Resolution of the rat brain heme oxygenase activity: Absence of a detectable amount of the inducible form (HO-1)
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The sinister face of heme oxygenase-1 in brain aging and disease
2019, Progress in NeurobiologyCitation Excerpt :In the normal, unstressed rodent brain, low-level HO-1 expression is seen in scattered neurons of the cerebral cortex, hippocampal dentate gyrus, thalamus, hypothalamus, cerebellum (Purkinje cells) and brain stem (Baranano and Snyder, 2001; Bergeron et al., 1998; Matz et al., 1996; Nakaso et al., 2000; Vincent et al., 1994). HO-2 mRNA and protein, in contrast, are relatively abundant in olfactory epithelium and olfactory bulb, hippocampal pyramidal cells and dentate gyrus, and cerebellar Purkinje and granule cell layers (Dwyer et al., 1995b; Trakshel et al., 1988; Verma et al., 1993). In rat brain, there is considerable overlap between the topography of HO-2 expression and the distribution of soluble guanylate cyclase.
Development of new HO-1 inhibitors by a thorough scaffold-hopping analysis
2018, Bioorganic ChemistryPotholing of the hydrophobic heme oxygenase-1 western region for the search of potent and selective imidazole-based inhibitors
2018, European Journal of Medicinal ChemistryCitation Excerpt :C18H17IN2O) C, H, N. HO-1 and HO-2 were obtained, respectively, from rat spleen and brain as the microsomal fraction prepared by differential centrifugation; the dominance of HO-1 protein in the rat spleen and of HO-2 in the rat brain has been well documented [47–50]. These particular microsomal preparations were selected in order to use the most native (i.e., closest to in vivo) forms of HO-1 and HO-2.
Physiology of Cerebral Blood Vessels
2017, Brain Edema: From Molecular Mechanisms to Clinical PracticeCharacterization of heme oxygenase and biliverdin reductase gene expression in zebrafish (Danio rerio): Basal expression and response to pro-oxidant exposures
2016, Toxicology and Applied PharmacologyCitation Excerpt :To this end, HMOX1 has been shown to be highly inducible by a variety of stressors in mammalian systems, and is detected at high levels in tissues involved in heme metabolism including spleen and liver (Tenhunen et al., 1969), bone marrow (Brown et al., 1988; Abraham et al., 1989) and erythroid cells (Garcia-Santos et al., 2014). The other heme degrading enzyme, HMOX2, is expressed at high levels in the testes (Trakshel et al., 1986), brain (Maines et al., 1986; Trakshel et al., 1988; Ewing and Maines, 1992), and vascular tissues (Zakhary et al., 1996). The BVR isoforms are distinct in their enzymatic actions and their evolutionary origins (Yamaguchi et al., 1993).
Ischemic preconditioning protects hippocampal pyramidal neurons from transient ischemic injury via the attenuation of oxidative damage through upregulating heme oxygenase-1
2015, Free Radical Biology and MedicineCitation Excerpt :To reduce background staining, the membranes were incubated with 5% nonfat dry milk in TBS containing 0.1% Tween 20 for 45 min, followed by incubation with rabbit anti-HO-1 (diluted 1:1000) overnight at 4 °C and subsequently exposed to peroxidase-conjugated donkey anti-rabbit IgG and an ECL kit (Pierce Chemical). HO-1 activity in the hippocampus at 12 h, 1 day, and 5 days after ischemia–reperfusion (n=7 at each time point) was measured by bilirubin generation as described previously [28,29]. The samples were homogenized in lysis buffer (50 mM Tris-HCl, pH 7.4, containing 150 mM NaCl, 250 mM sucrose, 0.4 mM PMSF, 1 g/L leupeptin, and 1 g/L aprotinin).