Partial covalent labeling with pyridoxal 5′-phosphate induces bis(sulfosuccinimidyl)suberate crosslinking of band 3 protein tetramers in intact human red blood cells

The effects of gemfibrozil (GFZ), an antihyperlipidemic agent, on the anionic transport of the human red blood cells (RBC) during the oxygenation-deoxygenation cycle were examined. Gemfibrozil clearly plays a role in the modulation of the anionic flux in erythrocytes; in fact it causes a strong increment of anions transport when the RBCs are in the high-oxygenation state (HOS). Such an effect is remarkably reduced in the lowoxygenation state (LOS). With the aim of identifying the dynamics of fibrate action, this effect has been investigated also in human ghost and chicken erythrocytes. These latter, in fact, are known to possess a B3 (anion transporter or Band 3) modified at the cytoplasmic domain (cdb3) which plays a significant role in the metabolic modulation of red blood cells. The results were analyzed taking into account the well-known interactions between fibrates and both conformational states of hemoglobin i.e. the T state (deoxy-conformation) and the R state (oxy-conformation). The effect of gemfibrozil on anionic influx appears to be due to a wide interaction involving a “multimeric” Hb-GFZ-cdb3 macromolecular complex.

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Characterization of anion transport system in trout red blood cell

AJP Cell Physiology ◽

10.1152/ajpcell.1984.246.3.c330 ◽

1984 ◽

Vol 246 (3) ◽

pp. C330-C338 ◽

Cited By ~ 57

Author(s):

L. Romano ◽

H. Passow

Keyword(s):

Blood Cell ◽

Red Blood Cells ◽

Red Blood Cell ◽

Blood Cells ◽

Sodium Dodecyl ◽

Band 3 ◽

Anion Transport ◽

Disulfonic Acid ◽

Band 3 Protein ◽

Proton Uptake

Anion transport in the trout red blood cell is mediated by a membrane protein that selectively binds dihydro-4,4'-dithiocyanostilbene-2,2'-disulfonic acid (3H2DIDS) and that forms on sodium dodecyl sulfate (SDS)-polyacrylamide gel electropherograms a band with the same diffuse structure at the same location as the band 3 protein of the mammalian red blood cells. There exists a linear relationship between binding of H2DIDS to this protein and the inhibition of anion equilibrium exchange. At maximal inhibition about 8 X 10(6) molecules/cell are bound to the protein. The kinetics of anion transport in the trout red blood cell differ from those of mammalian red blood cells. In addition to a H2DIDS-sensitive component of sulfate transport there exists a considerable H2DIDS-insensitive component with a relative magnitude that decreases with increasing temperature. At 23 degrees C, it amounts to about 25%. The temperature dependence of the H2DIDS-sensitive component is about 15 kcal/mol instead of 32 as in human red blood cells. Cl- transport increases with increasing pH. Above pH 7.4, the rate of transport becomes too fast to be measurable with either inhibitor stop or filtration technique. SO2-4 transport is nearly pH independent over the pH range 6.5 to 7.8 and the net entry of SO2-4 in exchange against intracellular Cl-, as followed in the absence of CO2, is accompanied by little if any proton uptake. Net proton uptake becomes measurable only at temperatures above 40 degrees C. Possibly at lower and more physiological temperatures, the band 3 protein in the red blood cell of the trout accomplishes part of the SO2-4 movements without cotransporting protons.

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Complement Factor D, Albumin, and Immunoglobulin G Anti-Band 3 Protein Antibodies Mimic Serum in Promoting Rosetting of Malaria-Infected Red Blood Cells

Infection and Immunity ◽

10.1128/iai.01514-06 ◽

2007 ◽

Vol 75 (4) ◽

pp. 1771-1777 ◽

Cited By ~ 25

Author(s):

Alexander Luginbühl ◽

Milica Nikolic ◽

Hans Peter Beck ◽

Mats Wahlgren ◽

Hans U. Lutz

Keyword(s):

Red Blood Cells ◽

Blood Cells ◽

De Novo ◽

Protein Band ◽

Band 3 ◽

Complement Factor ◽

Band 3 Protein ◽

Naturally Occurring ◽

Serum Dependent ◽

Naturally Occurring Antibodies

ABSTRACT Rosetting of Plasmodium falciparum-infected red blood cells (parasitized RBC [pRBC]) with uninfected RBC has been associated in many studies with malaria morbidity and is one form of cytoadherence observed with malarial parasites. Rosetting is serum dependent for many isolates of P. falciparum, including the strains FCR3S1.2 and Malayan Camp studied here. We identified the three naturally occurring components of sera which confer rosetting. Complement factor D alone induced 30 to 40% of de novo rosetting. Its effect was additive to that of 0.5 mg/ml albumin and to that of 15 ng/ml of naturally occurring antibodies to the anion transport protein, band 3. The three components together mediated rosetting as effectively as 10% serum. De novo rosetting experiments showed that naturally occurring anti-band 3 antibodies as well as factor D were effective only when added to pRBC. Factor D appeared to cleave a small fraction of a protein expressed on the surface of pRBC.

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Human Red Blood Cells Alterations in Primary Aldosteronism

The Journal of Clinical Endocrinology & Metabolism ◽

10.1210/jc.2012-3571 ◽

2013 ◽

Vol 98 (6) ◽

pp. 2494-2501 ◽

Cited By ~ 15

Author(s):

Luciana Bordin ◽

Gabriella Donà ◽

Chiara Sabbadin ◽

Eugenio Ragazzi ◽

Alessandra Andrisani ◽

...

Keyword(s):

Red Blood Cells ◽

Primary Aldosteronism ◽

Blood Cells ◽

Redox Status ◽

Band 3 ◽

Human Red Blood Cells ◽

Igg Binding ◽

Healthy Control ◽

Study Participants

Context: Aldosterone (Aldo) effects include NADPH oxidase activation involved in Aldo-related oxidative stress. Red blood cells (RBCs) are particularly sensitive to oxidative assault, and both the formation of high molecular weight aggregates (HMWAs) and the diamide-induced Tyr phosphorylation (Tyr-P) level of membrane band 3 can be used to monitor their redox status. Objective: The Aldo-related alterations in erythrocytes were evaluated by comparing in vitro evidence. Design: This was a multicenter comparative study. Study Participants: The study included 12 patients affected by primary aldosteronism (PA) and 6 healthy control subjects (HCs), whose RBCs were compared with those of patients with PA. For in vitro experiments, RBCs from HCs were incubated with increasing Aldo concentrations. Main Outcome Measures: The Tyr-P level, band 3 HMWA formation, and autologous IgG binding were evaluated. Results: In patients with PA, both Tyr-P levels and band 3 HMWAs were higher than those in HCs. RBCs from HCs were treated with increasing Aldo concentrations in both platelet-poor plasma (PPP) and charcoal-stripped (CS)-PPP. Results showed that Aldo had dose- and time-dependent effects on band 3 Tyr-P and HMWA formation in CS-PPP more than in PPP. These effects were almost completely prevented by canrenone or cortisol. Aldo-related membrane alterations led to increased autologous IgG binding. Conclusions: Erythrocytes from patients with PA show oxidative-like stress evidenced by increased HMWA content and diamide-induced band 3 Tyr-P level. Aldo effects are mediated by the mineralocorticoid receptor, as suggested by the inhibitory effects of canrenone, an antagonist of Aldo. In CS-PPP, in which Aldo induces remarkable membrane alterations leading to IgG binding, Aldo may be responsible for premature RBC removal from circulation.

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