scholarly journals Piezo1-xerocytosis red cell metabolome shows impaired glycolysis and increased hemoglobin oxygen affinity

2021 ◽  
Vol 5 (1) ◽  
pp. 84-88
Author(s):  
Laurent Kiger ◽  
Lydie Oliveira ◽  
Corinne Guitton ◽  
Laurence Bendélac ◽  
Kaldoun Ghazal ◽  
...  
Keyword(s):  
Oxygen Affinity ◽  
Red Cell ◽  
Hemoglobin Oxygen Affinity

scholarly journals Mechanism of red cell 2,3-diphosphoglycerate increase in neonatal lambs

Blood ◽  
1983 ◽  
Vol 61 (5) ◽  
pp. 920-924 ◽  
Author(s):  
NA Noble ◽  
CA Jansen ◽  
PW Nathanielsz ◽  
KR Tanaka
Keyword(s):  
Oxygen Affinity ◽  
Glucose Consumption ◽  
Red Cell ◽  
Sequential Effects ◽  
Blood Ph ◽  
Tenfold Increase ◽  
Hemoglobin Oxygen Affinity ◽  
Ph Increase ◽  
Neonatal Lambs

Abstract The tenfold increase in red cell 2,3-diphosphoglycerate (DPG) concentration that occurs during the first 5 days of life in lambs is an important adaptation to extrauterine life. In lambs, DPG reduces hemoglobin oxygen affinity by the Bohr effect. Our data on 10 neonatal lambs suggest that the biochemical mechanism underlying this DPG increase involves the following: (1) a rise in plasma glucose from 40 to 100 mg/dl in the first 48 hr of life, which allows for increased glucose consumption in the highly glucose-permeable neonatal RBC; (2) a transitory rise in blood pH begins at birth, peaks at about 20 hr, and falls slightly; (3) the pH increase coincides with a threefold increase in RBC fructose-1,6-diphosphate (FDP) concentration due, we believe, to pH activation of phosphofructokinase; (4) glycolytic intermediates after the glyceraldehyde-3-phosphate dehydrogenase (GAPD) step do not rise in the first 24 hr of life, possibly due to insufficient inorganic phosphate (Pi), a substrate of GAPD; (5) plasma Pi increases from about 7 mg/dl at birth to 11 mg/dl at 72 hr, activates the GAPD, and FDP levels decline; and (6) the in vitro activity of the DPG synthetic enzyme, DPG mutase, is increased 12-fold in neonatal compared to adult RBC. We conclude that the postnatal rise in DPG is explained at least in part by the sequential effects of these metabolic changes.

What is the Clinical Importance of Alterations of the Hemoglobin Oxygen Affinity in Preserved Blood - Especially as Produced by Variations of Red Cell 2,3 DPG Content?

Vox Sanguinis ◽  
1978 ◽  
Vol 34 (2) ◽  
pp. 111-127 ◽  
Author(s):  
J.C. Bakker ◽  
Ernest Beutler ◽  
John A. Collins ◽  
R. Ben Dawson ◽  
Lars Garby ◽  
...  
Keyword(s):  
Oxygen Affinity ◽  
Clinical Importance ◽  
Red Cell ◽  
Hemoglobin Oxygen Affinity ◽  
2,3 Dpg

scholarly journals Mechanism of red cell 2,3-diphosphoglycerate increase in neonatal lambs

Blood ◽  
1983 ◽  
Vol 61 (5) ◽  
pp. 920-924 ◽  
Author(s):  
NA Noble ◽  
CA Jansen ◽  
PW Nathanielsz ◽  
KR Tanaka
Keyword(s):  
Oxygen Affinity ◽  
Glucose Consumption ◽  
Red Cell ◽  
Sequential Effects ◽  
Blood Ph ◽  
Tenfold Increase ◽  
Hemoglobin Oxygen Affinity ◽  
Ph Increase ◽  
Neonatal Lambs

The tenfold increase in red cell 2,3-diphosphoglycerate (DPG) concentration that occurs during the first 5 days of life in lambs is an important adaptation to extrauterine life. In lambs, DPG reduces hemoglobin oxygen affinity by the Bohr effect. Our data on 10 neonatal lambs suggest that the biochemical mechanism underlying this DPG increase involves the following: (1) a rise in plasma glucose from 40 to 100 mg/dl in the first 48 hr of life, which allows for increased glucose consumption in the highly glucose-permeable neonatal RBC; (2) a transitory rise in blood pH begins at birth, peaks at about 20 hr, and falls slightly; (3) the pH increase coincides with a threefold increase in RBC fructose-1,6-diphosphate (FDP) concentration due, we believe, to pH activation of phosphofructokinase; (4) glycolytic intermediates after the glyceraldehyde-3-phosphate dehydrogenase (GAPD) step do not rise in the first 24 hr of life, possibly due to insufficient inorganic phosphate (Pi), a substrate of GAPD; (5) plasma Pi increases from about 7 mg/dl at birth to 11 mg/dl at 72 hr, activates the GAPD, and FDP levels decline; and (6) the in vitro activity of the DPG synthetic enzyme, DPG mutase, is increased 12-fold in neonatal compared to adult RBC. We conclude that the postnatal rise in DPG is explained at least in part by the sequential effects of these metabolic changes.

Decrease in the red cell cofactor 2,3-diphosphoglycerate increases hemoglobin oxygen affinity in the hibernating brown bear Ursus arctos

2013 ◽  
Vol 304 (1) ◽  
pp. R43-R49 ◽  
Author(s):  
Inge G. Revsbech ◽  
Hans Malte ◽  
Ole Fröbert ◽  
Alina Evans ◽  
Stéphane Blanc ◽  
...  
Keyword(s):  
Ursus Arctos ◽  
Oxygen Affinity ◽  
Brown Bear ◽  
Temperature Sensitive ◽  
Red Cell ◽  
Brown Bears ◽  
Hemoglobin Oxygen Affinity ◽  
Free Ranging ◽  
Winter Hibernation

During winter hibernation, brown bears ( Ursus arctos) reduce basal O2 consumption rate to ∼25% compared with the active state, while body temperature decreases moderately (to ∼30°C), suggesting a temperature-independent component in their metabolic depression. To establish whether changes in O2 consumption during hibernation correlate with changes in blood O2 affinity, we took blood samples from the same six individuals of hibernating and nonhibernating free-ranging brown bears during winter and summer, respectively. A single hemoglobin (Hb) component was detected in all samples, indicating no switch in Hb synthesis. O2 binding curves measured on red blood cell lysates at 30°C and 37°C showed a less temperature-sensitive O2 affinity than in other vertebrates. Furthermore, hemolysates from hibernating bears consistently showed lower cooperativity and higher O2 affinity than their summer counterparts, regardless of the temperature. We found that this increase in O2 affinity was associated with a significant decrease in the red cell Hb-cofactor 2,3-diphosphoglycerate (DPG) during hibernation to approximately half of the summer value. Experiments performed on purified Hb, to which DPG had been added to match summer and winter levels, confirmed that the low DPG content was the cause of the left shift in the Hb-O2 equilibrium curve during hibernation. Levels of plasma lactate indicated that glycolysis is not upregulated during hibernation and that metabolism is essentially aerobic. Calculations show that the increase in Hb-O2 affinity and decrease in cooperativity resulting from decreased red cell DPG may be crucial in maintaining a fairly constant tissue oxygen tension during hibernation in vivo.

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