme turnover, and speculation arose that the enzyme was also vital to cellular homeostasis.

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Sethi, J.M., Choi, A.M.K. (2001). Heme Oxygenase-1 in Acute Lung Injury. In: Wong, H.R., Shanley, T.P. (eds) Molecular Biology of Acute Lung Injury. Molecular and Cellular Biology of Critical Care Medicine, vol 1. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1427-5_8

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  • DOI: https://doi.org/10.1007/978-1-4615-1427-5_8

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