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Impact of cold storage on the oxygenation and oxidation reactions of red blood cells.
Kassa, Tigist; Jana, Sirsendu; Baek, Jin Hyen; Alayash, Abdu I.
Afiliación
  • Kassa T; Laboratory of Biochemistry and Vascular Physiology, Division of Blood Component and Devices, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, MD, United States.
  • Jana S; Laboratory of Biochemistry and Vascular Physiology, Division of Blood Component and Devices, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, MD, United States.
  • Baek JH; Laboratory of Biochemistry and Vascular Physiology, Division of Blood Component and Devices, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, MD, United States.
  • Alayash AI; Laboratory of Biochemistry and Vascular Physiology, Division of Blood Component and Devices, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, MD, United States.
Front Physiol ; 15: 1427094, 2024.
Article en En | MEDLINE | ID: mdl-39224206
ABSTRACT

Introduction:

Electrostatic binding of deoxyhemoglobin (Hb) to cytoplasmic domain of band 3 anion transport protein occurs as part of the glycolytic regulation in red blood cells (RBCs). Hb oxidation intermediates not only impact RBC's oxygenation but also RBC's membrane through the interaction with band 3. It is not known however whether these critical pathways undergo changes during the storage of RBCs. Methods and

Results:

Oxygen parameters of fresh blood showed a sigmoidal and cooperative oxygen dissociation curve (ODC) for the first week of storage. This was followed by a large drop in oxygen affinity (P50) (from 30 to 20 mmHg) which remained nearly unchanged with a slight elevation in Bohr coefficients and a significant drop in extracellular acidification rates (ECAR) at the 42-day storage. Oxidation of Hb increased with time as well as the formation of a highly reactive ferryl Hb under oxidative stress conditions. Ferryl Hb interacted avidly with RBC's membrane's band 3, but to lesser extent with old ghost RBCs.

Discussion:

The observed alterations in RBC's oxygen binding may have been affected by the alterations in band 3's integrity which are largely driven by the internal iron oxidation of Hb. Restoring oxygen homeostasis in stored blood may require therapeutic interventions that target changes in Hb oxidation and membrane changes.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Front Physiol Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Suiza
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Front Physiol Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Suiza