Role of diffusion of oxygen in the respiration of tissues at different temperatures

1965 ◽  
Vol 20 (4) ◽  
pp. 637-646 ◽  
Author(s):  
Douglas A. Farr ◽  
Frederick A. Fuhrman
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Absolute Temperature ◽  
Rat Diaphragm ◽  
Tissue Slices ◽  
Straight Line ◽  
Mammalian Tissues ◽  
Different Temperatures

The hypothesis is presented that rates of respiration of sheets and slices of mammalian tissues as measured in vitro are usually lower than the true ones because of inadequate oxygenation in thick preparations and excessive damage to cells in thin ones. Data to support the hypothesis were obtained by a study of Qo2 as a function of temperature. When particles were small enough (avian red blood cells and brain homogenates) that diffusion of oxygen did not limit Qo2, a plot of log Qo2 versus 1/T (T = absolute temperature) yielded a straight line. However, when sheets and slices of tissues were used, such plots yielded lines whose slopes decreased with increase in temperature. For rat diaphragm, oxygenation appeared to be inadequate above 18 C. For rat liver, equations are presented for correcting Qo2 for damage caused by slicing and for inadequate oxygenation at higher temperatures. Data for respiration of tissues in 10% oxygen and at 2 atm oxygen pressure supported the hypothesis. oxygen tension; tissue slices—limiting thickness; tissue slices—thickness and Qo2 Submitted on May 5, 1964

scholarly journals Antagonists of the system L neutral amino acid transporter (LAT) promote endothelial adhesivity of human red blood cells

2017 ◽  
Vol 117 (07) ◽  
pp. 1402-1411 ◽  
Author(s):  
Laura Beth Mann Dosier ◽  
Vikram J. Premkumar ◽  
Hongmei Zhu ◽  
Izzet Akosman ◽  
Michael F. Wempe ◽  
...  
Keyword(s):  
Amino Acid ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Amino Acid Transporter ◽  
Neutral Amino Acid ◽  
Neutral Amino Acid Transporter ◽  
System L

SummaryThe system L neutral amino acid transporter (LAT; LAT1, LAT2, LAT3, or LAT4) has multiple functions in human biology, including the cellular import of S-nitrosothiols (SNOs), biologically active derivatives of nitric oxide (NO). SNO formation by haemoglobin within red blood cells (RBC) has been studied, but the conduit whereby a SNO leaves the RBC remains unidentified. Here we hypothesised that SNO export by RBCs may also depend on LAT activity, and investigated the role of RBC LAT in modulating SNO-sensitive RBC-endothelial cell (EC) adhesion. We used multiple pharmacologic inhibitors of LAT in vitro and in vivo to test the role of LAT in SNO export from RBCs and in thereby modulating RBC-EC adhesion. Inhibition of human RBC LAT by type-1-specific or nonspecific LAT antagonists increased RBC-endothelial adhesivity in vitro, and LAT inhibitors tended to increase post-transfusion RBC sequestration in the lung and decreased oxygenation in vivo. A LAT1-specific inhibitor attenuated SNO export from RBCs, and we demonstrated LAT1 in RBC membranes and LAT1 mRNA in reticulocytes. The proadhesive effects of inhibiting LAT1 could be overcome by supplemental L-CSNO (S-nitroso-L-cysteine), but not D-CSNO or L-Cys, and suggest a basal anti-adhesive role for stereospecific intercellular SNO transport. This study reveals for the first time a novel role of LAT1 in the export of SNOs from RBCs to prevent their adhesion to ECs. The findings have implications for the mechanisms of intercellular SNO signalling, and for thrombosis, sickle cell disease, and post-storage RBC transfusion, when RBC adhesivity is increased.

scholarly journals Phagocytosis of phenylhydrazine oxidized and G-6-PD-deficient red blood cells: the role of cell-bound immunoglobulins

Blood ◽  
1991 ◽  
Vol 78 (7) ◽  
pp. 1818-1825 ◽  
Author(s):  
S Horn ◽  
N Bashan ◽  
J Gopas
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Protein A ◽  
Fluorescein Isothiocyanate ◽  
Fold Increase ◽  
Fc Receptor ◽  
Autologous Serum ◽  
Murine Macrophages

Abstract In this study, the role of Igs in the recognition and removal of oxidatively damaged human red blood cells (RBCs) was investigated. Phagocytosis of normal RBCs exposed to the oxidative hemolytic agent phenylhydrazine (Phz) and of glucose-6-phosphate dehydrogenase (G6PD)- deficient RBCs by murine macrophages was examined. A 40-fold increase in phagocytosis of RBCs treated with 3 mmol/L Phz was obtained both in the absence and presence of autologous serum, indicating that binding of autologous antibodies to the oxidized cells is not essential for phagocytosis. Yet, a basal number of IgG molecules was found to be present on the RBCs, as determined both by binding of 125I protein A and fluorescein isothiocyanate-antihuman Ig to the cells. Macrophage Fc receptors were found to be involved in the recognition of the RBCs, because phagocytosis was partially inhibited by incubating macrophages with bovine serum albumin (BSA) anti-BSA complexes, aIg (aggregated Igs), and anti-Fc receptor II monoclonal antibodies. Galactose/mannose inhibited phagocytosis of oxidized RBCs additively to aIg. Because phagocytosis was decreased when Phz-RBCs were incubated with F(ab')2 fragments of antihuman antibodies, it is suggested that the basal amount of Igs bound to the cells plays a role in the recognition of Phz- RBCs. G6PD-deficient RBCs were recognized and phagocytosed by murine macrophages without preexposure to oxidants in vitro (mean of 19 RBCs/100 macrophages). This phagocytosis was not affected by the addition of serum and was inhibited by incubating macrophages with galactose/mannose and the various Fc receptor blockers. A positive correlation between hemoglobin content and the number of cell-bound Igs to each patient erythrocytes was found. These results support the involvement of both an Fc and a lectin-like macrophage receptor in the recognition and phagocytosis of Phz-oxidized and G6PD-deficient RBCs and suggest opsonization as a possible physiologic process for the removal of severe damaged RBCs.

scholarly journals Cytoadherence of Plasmodium berghei-Infected Red Blood Cells to Murine Brain and Lung Microvascular Endothelial CellsIn Vitro

2013 ◽  
Vol 81 (11) ◽  
pp. 3984-3991 ◽  
Author(s):  
Fatima El-Assaad ◽  
Julie Wheway ◽  
Andrew John Mitchell ◽  
Jinning Lou ◽  
Nicholas Henry Hunt ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Red Blood Cells ◽  
Plasmodium Berghei ◽  
Blood Cells ◽  
Content Type ◽  
Murine Brain ◽  
Microvascular Endothelial ◽  
Mixed Stage

ABSTRACTSequestration of infected red blood cells (iRBC) within the cerebral and pulmonary microvasculature is a hallmark of human cerebral malaria (hCM). The interaction between iRBC and the endothelium in hCM has been studied extensively and is linked to the severity of malaria. Experimental CM (eCM) caused byPlasmodium bergheiANKA reproduces most features of hCM, although the sequestration of RBC infected byP. bergheiANKA (PbA-iRBC) has not been completely delineated. The role of PbA-iRBC sequestration in the severity of eCM is not well characterized. Using static and flow cytoadherence assays, we provide the first directin vitroevidence for the binding of PbA-iRBC to murine brain and lung microvascular endothelial cells (MVEC). We found that basal PbA-iRBC cytoadherence to MVECs was significantly higher than that of normal red blood cells (NRBC) and of RBC infected withP. bergheiK173 (PbK173-iRBC), a strain that causes noncerebral malaria (NCM). MVEC prestimulation with tumor necrosis factor (TNF) failed to promote any further significant increase in mixed-stage iRBC adherence. Interestingly, enrichment of the blood for mature parasites significantly increased PbA-iRBC binding to the MVECs prestimulated with TNF, while blockade of VCAM-1 reduced this adhesion. Our study provides evidence for the firm, flow-resistant binding to endothelial cells of iRBC from strain ANKA-infected mice, which develop CM, and for less binding of iRBC from strain K173-infected mice, which develop NCM. An understanding ofP. bergheicytoadherence may help elucidate the importance of sequestration in the development of CM and aid the development of antibinding therapies to help reduce the burden of this syndrome.

scholarly journals Favism: impairment of proteolytic systems in red blood cells

Blood ◽  
1987 ◽  
Vol 69 (6) ◽  
pp. 1753-1758
Author(s):  
A Morelli ◽  
M Grasso ◽  
T Meloni ◽  
G Forteleoni ◽  
E Zocchi ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Time Course ◽  
Acid Proteinase ◽  
Heinz Bodies ◽  
Calcium Loading ◽  
Endopeptidase Activity ◽  
Glucose 6 Phosphate Dehydrogenase

Red blood cells (RBC) from favic patients are characterized by (a) severe oxidative damage (contributed by autoxidation of divicine and isouramil, two pyrimidine aglycones present in fava beans) and (b) greatly increased calcium levels. In vitro, both autoxidation of divicine and calcium loading produced marked alterations of proteolytic systems in intact RBC. Specifically, autoxidizing divicine inactivated procalpain, the proenzyme species of calcium-activated cytosolic neutral proteinase, or calpain. Inactivation was much greater with glucose-6-phosphate dehydrogenase (G6PD)-deficient RBC than with normal RBC. On the other hand, loading of normal and G6PD-deficient RBC with calcium resulted in conversion of procalpain to calpain and eventual autoproteolytic inactivation of calpain itself, and extensive release of acid endopeptidase activity from the membranes into the cytosol. Damaged RBC from favic patients had significantly lowered procalpain activity and an abnormal subcellular distribution of acid proteinase activity that was found mostly in the cytosol. When purified calpain was incubated with membranes from acetylphenylhydrazine (APH)-treated RBC, significant proteolysis was observed affecting mostly band 3 and hemoglobin chains, ie, the two proteins involved in the onset of aggregation of Heinz bodies. Moreover, exposure of intact RBC to 20 mmol/L APH induced depletion of procalpain activity for which the time course was inversely related to formation of Heinz bodies. These findings support the role of procalpain in protecting G6PD-deficient RBC from oxidant-induced Heinz body formation and imply that exhaustion of the procalpain-calpain system is an important step in the mechanisms of RBC damage and destruction in favism.

scholarly journals New Role of Red Blood Cells in Absorption of DNA Bearing Tumorigenic Mutations from Lung Cancer Tissue

2021 ◽  
Author(s):  
Nai-Xin Liang ◽  
Tao Wang ◽  
Cong Zhang ◽  
Zichen Jiao ◽  
Tianqiang Song ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Red Blood Cells ◽  
Cancer Cell ◽  
Blood Cells ◽  
Early Stage ◽  
Digital Pcr ◽  
Cancer Tissue ◽  
Lung Cancer Patients

AbstractRed blood cells (RBC) are commonly assumed to be vehicles for oxygen, carbon dioxide, and cells’ metabolic byproducts. In this study, we investigated whether RBC may contain cancer-cell derived DNA and whether such cargo may be used as a biomarker for detecting cancer. Using an in vitro co-culture system, we showed that RBC could absorb DNA bearing tumorigenic mutations from cancer cell lines. Next, we demonstrated that we could detect common genetic mutations, including EGFR 19 deletion, L858R, and KRAS G12 in RBC collected from early-stage non-small cell lung cancer patients. We were able to repeat our finding using both next-generation sequencing and droplet digital PCR. Our study highlights a new biological phenomenon involving RBC and their translational potential as a novel liquid biopsy technology platform that can be used for early cancer screening.

scholarly journals Favism: impairment of proteolytic systems in red blood cells

Blood ◽  
1987 ◽  
Vol 69 (6) ◽  
pp. 1753-1758 ◽  
Author(s):  
A Morelli ◽  
M Grasso ◽  
T Meloni ◽  
G Forteleoni ◽  
E Zocchi ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Time Course ◽  
Acid Proteinase ◽  
Heinz Bodies ◽  
Calcium Loading ◽  
Endopeptidase Activity ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract Red blood cells (RBC) from favic patients are characterized by (a) severe oxidative damage (contributed by autoxidation of divicine and isouramil, two pyrimidine aglycones present in fava beans) and (b) greatly increased calcium levels. In vitro, both autoxidation of divicine and calcium loading produced marked alterations of proteolytic systems in intact RBC. Specifically, autoxidizing divicine inactivated procalpain, the proenzyme species of calcium-activated cytosolic neutral proteinase, or calpain. Inactivation was much greater with glucose-6-phosphate dehydrogenase (G6PD)-deficient RBC than with normal RBC. On the other hand, loading of normal and G6PD-deficient RBC with calcium resulted in conversion of procalpain to calpain and eventual autoproteolytic inactivation of calpain itself, and extensive release of acid endopeptidase activity from the membranes into the cytosol. Damaged RBC from favic patients had significantly lowered procalpain activity and an abnormal subcellular distribution of acid proteinase activity that was found mostly in the cytosol. When purified calpain was incubated with membranes from acetylphenylhydrazine (APH)-treated RBC, significant proteolysis was observed affecting mostly band 3 and hemoglobin chains, ie, the two proteins involved in the onset of aggregation of Heinz bodies. Moreover, exposure of intact RBC to 20 mmol/L APH induced depletion of procalpain activity for which the time course was inversely related to formation of Heinz bodies. These findings support the role of procalpain in protecting G6PD-deficient RBC from oxidant-induced Heinz body formation and imply that exhaustion of the procalpain-calpain system is an important step in the mechanisms of RBC damage and destruction in favism.

scholarly journals Phagocytosis of phenylhydrazine oxidized and G-6-PD-deficient red blood cells: the role of cell-bound immunoglobulins

Blood ◽  
1991 ◽  
Vol 78 (7) ◽  
pp. 1818-1825
Author(s):  
S Horn ◽  
N Bashan ◽  
J Gopas
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Protein A ◽  
Fluorescein Isothiocyanate ◽  
Fold Increase ◽  
Fc Receptor ◽  
Autologous Serum ◽  
Murine Macrophages

In this study, the role of Igs in the recognition and removal of oxidatively damaged human red blood cells (RBCs) was investigated. Phagocytosis of normal RBCs exposed to the oxidative hemolytic agent phenylhydrazine (Phz) and of glucose-6-phosphate dehydrogenase (G6PD)- deficient RBCs by murine macrophages was examined. A 40-fold increase in phagocytosis of RBCs treated with 3 mmol/L Phz was obtained both in the absence and presence of autologous serum, indicating that binding of autologous antibodies to the oxidized cells is not essential for phagocytosis. Yet, a basal number of IgG molecules was found to be present on the RBCs, as determined both by binding of 125I protein A and fluorescein isothiocyanate-antihuman Ig to the cells. Macrophage Fc receptors were found to be involved in the recognition of the RBCs, because phagocytosis was partially inhibited by incubating macrophages with bovine serum albumin (BSA) anti-BSA complexes, aIg (aggregated Igs), and anti-Fc receptor II monoclonal antibodies. Galactose/mannose inhibited phagocytosis of oxidized RBCs additively to aIg. Because phagocytosis was decreased when Phz-RBCs were incubated with F(ab')2 fragments of antihuman antibodies, it is suggested that the basal amount of Igs bound to the cells plays a role in the recognition of Phz- RBCs. G6PD-deficient RBCs were recognized and phagocytosed by murine macrophages without preexposure to oxidants in vitro (mean of 19 RBCs/100 macrophages). This phagocytosis was not affected by the addition of serum and was inhibited by incubating macrophages with galactose/mannose and the various Fc receptor blockers. A positive correlation between hemoglobin content and the number of cell-bound Igs to each patient erythrocytes was found. These results support the involvement of both an Fc and a lectin-like macrophage receptor in the recognition and phagocytosis of Phz-oxidized and G6PD-deficient RBCs and suggest opsonization as a possible physiologic process for the removal of severe damaged RBCs.

scholarly journals BIOMAGNETISM AS FACTOR IN RED BLOOD CELLS DEFORMATION

2018 ◽  
Vol 6 (12) ◽  
pp. 46-57
Author(s):  
Abraham A.
Keyword(s):  
Red Blood Cells ◽  
Optical Tweezers ◽  
Cross Talk ◽  
Blood Cells ◽  
Hair Shaft ◽  
In Vitro Experiments ◽  
Hydrophobic Properties ◽  
Blood Smears

The purpose of this manuscript is to report in vitro experiments showing the role of pulsed biomagnetic fields tissues cross-talk between Red Blood Cells (RBCs) and human hairs. Both tissues have been reported to express magnetic properties, ie: RBCs diamagnetic and paramagnetic forces and the hair follicle pulsed diamagnetic forces. This biomagnetic cross-talk is reported as a novel factor in RBCs deformation. In the in vitro experimental model herein used, other forces such as keratin biomagnetism, hydrophilic and hydrophobic properties of the hair shaft may also play a role in the deformation. Presently teardrop red blood cells found in blood smears; and oriented in the same direction are attributed to mechanical artifacts introduced during slide preparations. The data presented in this manuscript supports the new principle of biomagnetic cross talk forces as factor in replicating RBCs deformities.as described in Optical Tweezers Trapping.

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