Shape and Biomechanical Characteristics of Human Red Blood Cells in Health and Disease

AbstractThe biconcave shape and corresponding deformability of the human red blood cell (RBC) is an essential feature of its biological function. This feature of RBCs can be critically affected by genetic or acquired pathological conditions. In this review, we highlight new dynamicin vitroassays that explore various hereditary blood disorders and parasitic infectious diseases that cause disruption of RBC morphology and mechanics. In particular, recent advances in high-throughput microfluidic devices make it possible to sort/identify healthy and pathological human RBCs with different mechanobiological characteristics.

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Enrichment of two glycosyl-phosphatidylinositol-anchored proteins, acetylcholinesterase and decay accelerating factor, in vesicles released from human red blood cells

Blood ◽

10.1182/blood.v74.5.1481.bloodjournal7451481 ◽

1989 ◽

Vol 74 (5) ◽

pp. 1481-1485

Author(s):

P Butikofer ◽

FA Kuypers ◽

CM Xu ◽

DT Chiu ◽

B Lubin

Keyword(s):

Cell Membrane ◽

Blood Cells ◽

Cell Types ◽

Gpi Anchor ◽

Decay Accelerating Factor ◽

Glycosyl Phosphatidylinositol ◽

Human Red Blood Cells ◽

Rbc Membrane ◽

Human Rbcs

Several proteins are attached to the cell membrane by a glycosyl- phosphatidylinositol (GPI) anchor. In this report, we show that during vesiculation of human RBCs in vitro, two of these proteins, acetylcholinesterase and decay accelerating factor, redistribute on the cell surface and become enriched in the released vesicles. As a result, the remnant cells are depleted of these proteins. We suggest that alterations in the architecture of the RBC membrane that precede vesiculation lead to selective polarization of GPI-anchored proteins within the domain of the membrane destined to become a vesicle. Since vesiculation occurs in many cell types, and if the loss of GPI-anchored proteins accompanies this process, it may have important biologic significance.

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Enrichment of two glycosyl-phosphatidylinositol-anchored proteins, acetylcholinesterase and decay accelerating factor, in vesicles released from human red blood cells

Blood ◽

10.1182/blood.v74.5.1481.1481 ◽

1989 ◽

Vol 74 (5) ◽

pp. 1481-1485 ◽

Cited By ~ 65

Author(s):

P Butikofer ◽

FA Kuypers ◽

CM Xu ◽

DT Chiu ◽

B Lubin

Keyword(s):

Cell Membrane ◽

Blood Cells ◽

Cell Types ◽

Gpi Anchor ◽

Decay Accelerating Factor ◽

Glycosyl Phosphatidylinositol ◽

Human Red Blood Cells ◽

Rbc Membrane ◽

Human Rbcs

Abstract Several proteins are attached to the cell membrane by a glycosyl- phosphatidylinositol (GPI) anchor. In this report, we show that during vesiculation of human RBCs in vitro, two of these proteins, acetylcholinesterase and decay accelerating factor, redistribute on the cell surface and become enriched in the released vesicles. As a result, the remnant cells are depleted of these proteins. We suggest that alterations in the architecture of the RBC membrane that precede vesiculation lead to selective polarization of GPI-anchored proteins within the domain of the membrane destined to become a vesicle. Since vesiculation occurs in many cell types, and if the loss of GPI-anchored proteins accompanies this process, it may have important biologic significance.

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Pharmacological activation of PIEZO1 in human red blood cells prevents Plasmodium falciparum invasion

10.1101/2021.05.28.446171 ◽

2021 ◽

Author(s):

Rakhee Lohia ◽

Jordy Le Guet ◽

Laurence Berry ◽

Helene Guizouarn ◽

Roberto Bernal ◽

...

Keyword(s):

Plasmodium Falciparum ◽

Blood Cells ◽

Malaria Infection ◽

Significant Protection ◽

Surface Receptors ◽

Human Red Blood Cells ◽

Cationic Channel ◽

Human Rbcs ◽

Dependent Mechanism

An inherited gain-of-function variant (E756 del) in the mechanosensitive cationic channel PIEZO1 was recently shown to confer a significant protection against severe malaria. Here, we demonstrate in vitro that human red blood cell (RBC) infection by Plasmodium falciparum is prevented by the pharmacological activation of PIEZO1. The PIEZO1 activator Yoda1 inhibits RBC invasion, without affecting parasite intraerythrocytic growth, division or egress. RBC dehydration, echinocytosis and intracellular Na+/K+ imbalance are unrelated to the mechanism of protection. Inhibition of invasion is maintained, even after a prolonged wash out of Yoda1. Similarly, the chemically unrelated activators Jedi1 and Jedi2 potently inhibit parasitemia, further indicating a PIEZO1-dependent mechanism. Notably, Yoda1 treatment significantly reduced RBC surface receptors of P. falciparum, and decreased merozoite attachment and subsequent RBC deformation. Altogether these data indicate that the pharmacological activation of Piezo1 in human RBCs inhibits malaria infection by impairing P. falciparum invasion.

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Melatonin Ameliorates BPA Induced Oxidative Stress in Human Red Blood Cells: An In vitro Study

Endocrine Metabolic & Immune Disorders - Drug Targets ◽

10.2174/1871530320666200505112023 ◽

2020 ◽

Vol 20 (8) ◽

pp. 1321-1327

Author(s):

Saleh M. Abdullah ◽

Hina Rashid

Keyword(s):

Oxidative Stress ◽

Lipid Peroxidation ◽

Red Blood Cells ◽

Blood Cells ◽

In Vitro Study ◽

Limited Data ◽

Human Red Blood Cells ◽

Living Organisms ◽

Human Rbcs

Background: Bisphenol A (BPA) is a xenobiotic that causes oxidative stress in various organs in living organisms. Blood cells are also an endpoint where BPA is known to cause oxidative stress. Blood cells, especially red blood cells (RBCs), are crucial for maintaining homeostasis and overall wellbeing of the organism. They are highly susceptible to oxidative stress induced by xenobiotics. However, there is limited data about the oxidative stress induced by BPA in blood, especially in red blood cells. This study was carried out to evaluate BPA induced oxidative stress in human RBCs in vitro and its amelioration by melatonin. Objective: To find if melatonin exerts a protective effect on the oxidative stress induced by the BPA in human red blood cells in vitro. Methods: The erythrocyte suspensions (2 ml) were divided into six groups and treated with 0, 50, 100, 150, 200, and 250 μg/ml of BPA. Another set of erythrocyte suspension with similar BPA treatment and 50 μM Melatonin per group was also set. Incubations lasted for 12 hrs in the dark. Lipid peroxidation, glutathione, glutathione reductase, catalase, and superoxide dismutase were measured as indicators of oxidative stress. Results: BPA caused a significant increase in lipid peroxidation. A decrease in GSH levels was also observed. The activities of all the studied antioxidants also decreased with BPA treatment. Melatonin was seen to mitigate the oxidative stress induced by BPA. Conclusion: Treatment of red blood cells with BPA caused an increase in oxidative stress, while melatonin decreased the induced oxidative stress.

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

Nature Communications ◽

10.1038/s41467-020-20479-4 ◽

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.

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