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A broad diversity in oxygen affinity to haemoglobin

Oxygen affinity to haemoglobin is indicated by the p50 value (pO(2) at 50% O(2)Hb) and critically determines cellular oxygen availability. Although high Hb-O(2) affinity can cause tissue hypoxia under conditions of well O(2) saturated blood, individual differences in p50 are commonly not considered...

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Autores principales: Balcerek, Björn, Steinach, Mathias, Lichti, Julia, Maggioni, Martina A., Becker, Philipp N., Labes, Robert, Gunga, Hanns-Christian, Persson, Pontus B., Fähling, Michael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7547706/
https://www.ncbi.nlm.nih.gov/pubmed/33037242
http://dx.doi.org/10.1038/s41598-020-73560-9
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author Balcerek, Björn
Steinach, Mathias
Lichti, Julia
Maggioni, Martina A.
Becker, Philipp N.
Labes, Robert
Gunga, Hanns-Christian
Persson, Pontus B.
Fähling, Michael
author_facet Balcerek, Björn
Steinach, Mathias
Lichti, Julia
Maggioni, Martina A.
Becker, Philipp N.
Labes, Robert
Gunga, Hanns-Christian
Persson, Pontus B.
Fähling, Michael
author_sort Balcerek, Björn
collection PubMed
description Oxygen affinity to haemoglobin is indicated by the p50 value (pO(2) at 50% O(2)Hb) and critically determines cellular oxygen availability. Although high Hb-O(2) affinity can cause tissue hypoxia under conditions of well O(2) saturated blood, individual differences in p50 are commonly not considered in clinical routine. Here, we investigated the diversity in Hb-O(2) affinity in the context of physiological relevance. Oxyhaemoglobin dissociation curves (ODCs) of 60 volunteers (18–40 years, both sexes, either endurance trained or untrained) were measured at rest and after maximum exercise (VO(2)max) test. At rest, p50 values of all participants ranged over 7 mmHg. For comparison, right shift of ODC after VO(2)max test, representing the maximal physiological range to release oxygen to the tissue, indicated a p50 difference of up to 10 mmHg. P50 at rest differs significantly between women and men, with women showing lower Hb-O(2) affinity that is determined by higher 2,3-BPG and BPGM levels. Regular endurance exercise did not alter baseline Hb-O(2) affinity. Thus, p50 diversity is already high at baseline level and needs to be considered under conditions of impaired tissue oxygenation. For fast prediction of Hb-O(2) affinity by blood gas analysis, only venous but not capillary blood samples can be recommended.
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spelling pubmed-75477062020-10-14 A broad diversity in oxygen affinity to haemoglobin Balcerek, Björn Steinach, Mathias Lichti, Julia Maggioni, Martina A. Becker, Philipp N. Labes, Robert Gunga, Hanns-Christian Persson, Pontus B. Fähling, Michael Sci Rep Article Oxygen affinity to haemoglobin is indicated by the p50 value (pO(2) at 50% O(2)Hb) and critically determines cellular oxygen availability. Although high Hb-O(2) affinity can cause tissue hypoxia under conditions of well O(2) saturated blood, individual differences in p50 are commonly not considered in clinical routine. Here, we investigated the diversity in Hb-O(2) affinity in the context of physiological relevance. Oxyhaemoglobin dissociation curves (ODCs) of 60 volunteers (18–40 years, both sexes, either endurance trained or untrained) were measured at rest and after maximum exercise (VO(2)max) test. At rest, p50 values of all participants ranged over 7 mmHg. For comparison, right shift of ODC after VO(2)max test, representing the maximal physiological range to release oxygen to the tissue, indicated a p50 difference of up to 10 mmHg. P50 at rest differs significantly between women and men, with women showing lower Hb-O(2) affinity that is determined by higher 2,3-BPG and BPGM levels. Regular endurance exercise did not alter baseline Hb-O(2) affinity. Thus, p50 diversity is already high at baseline level and needs to be considered under conditions of impaired tissue oxygenation. For fast prediction of Hb-O(2) affinity by blood gas analysis, only venous but not capillary blood samples can be recommended. Nature Publishing Group UK 2020-10-09 /pmc/articles/PMC7547706/ /pubmed/33037242 http://dx.doi.org/10.1038/s41598-020-73560-9 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Balcerek, Björn
Steinach, Mathias
Lichti, Julia
Maggioni, Martina A.
Becker, Philipp N.
Labes, Robert
Gunga, Hanns-Christian
Persson, Pontus B.
Fähling, Michael
A broad diversity in oxygen affinity to haemoglobin
title A broad diversity in oxygen affinity to haemoglobin
title_full A broad diversity in oxygen affinity to haemoglobin
title_fullStr A broad diversity in oxygen affinity to haemoglobin
title_full_unstemmed A broad diversity in oxygen affinity to haemoglobin
title_short A broad diversity in oxygen affinity to haemoglobin
title_sort broad diversity in oxygen affinity to haemoglobin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7547706/
https://www.ncbi.nlm.nih.gov/pubmed/33037242
http://dx.doi.org/10.1038/s41598-020-73560-9
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