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Hemopexin is a plasma glycoprotein with the highest binding affinity for free heme in humans. It acts as a scavenger of free heme released during hemolysis, thereby preventing the pro-oxidant and pro-inflammatory effects of free heme and promoting its detoxification. By binding to free heme, hemopexin forms a complex that is cleared by receptors such as LRP1 on hepatocytes or macrophages in the liver, spleen, and bone marrow. This mechanism protects tissues from oxidative damage and inflammation associated with hemolytic conditions. Therapeutically, exogenous administration of hemopexin has shown promise in preclinical models for protecting against vascular dysfunction and organ damage in diseases characterized by excessive hemolysis, such as sickle cell disease and β-thalassemia[2][4][6].
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