scholarly journals Rhythmic glucose metabolism regulates the redox circadian clockwork in human red blood cells

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Ratnasekhar Ch ◽  
Guillaume Rey ◽  
Sandipan Ray ◽  
Pawan K. Jha ◽  
Paul C. Driscoll ◽  
...  
Keyword(s):  
Glucose Metabolism ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Mammalian Cells ◽  
Metabolic Flux ◽  
Pentose Phosphate ◽  
Human Red Blood Cells ◽  
Integral Process ◽  
Metabolic Oscillations ◽  
Human Rbcs

AbstractCircadian clocks coordinate mammalian behavior and physiology enabling organisms to anticipate 24-hour cycles. Transcription-translation feedback loops are thought to drive these clocks in most of mammalian cells. However, red blood cells (RBCs), which do not contain a nucleus, and cannot perform transcription or translation, nonetheless exhibit circadian redox rhythms. Here we show human RBCs display circadian regulation of glucose metabolism, which is required to sustain daily redox oscillations. We found daily rhythms of metabolite levels and flux through glycolysis and the pentose phosphate pathway (PPP). We show that inhibition of critical enzymes in either pathway abolished 24-hour rhythms in metabolic flux and redox oscillations, and determined that metabolic oscillations are necessary for redox rhythmicity. Furthermore, metabolic flux rhythms also occur in nucleated cells, and persist when the core transcriptional circadian clockwork is absent in Bmal1 knockouts. Thus, we propose that rhythmic glucose metabolism is an integral process in circadian rhythms.

scholarly journals Concanavalin A-mediated binding and sphering of human red blood cells by homologous monocytes.

1976 ◽  
Vol 144 (6) ◽  
pp. 1695-1700 ◽  
Author(s):  
D Guerry ◽  
M A Kenna ◽  
A D Schrieber ◽  
R A Cooper
Keyword(s):  
Blood Cell ◽  
Red Blood Cells ◽  
Concanavalin A ◽  
Blood Cells ◽  
Human Monocytes ◽  
Blood Monocytes ◽  
Con A ◽  
Peripheral Blood Monocytes ◽  
Human Red Blood Cells ◽  
Human Rbcs

Human red blood cells sensitized with concanavalin A became bound to homologous peripheral blood monocytes. Binding occured at a concentration of 10(5) molecules of tetrameric Con A per red blood cell (RBC) and increased with additional Con A. RBC binding began within 5 min and was maximal at 90 min. Phagocytosis of sensitized RBCs was minimal. RBC attachment was prevented by 0.01 M alpha-methyl-D-mannopyranoside, and, once the RBC-monocyte rosette was established, bound RBCs were largely removed with this specific saccharide inhibitor of Con A. RBCs attached to monocytes became spherocytic and osmotically fragile. The recognition of concanavalin A (Con A)-coated RBCs was not mediated through the monocyte IgG-Fc receptor. These studies demonstrate that, like IgG and C3b, Con A is capable of mediating the binding of human RBCs to human monocytes. Red cells so bound are damaged at the monocyte surface.

Deformation-induced ATP release from red blood cells requires CFTR activity

1998 ◽  
Vol 275 (5) ◽  
pp. H1726-H1732 ◽  
Author(s):  
Randy S. Sprague ◽  
Mary L. Ellsworth ◽  
Alan H. Stephenson ◽  
Mary E. Kleinhenz ◽  
Andrew J. Lonigro
Keyword(s):  
Cystic Fibrosis ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Atp Release ◽  
Chronic Obstructive Lung Disease ◽  
Mechanical Deformation ◽  
Chronic Obstructive ◽  
Healthy Humans ◽  
Human Red Blood Cells ◽  
Human Rbcs

Recently, it was reported that rabbit and human red blood cells (RBCs) release ATP in response to mechanical deformation. Here we investigate the hypothesis that the activity of the cystic fibrosis transmembrane conductance regulator (CFTR), a member of the ATP binding cassette, is required for deformation-induced ATP release from RBCs. Incubation of rabbit RBCs with either of two inhibitors of CFTR activity, glibenclamide (10 μM) or niflumic acid (20 μM), resulted in inhibition of deformation-induced ATP release. To demonstrate the contribution of CFTR to deformation-induced ATP release from human RBCs, cells from healthy humans, patients with cystic fibrosis (CF), or patients with chronic obstructive lung disease (COPD) unrelated to CF were studied. RBCs of healthy humans and COPD patients released ATP in response to mechanical deformation. In contrast, deformation of RBCs from patients with CF did not result in ATP release. We conclude that deformation-induced ATP release from rabbit and human RBCs requires CFTR activity, suggesting a previously unrecognized role for CFTR in the regulation of vascular resistance.

The comparison of the 1-C14-glucose and 6-C14-glucose metabolism of reticulocyte-rich and reticulocyte-poor human red blood cells

Metabolism ◽  
1965 ◽  
Vol 14 (4) ◽  
pp. 500-503 ◽  
Author(s):  
Yaye F. Herman ◽  
Craig J. Canfield ◽  
Marcel E. Conrad ◽  
Robert H. Herman
Keyword(s):  
Glucose Metabolism ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Human Red Blood Cells

scholarly journals Carbon Monoxide Signaling in Human Red Blood Cells: Evidence for Pentose Phosphate Pathway Activation and Protein Deglutathionylation

2014 ◽  
Vol 20 (3) ◽  
pp. 403-416 ◽  
Author(s):  
Alessio Metere ◽  
Egidio Iorio ◽  
Giuseppe Scorza ◽  
Serena Camerini ◽  
Marialuisa Casella ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Red Blood Cells ◽  
Pentose Phosphate Pathway ◽  
Blood Cells ◽  
Pentose Phosphate ◽  
Human Red Blood Cells ◽  
Pathway Activation

scholarly journals Human Red Blood Cells as Oxygen Carriers to Improve Ex-Situ Liver Perfusion in a Rat Model

2019 ◽  
Vol 8 (11) ◽  
pp. 1918 ◽  
Author(s):  
Daniele Dondossola ◽  
Alessandro Santini ◽  
Caterina Lonati ◽  
Alberto Zanella ◽  
Riccardo Merighi ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Rat Model ◽  
Blood Cells ◽  
Liver Perfusion ◽  
Small Animal ◽  
Lactate Clearance ◽  
Ex Situ ◽  
Oxygen Carriers ◽  
Human Red Blood Cells ◽  
Human Rbcs

Ex-situ machine perfusion (MP) has been increasingly used to enhance liver quality in different settings. Small animal models can help to implement this procedure. As most normothermic MP (NMP) models employ sub-physiological levels of oxygen delivery (DO2), the aim of this study was to investigate the effectiveness and safety of different DO2, using human red blood cells (RBCs) as oxygen carriers on metabolic recovery in a rat model of NMP. Four experimental groups (n = 5 each) consisted of (1) native (untreated/control), (2) liver static cold storage (SCS) 30 min without NMP, (3) SCS followed by 120 min of NMP with Dulbecco-Modified-Eagle-Medium as perfusate (DMEM), and (4) similar to group 3, but perfusion fluid was added with human RBCs (hematocrit 15%) (BLOOD). Compared to DMEM, the BLOOD group showed increased liver DO2 (p = 0.008) and oxygen consumption ( V O ˙ 2) (p < 0.001); lactate clearance (p < 0.001), potassium (p < 0.001), and glucose (p = 0.029) uptake were enhanced. ATP levels were likewise higher in BLOOD relative to DMEM (p = 0.031). V O ˙ 2 and DO2 were highly correlated (p < 0.001). Consistently, the main metabolic parameters were directly correlated with DO2 and V O ˙ 2. No human RBC related damage was detected. In conclusion, an optimized DO2 significantly reduces hypoxic damage-related effects occurring during NMP. Human RBCs can be safely used as oxygen carriers.

scholarly journals Phosphorylation of protein 4.1 in Plasmodium falciparum-infected human red blood cells

Blood ◽  
1994 ◽  
Vol 83 (11) ◽  
pp. 3339-3345 ◽  
Author(s):  
AH Chishti ◽  
GJ Maalouf ◽  
S Marfatia ◽  
J Palek ◽  
W Wang ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Plasma Membrane ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Malaria Parasite ◽  
Malaria Parasites ◽  
Protein 4.1 ◽  
Human Red Blood Cells ◽  
Human Rbcs

The composition of the erythrocyte plasma membrane is extensively modified during the intracellular growth of the malaria parasite Plasmodium falciparum. It has been previously shown that an 80-kD phosphoprotein is associated with the plasma membrane of human red blood cells (RBCs) infected with trophozoite/schizont stage malaria parasites. However, the identity of this 80-kD phosphoprotein is controversial. One line of evidence suggests that this protein is a phosphorylated form of RBC protein 4.1 and that it forms a tight complex with the mature parasite-infected erythrocyte surface antigen. In contrast, evidence from another group indicates that the 80-kD protein is derived from the intracellular malaria parasite. To resolve whether the 80-kD protein is indeed RBC protein 4.1, we made use of RBCs obtained from a patient with homozygous 4.1(-) negative hereditary elliptocytosis. RBCs from this patient are completely devoid of protein 4.1. We report here that this lack of protein 4.1 is correlated with the absence of phosphorylation of the 80-kD protein in parasite- infected RBCs, a finding that provides conclusive evidence that the 80- kD phosphoprotein is indeed protein 4.1. In addition, we also identify and partially characterize a casein kinase that phosphorylates protein 4.1 in P falciparum-infected human RBCs. Based on these results, we suggest that the maturation of malaria parasites in human RBCs is accompanied by the phosphorylation of protein 4.1. This phosphorylation of RBC protein 4.1 may provide a mechanism by which the intracellular malaria parasite alters the mechanical properties of the host plasma membrane and modulates parasite growth and survival in vivo.

Spectroscopy-based characterization of Hb–NO adducts in human red blood cells exposed to NO-donor and endothelium-derived NO

The Analyst ◽  
2018 ◽  
Vol 143 (18) ◽  
pp. 4335-4346 ◽  
Author(s):  
Jakub Dybas ◽  
Piotr Berkowicz ◽  
Bartosz Proniewski ◽  
Katarzyna Dziedzic-Kocurek ◽  
Jan Stanek ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
No Donor ◽  
Human Red Blood Cells ◽  
Complementary Approach ◽  
Human Rbcs

The work presents the complementary approach to characterize the formation of various Hb species inside isolated human RBCs exposed to NO, with a focus on the formed Hb–NO adducts.

scholarly journals Phosphorylation of protein 4.1 in Plasmodium falciparum-infected human red blood cells

Blood ◽  
1994 ◽  
Vol 83 (11) ◽  
pp. 3339-3345 ◽  
Author(s):  
AH Chishti ◽  
GJ Maalouf ◽  
S Marfatia ◽  
J Palek ◽  
W Wang ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Plasma Membrane ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Malaria Parasite ◽  
Malaria Parasites ◽  
Protein 4.1 ◽  
Human Red Blood Cells ◽  
Human Rbcs

Abstract The composition of the erythrocyte plasma membrane is extensively modified during the intracellular growth of the malaria parasite Plasmodium falciparum. It has been previously shown that an 80-kD phosphoprotein is associated with the plasma membrane of human red blood cells (RBCs) infected with trophozoite/schizont stage malaria parasites. However, the identity of this 80-kD phosphoprotein is controversial. One line of evidence suggests that this protein is a phosphorylated form of RBC protein 4.1 and that it forms a tight complex with the mature parasite-infected erythrocyte surface antigen. In contrast, evidence from another group indicates that the 80-kD protein is derived from the intracellular malaria parasite. To resolve whether the 80-kD protein is indeed RBC protein 4.1, we made use of RBCs obtained from a patient with homozygous 4.1(-) negative hereditary elliptocytosis. RBCs from this patient are completely devoid of protein 4.1. We report here that this lack of protein 4.1 is correlated with the absence of phosphorylation of the 80-kD protein in parasite- infected RBCs, a finding that provides conclusive evidence that the 80- kD phosphoprotein is indeed protein 4.1. In addition, we also identify and partially characterize a casein kinase that phosphorylates protein 4.1 in P falciparum-infected human RBCs. Based on these results, we suggest that the maturation of malaria parasites in human RBCs is accompanied by the phosphorylation of protein 4.1. This phosphorylation of RBC protein 4.1 may provide a mechanism by which the intracellular malaria parasite alters the mechanical properties of the host plasma membrane and modulates parasite growth and survival in vivo.

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