Viktória Jeney

TL;DR: The mechanism underlying this cytoprotective effect relies on the ability of HO-1 to catabolize free heme and prevent it from sensitizing cells to undergo programmed cell death.

TL;DR: It is concluded that hemoglobin, when oxidized in plasma, can be indirectly cytotoxic through the generation of oxidized LDL by released heme and that, in response, the intracellular defense-HO-1 and ferritin-is induced.

TL;DR: Both heme oxygenase-1 and carbon monoxide prevented blood-brain barrier disruption, brain microvasculature congestion and neuroinflammation, including CD8+ T-cell brain sequestration and were mediated by the binding of CO to hemoglobin, preventing hemoglobin oxidation and the generation of free heme, a molecule that triggers ECM pathogenesis.

TL;DR: Protective effect of this heme-catabolizing enzyme relies on its ability to prevent tissue damage caused by the circulating free heme released from hemoglobin during infection, and it is proposed that targeting freeHeme by HPX might be used therapeutically to treat severe sepsis.

TL;DR: Sickle human hemoglobin confers a survival advantage to individuals living in endemic areas of malaria, the disease caused by Plasmodium infection, as demonstrated hereby, mice expressing sickle Hb do not succumb to experimental cerebral malaria (ECM).