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Heme degradation and vascular injury Belcher JD; Beckman JD; Balla G; Balla J; Vercellotti GAntioxid Redox Signal 2010[Feb]; 12 (2): 233-48Heme is an essential molecule in aerobic organisms. Heme consists of protoporphyrin IX and a ferrous (Fe(2+)) iron atom, which has high affinity for oxygen (O(2)). Hemoglobin, the major oxygen-carrying protein in blood, is the most abundant heme-protein in animals and humans. Hemoglobin consists of four globin subunits (alpha(2)beta(2)), with each subunit carrying a heme group. Ferrous (Fe(2+)) hemoglobin is easily oxidized in circulation to ferric (Fe(3+)) hemoglobin, which readily releases free hemin. Hemin is hydrophobic and intercalates into cell membranes. Hydrogen peroxide can split the heme ring and release "free" redox-active iron, which catalytically amplifies the production of reactive oxygen species. These oxidants can oxidize lipids, proteins, and DNA; activate cell-signaling pathways and oxidant-sensitive, proinflammatory transcription factors; alter protein expression; perturb membrane channels; and induce apoptosis and cell death. Heme-derived oxidants induce recruitment of leukocytes, platelets, and red blood cells to the vessel wall; oxidize low-density lipoproteins; and consume nitric oxide. Heme metabolism, extracellular and intracellular defenses against heme, and cellular cytoprotective adaptations are emphasized. Sickle cell disease, an archetypal example of hemolysis, heme-induced oxidative stress, and cytoprotective adaptation, is reviewed.|Anemia, Sickle Cell/metabolism[MESH]|Animals[MESH]|Blood Vessels/injuries[MESH]|Enzyme Activation/drug effects[MESH]|Heme Oxygenase-1/metabolism[MESH]|Heme/*metabolism[MESH]|Hemin/metabolism/pharmacology[MESH]|Hemoglobins/metabolism[MESH]|Humans[MESH]|Hydrogen Peroxide/metabolism[MESH]|Mice[MESH]|Models, Biological[MESH]|Oxidants/metabolism[MESH]|Oxidation-Reduction/drug effects[MESH]|Oxidative Stress/drug effects/physiology[MESH] |
