Inhibition of p. falciparum invasion in PK- and PGI deficient red blood cells by inducing band 3 protein degradation

2000 ◽  
Vol 28 (5) ◽  
pp. A217-A217
Author(s):  
G. Jacobasch ◽  
A. Lindhammer ◽  
J. Schulz
Keyword(s):  
Red Blood Cells ◽  
Protein Degradation ◽  
Blood Cells ◽  
Band 3 ◽  
Band 3 Protein

Characterization of anion transport system in trout red blood cell

1984 ◽  
Vol 246 (3) ◽  
pp. C330-C338 ◽  
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.

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

2007 ◽  
Vol 75 (4) ◽  
pp. 1771-1777 ◽  
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.

Alterations in band 3 protein and anion exchange in red blood cells of renal failure patients

2005 ◽  
Vol 273 (1-2) ◽  
pp. 11-24 ◽  
Author(s):  
Varadharaj Saradhadevi ◽  
Ramasamy Sakthivel ◽  
Srikanth Vedamoorthy ◽  
Ramasamy Selvam ◽  
Narasimham Parinandi
Keyword(s):  
Renal Failure ◽  
Red Blood Cells ◽  
Anion Exchange ◽  
Blood Cells ◽  
Band 3 ◽  
Band 3 Protein

scholarly journals Syk inhibitors interfere with erythrocyte membrane modification during P falciparum growth and suppress parasite egress

Blood ◽  
2017 ◽  
Vol 130 (8) ◽  
pp. 1031-1040 ◽  
Author(s):  
Antonella Pantaleo ◽  
Kristina R. Kesely ◽  
Maria Carmina Pau ◽  
Ioannis Tsamesidis ◽  
Evelin Schwarzer ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Tyrosine Phosphorylation ◽  
Erythrocyte Membrane ◽  
Blood Cells ◽  
Band 3 ◽  
Membrane Modification ◽  
Syk Kinase ◽  
Key Points ◽  
Parasite Egress

Key PointsInhibitors of human Syk kinase suppress parasite egress. Syk inhibitors prevent the tyrosine phosphorylation of band 3 in P falciparum parasitized red blood cells, reducing the release of microparticles.

K562 cell anion exchange differs markedly from that of mature red blood cells

1983 ◽  
Vol 244 (1) ◽  
pp. C68-C74 ◽  
Author(s):  
F. Y. Law ◽  
R. Steinfeld ◽  
P. A. Knauf
Keyword(s):  
Blood Cell ◽  
Red Blood Cells ◽  
Red Blood Cell ◽  
Blood Cells ◽  
Chloride Transport ◽  
K562 Cells ◽  
Band 3 ◽  
Anion Transport ◽  
Leukemic Cells ◽  
Anion Transport System

Human K562 leukemic cells exhibit several erythroid properties, including synthesis and expression of the major red blood cell sialoglycoprotein, glycophorin. This has led us to ask if these cells express a functional anion transport system analogous to that which is associated with the other major erythrocyte glycoprotein, band 3. The chloride-36 exchange flux in K562 cells is less than 0.6% of that which would be expected in mature erythrocytes under similar conditions. Unlike red blood cells, K562 cells do not exhibit a high chloride-sulfate selectivity, and various agents that inhibit red blood cell chloride exchange are all much less effective in K562 cells. On the basis of these flux measurements, K562 cells probably contain less than 600 fully functional red blood cell-like band 3 molecules per cell, in contrast to about a million molecules in the mature red blood cell. The possible-existence of greatly altered band 3 molecules with a reduced turnover rate and/or a reduced affinity for chloride and for various inhibitors is unlikely but cannot be completely excluded. Anion transport was also measured in K562 cells that had been induced to increase hemoglobin synthesis by various chemical agents. Even under these conditions, chloride fluxes indicated no substantial increase in the number of functional anion transport sites or their chloride transport rate.

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