Oxygen binding of single red blood cells of the annelid bloodwormGlycera dibranchiata

1989 ◽  
Vol 249 (2) ◽  
pp. 144-149 ◽  
Author(s):  
C. P. Mangum ◽  
J. M. Colacino ◽  
T. L. Vandergon
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Oxygen Binding

scholarly journals Irreversible alterations in the hemoglobin structure affect oxygen binding in human packed red blood cells

2020 ◽  
Vol 1867 (11) ◽  
pp. 118803 ◽  
Author(s):  
Ewa Szczesny-Malysiak ◽  
Jakub Dybas ◽  
Aneta Blat ◽  
Katarzyna Bulat ◽  
Kamil Kus ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Oxygen Binding ◽  
Packed Red Blood Cells

The structural and functional changes of blood cells and molecular components in diabetes mellitus

2017 ◽  
Vol 398 (4) ◽  
pp. 411-423 ◽  
Author(s):  
Leszek Szablewski ◽  
Anna Sulima
Keyword(s):  
Diabetes Mellitus ◽  
Red Blood Cells ◽  
Blood Cells ◽  
White Blood Cells ◽  
Neutrophil Function ◽  
Cardiovascular Complications ◽  
Oxygen Binding ◽  
Functional Changes ◽  
Coronary Syndrome ◽  
Patients With Diabetes

Abstract It is known fact that diabetes mellitus (DM) affects blood cells. Changes in the erythrocyte membrane, disorder in hemoglobin oxygen-binding and modification in mechanical characteristics, are effects of hyperglycemia on red blood cells. Altered susceptibility infection of patients with diabetes has been ascribed to a depression in the function of polymorphonuclear leukocytes. Neutrophil function in patients with diabetes with good glucose control is slightly different than in healthy ones. DM causes significant changes in lymphocytes metabolism and their functions. Patients with diabetes, presenting with acute coronary syndrome, are at higher risk of cardiovascular complications and recurrent ischemic events in comparison to non-diabetic counterparts. Various mechanisms, including endothelial dysfunction, platelet hyperactivity, and abnormalities in coagulation and fibrynolysis have been implicated for this increased atherothrombotic risk. There are many other alterations of blood cells due to DM. In the present review we focused on modifications of blood cells due to DM. Then, as a second point, we explored how the changes affect functions of red blood cells, white blood cells and platelets.

scholarly journals Improving Oxygen Binding of Desiccated Human Red Blood Cells

2016 ◽  
Vol 07 (02) ◽  
pp. 47-54 ◽  
Author(s):  
Steingrimur Stefansson ◽  
David S. Chung ◽  
Jamie Yoon ◽  
Won Seok Yoo ◽  
Young Wook Park ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Oxygen Binding ◽  
Human Red Blood Cells

scholarly journals The Influence of Oxidative Stress and Natural Antioxidants on Morphometric Parameters of Red Blood Cells, the Hemoglobin Oxygen Binding Capacity, and the Activity of Antioxidant Enzymes

2019 ◽  
Vol 2019 ◽  
pp. 1-12 ◽  
Author(s):  
Victor V. Revin ◽  
Natalia V. Gromova ◽  
Elvira S. Revina ◽  
Anastasia Yu. Samonova ◽  
Alexander Yu. Tychkov ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Antioxidant Enzymes ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Binding Capacity ◽  
Natural Antioxidants ◽  
Oxygen Binding ◽  
Wide Range ◽  
Oxidative Processes ◽  
Physical And Chemical

Using a wide range of different physical and chemical methods, it was found that the oxidative stress caused by addition of hydrogen peroxide to the incubation medium has a significant effect on the conformation of haematoporphyrin, influencing the oxygen-binding properties of haemoglobin in red blood cells. Morphofunctional characteristics of red blood cells change; in particular, we have observed the transformation of erythrocytes, their transition into echinocytes. In erythrocytes, in response to increased lipid peroxidation (LPO) antioxidant enzymes become active. The use of natural antioxidants (β-carotene and resveratrol) works towards reducting the level of oxidative processes. Resveratrol has the greatest antioxidant effect.

Resveratrol treatment induces redox stress in red blood cells: a possible role of caspase 3 in metabolism and anion transport

2010 ◽  
Vol 391 (9) ◽  
Author(s):  
Antonio Galtieri ◽  
Ester Tellone ◽  
Silvana Ficarra ◽  
Annamaria Russo ◽  
Ersilia Bellocco ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Caspase 3 ◽  
Conformational Transition ◽  
Reducing Power ◽  
Band 3 ◽  
Anion Transport ◽  
Heme Iron ◽  
Strong Impact ◽  
Oxygen Binding

AbstractResveratrol, an important phytoalexine found in many plants, has been shown to be significantly effective in the treatment of several pathological conditions such as cancer, coronary heart disease and osteoarthritis. This study focuses on the effects of this drug on human red blood cells. In particular, we have examined the influence of resveratrol on Band 3, the anion exchanger protein, and hemoglobin as a function of the oxygenation-deoxygenation cycle. Moreover, special attention has been given to the metabolic changes imposed by caspase 3 activation. Resveratrol has proved to lower superoxide production, thereby decreasing heme-iron oxidation and saving the reducing power required for met-hemoglobin reduction. Oxygen binding experiments showed that resveratrol interacts with hemoglobin, shifting the T→R conformational transition towards the higher-affinity R state. This might contribute to altering the metabolic balance of the cell through an intensification of the pentose phosphate pathway. Moreover, at high oxygenation levels of the erythrocytic hemoglobin, resveratrol induces a significant activation of caspase 3, the action of which on Band 3 has a strong impact on cellular metabolism and anion transport.

Oxygen binding by single red blood cells from the red-eared turtle Trachemys scripta

2001 ◽  
Vol 90 (5) ◽  
pp. 1679-1684 ◽  
Author(s):  
Sebastian Frische ◽  
Stefano Bruno ◽  
Angela Fago ◽  
Roy E. Weber ◽  
Andrea Mozzarelli
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Oxygen Affinity ◽  
Trachemys Scripta ◽  
Oxygen Binding ◽  
Binding Properties ◽  
Cell Variation ◽  
Insight Into

Oxygen-binding properties of single red blood cells from the red-eared turtle Trachemys scripta were measured by microspectrophotometry to describe the variation in oxygen affinity of red blood cells and to gain insight into the distribution of functionally different hemoglobins among red blood cells. Methodologically, this study represents the first report on the cell-to-cell variation in oxygen-binding properties based on oxygen-binding curves of single vertebrate red blood cells. The cells differed significantly with respect to oxygen affinity. Mean oxygen pressure at half saturation of the cells in a blood sample was found to be 20.1 ± 3.3 (SD) Torr. The distribution of oxygen affinities among red blood cells is unimodal, indicating that the two hemoglobins found in turtle blood are not segregated in distinct cells. Therefore, the functional interaction shown by these hemoglobins in vitro is likely to take place in vivo. The considerable variation in oxygen affinity between individual red blood cells calls for its incorporation in models of tissue oxygenation.

scholarly journals Phytoglobin: a novel nomenclature for plant globins accepted by the globin community at the 2014 XVIII conference on Oxygen-Binding and Sensing Proteins

F1000Research ◽  
2016 ◽  
Vol 5 ◽  
pp. 212 ◽  
Author(s):  
Robert Hill ◽  
Mark Hargrove ◽  
Raúl Arredondo-Peter
Keyword(s):  
Blood Cell ◽  
Red Blood Cells ◽  
Red Blood Cell ◽  
Classification System ◽  
Blood Cells ◽  
Research Community ◽  
Oxygen Binding ◽  
Name Change ◽  
Definition Of ◽  
Phylogenetic Scheme

Hemoglobin (Hb) is a heme-containing protein found in the red blood cells of vertebrates. For many years, the only known Hb-like molecule in plants was leghemoglobin (Lb). The discovery that other Hb-like proteins existed in plants led to the term “nonsymbiotic Hbs (nsHbs)” to differentiate them from the Lbs. While this terminology was adequate in the early stages of research on the protein, the complexity of the research in this area necessitates a change in the definition of these proteins to delineate them from red blood cell Hb. At the 2014 XVIII Conference on Oxygen-Binding and Sensing Proteins, the group devoted to the study of heme-containing proteins, this issue was discussed and a consensus was reached on a proposed name change. We propose Phytoglobin (Phytogb) as a logical, descriptive name to describe a heme-containing (Hb-like) protein found in plants. It will be readily recognized by the research community without a prolonged explanation of the origin of the term. The classification system that has been established can essentially remain unchanged substituting Phytogb in place of nsHb. Here, we present a guide to the new nomenclature, with reference to the existing terminology and a phylogenetic scheme, placing the known Phytogbs in the new nomenclature.

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