Szczegóły publikacji
Opis bibliograficzny
Irreversible alterations in the hemoglobin structure affect oxygen binding in human packed red blood cells / Ewa Szczęsny-Małysiak, Jakub Dybaś, Aneta Blat, Katarzyna Bułat, Kamil Kuś, Magdalena Kaczmarska, Aleksandra WAJDA, Kamilla Małek, Stefan Chłopicki, Katarzyna M. Marzec // Biochimica et Biophysica Acta. Molecular Cell Research ; ISSN 0167-4889. — 2020 — vol. 1867 iss. 11 art. no. 118803, s. 1–11. — Bibliogr. s. 9–11, Abstr. — Publikacja dostępna online od: 2020-07-30. — A. Wajda – dod. afiliacja: Jagiellonian Center for Experimental Therapeutics, Jagiellonian University; K. Bułat, K. Marzec – afiliacja: Jagiellonian Center for Experimental Therapeutics, Jagiellonian Universit
Autorzy (10)
- Szczęsny-Małysiak Ewa
- Dybaś Jakub
- Blat Aneta
- Bułat Katarzyna
- Kuś Kamil
- Kaczmarska Magdalena
- AGHWajda Aleksandra Anna
- Małek Kamilla
- Chłopicki Stefan
- Marzec Katarzyna M.
Słowa kluczowe
Dane bibliometryczne
| ID BaDAP | 129965 |
|---|---|
| Data dodania do BaDAP | 2020-09-15 |
| Tekst źródłowy | URL |
| DOI | 10.1016/j.bbamcr.2020.118803 |
| Rok publikacji | 2020 |
| Typ publikacji | artykuł w czasopiśmie |
| Otwarty dostęp |  |
| Creative Commons | |
| Czasopismo/seria | Biochimica et Biophysica Acta, Molecular Cell Research |
Abstract
The ability of hemoglobin (Hb) to transport respiratory gases is directly linked to its quaternary structure properties and reversible changes between T (tense) and R (relax) state. In this study we demonstrated that packed red blood cells (pRBCs) storage resulted in a gradual increase in the irreversible changes in the secondary and quaternary structures of Hb, with subsequent impairment of the T↔R transition. Such alteration was associated with the presence of irreversibly settled in the relaxed form, quaternary structure of Hb, which we termed R′. On the secondary structure level, disordered protein organization involved formation of β-sheets and a decrease in α-helices related to the aggregation process stabilized by strong intermolecular hydrogen bonding. Compensatory changes in RBCs metabolism launched to preserve reductive microenvironment were disclosed as an activation of nicotinamide adenine dinucleotide phosphate (NADPH) production and increased reduced to oxidized glutathione (GSH/GSSG) ratio. For the first time we showed the relationship between secondary structure changes and the occurrence of newly discovered R′, which through an artificial increase in oxyhemoglobin level altered Hb ability to bind and release oxygen.
