Features of ozone effect on oxygen-dependent processes in the blood under hypoxic conditions

2021 ◽  
Vol 20 (3) ◽  
pp. 70-76
Author(s):  
V. V. Zinchuk ◽  
E. S. Biletskaya
Keyword(s):  
Malonic Dialdehyde ◽  
Oxygen Affinity ◽  
Diene Conjugates ◽  
Physiological Factor ◽  
Sodium Hydrosulfide ◽  
Hypoxic Conditions ◽  
Hemoglobin Oxygen Affinity ◽  
Gaseous Transmitters ◽  
Dependent Processes

Introduction. Ozone is a physiological factor that can change hemoglobin oxygen affinity and the formation of gaseous transmitters (NO, H2S). The aim is to study the effect of ozone with gaseous transmitters donors on oxygen-dependent processes in the blood under hypoxic conditions in vitro. Materials and methods. Blood samples were divided into 6 groups of 3 ml each. Groups 2, 4, 5, 6 were pretreated with a deoxygenating gas mixture (5.5 % CO2; 94.5 % N2). In groups 3, 4, 5, 6, ozonized isotonic sodium chloride solution (with an ozone concentration of 6 mg/l) was added, and in groups 5 and 6, the donors of gas transmitters nitroglycerin and sodium hydrosulfide, respectively, were additionally introduced. Results. Pre-deoxygenation reduces the effect of ozone on oxygen transport in the blood. Nitroglycerin prevents this effect. The action of ozone under hypoxic conditions leads to an increase of content of NO3-/NO2- and H2S, and combination with nitroglycerin and sodium hydrosulfide increase these parameters. Deoxygenation due to ozone reduces parameters of lipid peroxidation (malonic dialdehyde, diene conjugates), retinol and α-tocopherol, and the same result in the nitroglycerin group. Conclusion. Under hypoxic conditions, a decrease in the effect of ozone on oxygen-dependent processes is reported. Nitroglycerin reduces its manifestation, while sodium hydrosulfide does not have a similar effect.

scholarly journals Analysis of the relationship between hemoglobin-oxygen affinity and lipid peroxidation during fever.

1995 ◽  
Vol 42 (1) ◽  
pp. 69-74 ◽  
Author(s):  
M V Borisiuk ◽  
V V Zinchuk
Keyword(s):  
Lipid Peroxidation ◽  
Malonic Dialdehyde ◽  
Oxygen Affinity ◽  
Alpha Tocopherol ◽  
Diene Conjugates ◽  
Tocopherol Concentration ◽  
Hemoglobin Oxygen Affinity ◽  
The Relationship ◽  
Free Radical Lipid Oxidation ◽  
Oxyhemoglobin Dissociation

Endogenous hyperthermia was induced in rabbits by i.v. pyrogenal administration. Hemoglobin-oxygen affinity and parameters of free radical lipid oxidation in plasma and red blood cells were measured. The content of diene conjugates, malonic dialdehyde and Schiff bases were determined at a pyrogenal dose of 4 minimal pyrogenic doses/kg, and iron-initiated chemiluminescence, catalase activity and alpha-tocopherol concentration were determined at 6 minimal pyrogenic doses/kg. A rightward shift of the real oxyhemoglobin dissociation curve and activation of lipid peroxidation were observed. Relationships between the parameters measured were analyzed. Decreased hemoglobin-oxygen affinity is considered to be a possible mechanism of activation of free radicals during fever.

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.

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.

scholarly journals Autosomal Dominant familial erythrocytosis due to autonomous erythropoietin production

Blood ◽  
1981 ◽  
Vol 58 (6) ◽  
pp. 1155-1158 ◽  
Author(s):  
CW Distelhorst ◽  
DS Wagner ◽  
E Goldwasser ◽  
JW Adamson
Keyword(s):  
Autosomal Dominant ◽  
Cell Mass ◽  
Family Members ◽  
Oxygen Affinity ◽  
Erythropoietin Production ◽  
Affected Family Member ◽  
Hemoglobin Oxygen Affinity ◽  
Oxygen Carrying Capacity ◽  
Serum Erythropoietin

Abstract A family is described in which four members spanning three consecutive generations have erythrocytosis associated with a normal hemoglobin oxygen affinity. When bone marrow from one affected family member was cultured in vitro, erythroid colonies formed only when erythropoietin was added to the culture. Serum erythropoietin, measured by radioimmunoassay, was significantly elevated above normal in each of the affected family members. Bioassayable erythropoietin was detected in the urine of two of the three affected family members. In two of the affected family members, erythropoietin was measured in serum by radioimmunoassay and in urine by bioassay before and for 4 days following an isovolemic phlebotomy, which reduced the red cell mass by 20%. Neither serum nor urinary erythropoietin levels changes following phlebotomy. The erythrocytosis in this family appears to be secondary to inappropriately increased erythropoietin production unassociated with a decrease in the blood oxygen-carrying capacity. This is the first instance in which autonomous erythropoietin production appears to be inherited on an autosomal dominant basis.

Hypoxia, Hormones, and Red Blood Cell Function in Chick Embryos

Physiology ◽  
2003 ◽  
Vol 18 (2) ◽  
pp. 77-82 ◽  
Author(s):  
Stefanie Dragon ◽  
Rosemarie Baumann
Keyword(s):  
Blood Cell ◽  
Red Blood Cell ◽  
Adrenergic Receptor ◽  
Cell Function ◽  
Oxygen Affinity ◽  
Terminal Differentiation ◽  
Receptor Activation ◽  
Avian Embryos ◽  
Hypoxic Conditions ◽  
Hemoglobin Oxygen Affinity

The red blood cell function of avian embryos is regulated by cAMP. Adenosine A2A and β-adrenergic receptor activation during hypoxic conditions cause changes in the hemoglobin oxygen affinity and CO2 transport. Furthermore, experimental evidence suggests a general involvement of cAMP in terminal differentiation of avian erythroblasts.

scholarly journals Dose- and Sex-Dependent Changes in Hemoglobin Oxygen Affinity by the Micronutrient 5-Hydroxymethylfurfural and α-Ketoglutaric Acid

Nutrients ◽  
2021 ◽  
Vol 13 (10) ◽  
pp. 3448
Author(s):  
Simon Woyke ◽  
Norbert Mair ◽  
Astrid Ortner ◽  
Thomas Haller ◽  
Marco Ronzani ◽  
...  
Keyword(s):  
Linear Regression Analysis ◽  
Oxygen Affinity ◽  
Nutritional Supplement ◽  
Hill Coefficient ◽  
Therapeutic Effects ◽  
Oxygen Dissociation ◽  
Hemoglobin Oxygen Affinity ◽  
Clinical Conditions

5-Hydroxymethylfurfural (5-HMF) is known to increase hemoglobin oxygen affinity (Hb–O2 affinity) and to induce a left shift of the oxygen dissociation curve (ODC). It is under investigation as a therapeutic agent in sickle cell anemia and in conditions where pulmonary oxygen uptake is deteriorated or limited (e.g., various clinical conditions or altitude exposure). The combination of 5-HMF and α-ketoglutaric acid (αKG) is commercially available as a nutritional supplement. To further elucidate dose effects, ODCs were measured in vitro in venous whole blood samples of 20 healthy volunteers (10 female and 10 male) after the addition of three different doses of 5-HMF, αKG and the combination of both. Linear regression analysis revealed a strong dose-dependent increase in Hb–O2 affinity for 5-HMF (R2 = 0.887; p < 0.001) and the commercially available combination with αKG (R2 = 0.882; p < 0.001). αKG alone increased Hb–O2 affinity as well but to a lower extent. Both the combination (5-HMF + αKG) and 5-HMF alone exerted different P50 and Hill coefficient responses overall and between sexes, with more pronounced effects in females. With increasing Hb–O2 affinity, the sigmoidal shape of the ODC was better preserved by the combination of 5-HMF and αKG than by 5-HMF alone. Concerning the therapeutic effects of 5-HMF, this study emphasizes the importance of adequate dosing in various physiological and clinical conditions, where a left-shifted ODC might be beneficial. By preserving the sigmoidal shape of the ODC, the combination of 5-HMF and αKG at low (both sexes) and medium (males only) doses might be able to better maintain efficient oxygen transport, particularly by mitigating potentially deteriorated oxygen unloading in the tissue. However, expanding knowledge on the interaction between 5-HMF and Hb–O2 affinity in vitro necessitates further investigations in vivo to additionally assess pharmacokinetic mechanisms.

Blood Gases of the Tench (Tinca tinca) in Well Aerated and Oxygen-Deficient Waters

1974 ◽  
Vol 60 (1) ◽  
pp. 71-83 ◽  
Author(s):  
F. B. EDDY
Keyword(s):  
Venous Blood ◽  
Oxygen Affinity ◽  
Blood Gases ◽  
Mean Value ◽  
Hypoxic Conditions ◽  
Arterial Blood ◽  
The Mean ◽  
Tench Tinca Tinca

1. The respiration of tench at 13°C was investigated, particular attention being given to the role of the blood in uptake and transport of oxygen. 2. In well aerated water the mean value for arterial blood was 36 mmHg, for PCOCO2 3.3 mmHg and for pH 8.16; the respective venous values were 7 mmHg, 5 mmHg and 8.08. Arterial blood averaged about 75% and venous blood about 40° oxygen saturation. The mean value for oxygen uptake was 0.5 ml/min/kg and for ventilation volume 132/ml/mm/kg. 3. The oxygen tension and the percentage saturation of the blood determined in vivo are discussed in terms of the oxygen dissociation curve determined in vitro. 4. When the environmental POO2 was decreased, tench responded by increasing breathing rate and ventilation volume. Arterial POO2 and PCOCO2 decreased but arterial pH tended to remain steady. There was also a significant increase in blood lactate. 5. That tenth can withstand severe hypoxic conditions is attributed to blood of high oxygen affinity and the ability to maintain a favourable acid-base status in the blood for oxygen transport. 6. Respiration in tench is compared with that in other fish species.

GTx011, a Potent Allosteric Modifier Of Hemoglobin Oxygen Affinity, Delays Polymerization and Prevents Sickling

Blood ◽  
2013 ◽  
Vol 122 (21) ◽  
pp. 316-316 ◽  
Author(s):  
Kobina Dufu ◽  
Donna Oksenberg ◽  
Brian Metcalf ◽  
Uma Sinha
Keyword(s):  
Blood Cells ◽  
Globin Gene ◽  
Oxygen Affinity ◽  
Potassium Phosphate ◽  
Experimental System ◽  
Dependent Manner ◽  
Employment Equity ◽  
Hemoglobin Oxygen Affinity ◽  
Equity Ownership

Abstract Sickle cell disease (SCD) is an inherited disorder caused by a point mutation in the β-globin gene leading to formation of hemoglobin S (HbS). A primary and obligatory event in the molecular pathogenesis of SCD is the polymerization of deoxygenated HbS leading to sickling of red blood cells (RBCs). Prolonging the oxygenation of HbS should in principle delay polymerization relative to transit time through microcirculation, thus avoiding sickling. Discovered by Global Blood Therapeutics, GTx011 is a novel orally available small molecule that demonstrates desirable pharmacokinetics in multiple species. In addition, GTx011 binding to HbS produces concentration-dependent left shifts in partial oxygen pressure (p50) of oxygen equilibrium curves, indicating an increase in oxygen affinity. We report here that GTx011 delays in vitro polymerization and prevents sickling. GTx011 was evaluated in an adapted version of the polymerization assay described by Adachi et al. [Blood Cells (1982) 8:213-224]. Purified HbS (pre-incubated with GTx011) in 1.8 M potassium phosphate was passively de-oxygenated, followed by an induction of polymerization via temperature jump from 4°C to 37°C. Polymerization was quantified by measuring turbidity of the HbS solution under continued hypoxia. For sickling experiments, RBCs pre-incubated with GTx011 were subjected to hypoxia (pO2 of ∼30 mmHg) for 0.5 hr and subsequently imaged using a light microscope. In de-sickling experiments, RBCs were first sickled under hypoxia and then treated with GTx011 under continued hypoxia (2 hr) before acquiring images of cells. The percentage of sickled cells in each image was quantified using CellVigene software. GTx011 delayed HbS polymerization in a dose-dependent manner. The delay profile was similar to that of CO-liganded HbA, a well characterized intracellular inhibitor of HbS polymerization. Moreover, GTx011 prevented sickling of RBCs under hypoxia suggesting that GTx011 has the ability to prevent intracellular HbS polymerization. It should be noted that in this experimental system, RBCs were exposed to hypoxia for a relatively longer period of time than typical RBC transit times through microcirculation. Interestingly, GTx011 also reversed sickling of pre-sickled RBCs. The ability of GTx011 to de-sickle RBCs suggests that it may promote transition from the low affinity HbS (T-state HbS) into its high affinity conformer (R-state HbS), a form that is not incorporated into HbS polymers. Thus, by stabilizing the oxy (R) conformation of HbS, GTx011 has the potential to be a therapeutic agent for prevention of HbS polymerization and sickling in SCD patients. Table 1 Assay Polymerization Sickling De-sickling Unit DT cpd -DT HbS (min) (% sickled) (% sickled) [HbS] 50 µM ∼1 mM (20% HCT) ∼1 mM (20% HCT) [Cpd] 25 µM 50 µM 100 µM 1 mM 2 mM 5 mM 1 mM 2 mM 5 mM GTx011 3.9 12.8 22.9 41 33 28 57 34 31 5-HMF 1 1.8 6.3 76 65 50 97 96 89 No Cpd 0 0 0 85 85 85 96 96 96 Table 2 Assay Polymerization Unit DT HbS/HbA -DT HbS (min) [Hb] 50 µM % HbA-CO 20% 30% 40% HbA-CO 2.3 11.8 16.8 Disclosures: Dufu: Global Blood Therapeutics: Employment, Equity Ownership. Sinha:Global Blood Therapeutics: Employment, Equity Ownership.

scholarly journals GBT440 reverses sickling of sickled red blood cells under hypoxic conditions in vitro

2018 ◽  
Vol 10 (2) ◽  
Author(s):  
Kobina Dufu ◽  
Donna Oksenberg
Keyword(s):  
Sickle Cell Disease ◽  
Red Blood Cells ◽  
Sickle Cell ◽  
Blood Cells ◽  
Oxygen Affinity ◽  
Microvascular Blood Flow ◽  
Cell Disease ◽  
Hypoxic Conditions

Sickle cell disease is characterized by hemolytic anemia, vasoocclusion and early mortality. Polymerization of hemoglobin S followed by red blood cell sickling and subsequent vascular injury are key events in the pathogenesis of sickle cell disease. Sickled red blood cells are major contributors to the abnormal blood rheology, poor microvascular blood flow and endothelial injury in sickle cell disease. Therefore, an agent that can prevent and or reverse sickling of red blood cells, may provide therapeutic benefit for the treatment of sickle cell disease. We report here that GBT440, an anti-polymerization agent being developed for the chronic treatment of sickle cell disease, increases hemoglobin oxygen affinity and reverses in vitro sickling of previously sickled red blood cells under hypoxic conditions. Our results suggest that besides preventing sickling of red blood cells, GBT440 may mitigate vasoocclusion and microvascular dysfunction by reversing sickling of circulating sickled red blood cells in vivo.

scholarly journals Participation of melatonin in regulation of blood oxygen-transport function in oxidative stress induced by injection of lipopolisaccharide

2017 ◽  
Vol 63 (6) ◽  
pp. 520-526 ◽  
Author(s):  
V.V. Zinchuk ◽  
M.E. Firago
Keyword(s):  
Oxidative Stress ◽  
Hydrogen Sulfide ◽  
Oxygen Transport ◽  
Oxygen Affinity ◽  
Nitrogen Monoxide ◽  
Blood Oxygen ◽  
Transport Function ◽  
Blood Oxygen Saturation ◽  
Sodium Hydrosulfide ◽  
Hemoglobin Oxygen Affinity

The contribution of melatonin to the regulatoin of the blood oxygen transport function was studied during oxidative stress induced by a triple injection of lipopolysaccharide (at a dose of 5 mg/kg) in conditions of erythropoietin and gasetransmitters (nitrogen monoxide, hydrogen sulfide) action. In the experimental groups, intraperitoneal injections of melatonin (5 mg/kg), erythropoietin (1000 U/kg), hydrogen sulfide donor (NaHS 5 mg/kg), and L-arginine (100 mg/kg), were performed. The use of melatonin alone or in combination with erythropoietin, sodium hydrosulfide or L-arginine led to a decrease in lipid peroxidation products and an increase in the antioxidant protection. Melatonin, during lipopolysaccharide administration, caused changes of blood oxygen transport function: blood oxygen saturation increased, hemoglobin oxygen affinity increased. The modifying effect of melatonin on the blood oxygen transport function in combination with erythropoietin and gastransmitters did not exceed the effect of melatonin alone.

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