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- W81085150 abstract "Cell injury and inflammation evoke several adaptive responses that are beneficial and protective. Many of these cellular responses occur due to inflammatory stimuli such as cytokines, endotoxin, growth factors (e.g. transforming growth factor-p), lipid derivatives (e.g. oxidized LDL) and a diverse array of oxidants [1, 2]. One such cellular response in cells and tissues exposed to these stimuli is the induction of heme oxygenase-1 (HO-1), a — 32 kDa microsomal enzyme [3-9]. HO-1 catalyzes the rate limiting step in heme degradation resulting in the liberation of equimolar quantities of biliverdin, iron and carbon monoxide (CO) as shown below. Biliverdin is subsequently converted to bilirubin. Heme is derived from ubiquitously distributed heme proteins such as cytochromes, peroxidases, respiratory burst oxidases, pyrrolases, catalase, nitric oxide synthases, hemoglobin and myoglobin; all crucial in the maintenance of normal cellular functions [6]. Recent attention has focussed on the by product(s) of this reaction which possess important antioxidant, anti-inflammatory, anti-apoptotic and possible immune modulatory functions [10-17]." @default.
- W81085150 created "2016-06-24" @default.
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- W81085150 date "2001-01-01" @default.
- W81085150 modified "2023-09-25" @default.
- W81085150 title "Heme Oxygenase-1, Inflammation and Atherosclerosis" @default.
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- W81085150 doi "https://doi.org/10.1007/978-3-0348-8239-2_10" @default.
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