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β-Carotene-Induced Alterations in Haemoglobin Affinity to O(2)
β-Carotene (β-Crt) can be dispersed in hydrophobic regions of the membrane of red blood cells (RBC). Its location, orientation and distribution strongly depend on carotenoid concentration. In the present pilot trial (six human subjects involved), it is demonstrated that incubation of RBCs with β-Crt...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8001951/ https://www.ncbi.nlm.nih.gov/pubmed/33805826 http://dx.doi.org/10.3390/antiox10030451 |
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author | Fiedor, Joanna Przetocki, Mateusz Siniarski, Aleksander Gajos, Grzegorz Spiridis, Nika Freindl, Kinga Burda, Kvetoslava |
author_facet | Fiedor, Joanna Przetocki, Mateusz Siniarski, Aleksander Gajos, Grzegorz Spiridis, Nika Freindl, Kinga Burda, Kvetoslava |
author_sort | Fiedor, Joanna |
collection | PubMed |
description | β-Carotene (β-Crt) can be dispersed in hydrophobic regions of the membrane of red blood cells (RBC). Its location, orientation and distribution strongly depend on carotenoid concentration. In the present pilot trial (six human subjects involved), it is demonstrated that incubation of RBCs with β-Crt (1.8 × 10(7) β-Crt molecules per RBC, 50 μmol/L) results in expansion of the membrane of RBCs and slight elongation of the cell. The changes are of statistical significance, as verified by the Wilcoxon test at p < 0.05. They indicate (i) a highly random orientation and location of β-Crt inside the membrane and (ii) a tendency for its interaction with membrane skeleton proteins. The accompanying effect of decreased RBC resistance to lysis is possibly a result of the incorrect functioning of ion channels due to their modification/disruption. At higher β-Crt concentrations, its clustering inside membranes may occur, leading to further alterations in the shape and size of RBCs, with the most pronounced changes observed at 1.8 × 10(8) β-Crt molecules per RBC (500 μmol/L). Due to the reduced permeability of ions, such membranes exhibit increased resistance to haemolysis. Finally, we show that interactions of β-Crt with the membrane of RBCs lead to an alteration in haemoglobin-oxygen affinity, shifting the oxyhaemoglobin dissociation curve toward higher oxygen partial pressures. If the impact of β-Crt on a curve course is confirmed in vivo, one may consider its role in the fine tuning of O(2) transportation to tissues. Hence, at low concentrations, providing unchanged elastic and functional properties of RBCs, it could serve as a beneficial agent in optimising heart performance and cardiovascular load. |
format | Online Article Text |
id | pubmed-8001951 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-80019512021-03-28 β-Carotene-Induced Alterations in Haemoglobin Affinity to O(2) Fiedor, Joanna Przetocki, Mateusz Siniarski, Aleksander Gajos, Grzegorz Spiridis, Nika Freindl, Kinga Burda, Kvetoslava Antioxidants (Basel) Article β-Carotene (β-Crt) can be dispersed in hydrophobic regions of the membrane of red blood cells (RBC). Its location, orientation and distribution strongly depend on carotenoid concentration. In the present pilot trial (six human subjects involved), it is demonstrated that incubation of RBCs with β-Crt (1.8 × 10(7) β-Crt molecules per RBC, 50 μmol/L) results in expansion of the membrane of RBCs and slight elongation of the cell. The changes are of statistical significance, as verified by the Wilcoxon test at p < 0.05. They indicate (i) a highly random orientation and location of β-Crt inside the membrane and (ii) a tendency for its interaction with membrane skeleton proteins. The accompanying effect of decreased RBC resistance to lysis is possibly a result of the incorrect functioning of ion channels due to their modification/disruption. At higher β-Crt concentrations, its clustering inside membranes may occur, leading to further alterations in the shape and size of RBCs, with the most pronounced changes observed at 1.8 × 10(8) β-Crt molecules per RBC (500 μmol/L). Due to the reduced permeability of ions, such membranes exhibit increased resistance to haemolysis. Finally, we show that interactions of β-Crt with the membrane of RBCs lead to an alteration in haemoglobin-oxygen affinity, shifting the oxyhaemoglobin dissociation curve toward higher oxygen partial pressures. If the impact of β-Crt on a curve course is confirmed in vivo, one may consider its role in the fine tuning of O(2) transportation to tissues. Hence, at low concentrations, providing unchanged elastic and functional properties of RBCs, it could serve as a beneficial agent in optimising heart performance and cardiovascular load. MDPI 2021-03-13 /pmc/articles/PMC8001951/ /pubmed/33805826 http://dx.doi.org/10.3390/antiox10030451 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ). |
spellingShingle | Article Fiedor, Joanna Przetocki, Mateusz Siniarski, Aleksander Gajos, Grzegorz Spiridis, Nika Freindl, Kinga Burda, Kvetoslava β-Carotene-Induced Alterations in Haemoglobin Affinity to O(2) |
title | β-Carotene-Induced Alterations in Haemoglobin Affinity to O(2) |
title_full | β-Carotene-Induced Alterations in Haemoglobin Affinity to O(2) |
title_fullStr | β-Carotene-Induced Alterations in Haemoglobin Affinity to O(2) |
title_full_unstemmed | β-Carotene-Induced Alterations in Haemoglobin Affinity to O(2) |
title_short | β-Carotene-Induced Alterations in Haemoglobin Affinity to O(2) |
title_sort | β-carotene-induced alterations in haemoglobin affinity to o(2) |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8001951/ https://www.ncbi.nlm.nih.gov/pubmed/33805826 http://dx.doi.org/10.3390/antiox10030451 |
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