Heme oxygenase-1 induction protects murine cortical astrocytes from hemoglobin toxicity
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Deferoxamine deconditioning increases neuronal vulnerability to hemoglobin
2020, Experimental Cell ResearchSystemic hemin therapy attenuates blood-brain barrier disruption after intracerebral hemorrhage
2014, Neurobiology of DiseaseCitation Excerpt :It may contribute to cell injury in adjacent tissue by a direct cytotoxic effect and also by release of redox-active iron with its breakdown (Robinson et al., 2009). However, at nontoxic concentrations, hemin delivers a potent preconditioning stimulus to cultured cells that protects them from subsequent exposure to toxic concentrations of hemin and other oxidants (Balla et al., 1992; Li et al., 2009; Regan et al., 2000). This effect, which requires a preconditioning interval of several hours (Balla et al., 1993), is mediated at least in part by induction of heme oxygenase (HO)-1 (Belcher et al., 2006; Li et al., 2009).
Cytotoxic effect of hemin in colonic epithelial cell line: Involvement of 18 kDa translocator protein (TSPO)
2014, Life SciencesCitation Excerpt :Several researchers on neuronal cells showed that iron release from hemin after HO-1 activity was responsible of the cell toxicity (Goldstein et al., 2003; Dwyer et al., 1998; Huang et al., 2002). However, Regan et al. (2000) previously observed that HO-1 induction was protective in cultured astrocytes exposed to hemoglobin (Regan et al., 2000). A beneficial effect of HO-1 has also been observed by Doré and Snyder (1999) in hippocampal neurons exposed to hydrogen peroxide and in systems of non-neural origin (Vile et al., 1994; Abraham et al., 1995; Dennery et al., 1997; Ishikawa et al., 2010).
Blood-brain barrier disruption and oxidative stress in guinea pig after systemic exposure to modified cell-free hemoglobin
2011, American Journal of PathologyHeme oxygenase activity and hemoglobin neurotoxicity are attenuated by inhibitors of the MEK/ERK pathway
2009, NeuropharmacologyCitation Excerpt :Although the association of reduced HO activity and neuronal resistance to hemoglobin is consistent with prior observations using more specific approaches (Huang et al., 2002; Rogers et al., 2003), the downstream mechanistic information provided by inhibiting the MEK/ERK pathway is limited by the myriad effects of ERK signaling. We have previously reported that HO-1 is expressed at a low level in primary cultured neurons and glia, and that it is rapidly induced in glia by hemoglobin or hemin treatment (Regan et al., 2000; Benvenisti-Zarom et al., 2006). In contrast to the effect of HO on neurons, HO-1 expression protects glial cells from hemoglobin (Regan et al., 2000; Chen-Roetling and Regan, 2006).
The Nrf2-ARE cytoprotective pathway in astrocytes
2009, Expert Reviews in Molecular Medicine