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lüll The story so far: Molecular regulation of the heme oxygenase-1 gene in renal injury Sikorski EM; Hock T; Hill-Kapturczak N; Agarwal AAm J Physiol Renal Physiol 2004[Mar]; 286 (3): F425-41Heme oxygenases (HOs) catalyze the rate-limiting step in heme degradation, resulting in the formation of iron, carbon monoxide, and biliverdin, the latter of which is subsequently converted to bilirubin by biliverdin reductase. Recent attention has focused on the biological effects of product(s) of this enzymatic reaction, which have important antioxidant, anti-inflammatory, and cytoprotective functions. Two major isoforms of the HO enzyme have been described: an inducible isoform, HO-1, and a constitutively expressed isoform, HO-2. A third isoform, HO-3, closely related to HO-2, has also been described. Several stimuli implicated in the pathogenesis of renal injury, such as heme, nitric oxide, growth factors, angiotensin II, cytokines, and nephrotoxins, induce HO-1. Induction of HO-1 occurs as an adaptive and beneficial response to these stimuli, as demonstrated by studies in renal and non-renal disease states. This review will focus on the molecular regulation of the HO-1 gene in renal injury and will highlight the interspecies differences, predominantly between the rodent and human HO-1 genes.|Animals[MESH]|Base Sequence[MESH]|Gene Expression Regulation[MESH]|Heme Oxygenase (Decyclizing)/biosynthesis/*genetics/physiology[MESH]|Heme Oxygenase-1[MESH]|Humans[MESH]|Kidney Diseases/*enzymology/genetics[MESH]|Membrane Proteins[MESH]|Mice[MESH]|Molecular Sequence Data[MESH]|Species Specificity[MESH] |