Desferrioxamine protects human red blood cells from hemin-induced hemolysis
| Autor: | Stephen Gene Sullivan, Erol Baysal, Hugo P. Monteiro, Arnold Stern |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Hemeprotein
Lysis Free Radicals Deferoxamine Hemolysis Biochemistry chemistry.chemical_compound Physiology (medical) polycyclic compounds medicine Humans heterocyclic compounds Red Cell Erythrocyte Membrane equipment and supplies medicine.disease Molecular biology Red blood cell medicine.anatomical_structure Membrane chemistry Spectrophotometry Hemin Hemoglobin |
| Zdroj: | Free Radical Biology and Medicine. 9:5-10 |
| ISSN: | 0891-5849 |
| DOI: | 10.1016/0891-5849(90)90043-i |
| Popis: | Hemin binding to red cell membranes, its effect on red cell hemolysis, and it interaction with desferrioxamine (DFO) in these processes were investigated. DFO interacted with hemin via the iron moiety. Blockage of the binding groups in DFO prevented interaction of DFO with hemin, implying the importance of the hydroxamic acid groups in DFO-hemin interactions. Since hemolysis is a result of hemin association with the membrane components, its binding in the presence and absence of DFO was studied. DFO strongly inhibited hemin-induced lysis in a concentration-dependent manner. With 50 microM hemin, 1 mM DFO completely inhibited lysis. Preincubation of ghost membranes with DFO (1 mM) inhibited binding of hemin (50 microM) to membranes by 42%. After ghost membranes were preincubated with hemin (50 microM), the addition of DFO (1 mM) removed 20% of the membrane-bound hemin. It is suggested that DFO may have an important role in alleviating the hemin-induced deleterious effects on the red cell membrane, especially in hemolytic anemias associated with unstable, autoxidized hemoglobins. |
| Databáze: | OpenAIRE |
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