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Hemoglobin Oxidation Reactions in Stored Blood
1Laboratory of Biochemistry and Vascular Biology, Division of Blood Components and Devices (DBCD), Center for Biologics Evaluation and Research (CBER), Food and Drug Administration (FDA), Silver Spring, MD 20993, USA.
Hemoglobin (Hb) oxidation, forming ferric (Fe3+) and ferryl (Fe4+) heme, can impair red blood cell (RBC) function. This review details Hb oxidative lesions and their clinical impact on stored or processed blood.
Area of Science:
- Biochemistry
- Hematology
- Cell Biology
Background:
- Hemoglobin (Hb) undergoes autoxidation, converting functional ferrous (Fe2+) heme to oxidized ferric (Fe3+) and highly reactive ferryl (Fe4+) forms.
- Red blood cells (RBCs) possess mechanisms to counteract Hb oxidation, maintaining cellular integrity during their lifespan.
- Oxidative stress can accelerate Hb oxidation, leading to non-functional Hb and potential cellular damage.
Purpose of the Study:
- To review the biochemical processes of hemoglobin oxidation within red blood cells.
- To describe the impact of Hb oxidation on RBC integrity and function.
- To discuss the clinical implications of Hb oxidative lesions in stored or processed blood.
Main Methods:
- Literature review of Hb autoxidation and redox reactions.
- Analysis of factors influencing Hb oxidation in RBCs.
- Examination of the consequences of Hb oxidation on blood product efficacy.
Main Results:
- Hb autoxidation produces Fe3+ and Fe4+ forms, with Fe4+ exhibiting high reactivity.
- RBCs have endogenous systems to reduce oxidized Hb, but these can be overwhelmed.
- Hb oxidation is exacerbated under oxidative stress and during ex vivo storage or processing.
Conclusions:
- Hb oxidation represents a significant 'oxidative lesion' impacting RBC function and integrity.
- Understanding Hb oxidation mechanisms is crucial for improving the clinical utility of stored and processed blood.
- Further research is needed to mitigate Hb oxidation and its adverse effects in transfusion medicine.
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