Lead and calcium transport in human erythrocyte

1999 ◽  
Vol 18 (5) ◽  
pp. 327-332 ◽  
Author(s):  
J V Calderón-Salinas ◽  
M A Quintanar-Escorcia ◽  
M T González-Martínez ◽  
C E Hernández-Luna
Keyword(s):  
Transport System ◽  
Human Erythrocyte ◽  
Calcium Transport ◽  
Human Erythrocytes ◽  
The Other ◽  
Erythrocyte Ghosts ◽  
Passive Transport ◽  
Ca Uptake

In this paper we report the lead (Pb) and calcium (Ca) uptake by erythrocyte ghosts. In both cases the transport was carried out by a passive transport system with two kinetic components (Michaelis-Menten and Hill). Pb and Ca were capable of inhibiting the transport of the other metal in a non-competitive way. Under hyperpolarization, the uptakes of Ca and Pb were enhanced and the Michaelis-Menten component prevailed. Both Ca and Pb uptakes were inhibited by N-ethyl-maleimide to the same extent. These results indicate that Pb and Ca share the same permeability pathway in human erythrocytes and that this transport system is electrogenic.

Effect of lead on the calcium transport in human erythrocyte

1999 ◽  
Vol 18 (3) ◽  
pp. 146-153 ◽  
Author(s):  
J V Calderón-Salinas ◽  
M A Quintanar-Escorza ◽  
C E Hernández-Luna ◽  
M T González-Martínez
Keyword(s):  
Intracellular Calcium ◽  
Transport System ◽  
Human Erythrocyte ◽  
Calcium Transport ◽  
Calcium Uptake ◽  
Calcium Influx ◽  
Passive Transport ◽  
Calcium Efflux ◽  
Excitable Cell ◽  
Physiological Conditions

In this paper we study the calcium uptake in the erythrocyte, a non-excitable cell. This uptake is performed through a passive transport system with two kinetic components (Michaelis-Menten and Hill). The uptake of calcium seems to be driven by voltage through its electrophoretical effect. Lead is capable of inhibiting calcium uptake in a non-competitive manner. As it has been described in other systems, lead is also capable of inhibiting calcium efflux by inhibiting Ca(Mg)-ATPase. Under physiological conditions, the function of ATPase reduces the effect of lead on calcium influx. However, in chronic intoxication a small increment of intracellular calcium is observed, indicating that lead is affecting calcium efflux mainly. We discuss the effects of lead on calcium equilibrium in erythrocytes.

scholarly journals Reconstitution of the Ca2+-transport system of human erythrocytes

1980 ◽  
Vol 188 (1) ◽  
pp. 47-54 ◽  
Author(s):  
K Gietzen ◽  
S Seiler ◽  
S Fleischer ◽  
H U Wolf
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Transport System ◽  
Human Erythrocyte ◽  
Room Temperature ◽  
Proteinase Inhibitors ◽  
Membrane Vesicles ◽  
Tween 20 ◽  
Erythrocyte Ghosts ◽  
Lipid Ratio

The (Ca2+ + Mg2+)-dependent ATPase of human erythrocyte ‘ghosts’ was solubilized and reconstituted to form membranous vesicles capable of energized Ca2+ accumulation. The erythrocyte ‘ghosts’ for this purpose were prepared by using isoosmotic freeze-haemolysis in the presence of Tween 20 and proteinase inhibitors to stabilize the preparation. The reconstitution procedure is similar to that developed by Meissner & Fleischer [(1974) J. Biol. Chem. 249, 302-309] for skeletal-muscle sarcoplasmic-reticulum in that: (1) deoxycholate is used for the solubilization of the membrane; (2) controlled dialysis at near room temperature, rather than 0 degree C, is required in order to obtain a functional preparation capable of Ca2+ accumulation; and (3) membrane vesicles can be reassembled with protein/lipid ratio (approx. 60% protein and 40% lipid) similar to that of the original membrane.

scholarly journals Active transport of GSSG from reconstituted erythrocyte ghosts

Blood ◽  
1975 ◽  
Vol 46 (1) ◽  
pp. 111-117 ◽  
Author(s):  
J Prchal ◽  
SK Srivastava ◽  
E Beutler
Keyword(s):  
Active Transport ◽  
Transport System ◽  
Concentration Gradient ◽  
Human Erythrocyte ◽  
Red Cells ◽  
Intracellular Concentration ◽  
Maximal Velocity ◽  
Erythrocyte Ghosts ◽  
The Relationship

Abstract Human erythrocyte ghosts were loaded with 35S-labeled GSSG and with a sucrose marker, and the transport of GSSG to the suspending medium was studied. GSSG transport from ghosts occurred only when ATP was also present in the ghosts, proceeded against a concentration gradient, and was inhibited by fluoride. The rate of transport was dependent upon the intracellular concentration of GSSG. The relationship between GSSG concentration and rate of transport was sigmoidal. Half-maximal transport was observed at a GSSG concentration of approximately 9.6mM. The maximal velocity was estimated to be in the range of 0.27 umole GSSG per ml of ghosts per hr. These data suggest that the rate of GSSG transport a physiologic concentrations of GSSG is not sufficiently rapid to account for the turnover of glutathione by red cells. It seems more likely that the GSSG transport system serves an emergency function of erythrocytes.

scholarly journals Active transport of GSSG from reconstituted erythrocyte ghosts

Blood ◽  
1975 ◽  
Vol 46 (1) ◽  
pp. 111-117
Author(s):  
J Prchal ◽  
SK Srivastava ◽  
E Beutler
Keyword(s):  
Active Transport ◽  
Transport System ◽  
Concentration Gradient ◽  
Human Erythrocyte ◽  
Red Cells ◽  
Intracellular Concentration ◽  
Maximal Velocity ◽  
Erythrocyte Ghosts ◽  
The Relationship

Human erythrocyte ghosts were loaded with 35S-labeled GSSG and with a sucrose marker, and the transport of GSSG to the suspending medium was studied. GSSG transport from ghosts occurred only when ATP was also present in the ghosts, proceeded against a concentration gradient, and was inhibited by fluoride. The rate of transport was dependent upon the intracellular concentration of GSSG. The relationship between GSSG concentration and rate of transport was sigmoidal. Half-maximal transport was observed at a GSSG concentration of approximately 9.6mM. The maximal velocity was estimated to be in the range of 0.27 umole GSSG per ml of ghosts per hr. These data suggest that the rate of GSSG transport a physiologic concentrations of GSSG is not sufficiently rapid to account for the turnover of glutathione by red cells. It seems more likely that the GSSG transport system serves an emergency function of erythrocytes.

Shape transformation of erythrocyte ghosts depends on ion concentrations

1985 ◽  
Vol 5 (5) ◽  
pp. 417-423 ◽  
Author(s):  
Andreas Herrmann ◽  
Peter Müller ◽  
Roland Glaser
Keyword(s):  
Human Erythrocyte ◽  
Transmembrane Potential ◽  
Human Erythrocytes ◽  
Erythrocyte Ghosts ◽  
Shape Transformation ◽  
Ion Concentrations ◽  
Nacl Concentration ◽  
Shape Transformations

Resealed human erythrocyte ghosts undergo shape transformations similar to those of intact erythrocytes. The results indicate that the shape of these ghosts depends on the inner as well as on the outer NaCl concentration. A correlation between shape and calculated transmembrane potential was established similar to that for intact human erythrocytes.

scholarly journals The reactivities of human erythrocyte autoantibodies anti-Pr2, anti-Gd, Fl and Sa with gangliosides in a chromatogram binding assay

1984 ◽  
Vol 219 (3) ◽  
pp. 865-874 ◽  
Author(s):  
K Uemura ◽  
D Roelcke ◽  
Y Nagai ◽  
T Feizi
Keyword(s):  
Sialic Acid ◽  
Thin Layer ◽  
Human Erythrocyte ◽  
Binding Assay ◽  
Neuraminic Acid ◽  
Human Erythrocytes ◽  
The Other ◽  
Thin Layer Chromatogram ◽  
Acetylneuraminic Acid ◽  
Bovine Erythrocytes

The thin layer chromatogram binding assay was used to study the reaction of several natural-monoclonal autoantibodies which recognize sialic acid-dependent antigens of human erythrocytes. Immunostaining of gangliosides derived from human and bovine erythrocytes was achieved with four autoantibodies designated anti-Pr2, anti-Gd, Sa and Fl, each of which has a different haemagglutination pattern with untreated and proteinase-treated erythrocytes and with cells of I and i antigen types. From the chromatogram binding patterns of anti-Pr2 with gangliosides of the neolacto and the ganglio series, it is deduced that this antibody reacts best with N-acetylneuraminic acid when it is alpha 2-3- or alpha 2-6-linked to a terminal Gal(beta 1-4)Glc/GlcNAc GlcNAc sequence and to a lesser extent when it is alpha 2-3-linked to a terminal Gal(beta 1-3)GalNAc sequence or to an internal galactose and when it is alpha 2-8-linked to another, internal N-acetylneuraminic acid residue. The other three antibodies differ from anti-Pr2 in their lack of reaction with glycolipids of the ganglio series. They react with the NeuAc(alpha 2-3)Gal(beta 1-4)Glc/GlcNAc sequence as found in GM3 and in glycolipids of the neolacto series, but show a preference for the latter, longer sequences. Thus all four antibodies react with sialylated oligosaccharides containing i type (linear) and I type (branched) neolacto backbones. Fl antibody differs from the other three in its stronger reaction with branched neolacto sequences in accordance with its stronger agglutination of erythrocytes of I rather than i type. The four antibodies show a specificity for N-acetyl- rather than N-glycolyl-neuraminic acid.

scholarly journals The organization of the major protein of the human erythrocyte membrane

1974 ◽  
Vol 137 (3) ◽  
pp. 531-534 ◽  
Author(s):  
D. H. Boxer ◽  
R. E. Jenkins ◽  
M. J. A. Tanner
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Intact Cell ◽  
The Other ◽  
Major Protein ◽  
Erythrocyte Ghosts ◽  
Human Erythrocyte Membrane ◽  
Cytoplasmic Surface ◽  
Peptide Maps

The enzyme lactoperoxidase was used to catalyse the radioiodination of membrane proteins in intact human erythrocytes and in erythrocyte ‘ghosts’. Two major proteins of the erythrocyte membrane were isolated after iodination of these two preparations, and the peptide ‘maps’ of each protein so labelled were compared. Peptides from both proteins are labelled in the intact cell. In addition, further mobile peptides derived from one of the proteins are labelled only in the ‘ghost’ preparation. Various sealed ‘ghost’ preparations were also iodinated, lactoperoxidase being present only at either the cytoplasmic or extra-cellular surface of the membrane. The peptide ‘maps’ of protein E (the major membrane protein) labelled in each case were compared. Two discrete sets of labelled peptides were consistently found. One group is obtained when lactoperoxidase is present at the extra-cellular surface and the other group is found when the enzyme is accessible only to the cytoplasmic surface of the membrane. The results support the assumption that the organization of protein E in the membrane of the intact erythrocyte is unaltered on making erythrocyte ‘ghosts’. They also confirm previous suggestions that both the sialoglycoprotein and protein E extend through the human erythrocyte membrane.

scholarly journals Lipid organization in erythrocyte membrane microvesicles

1984 ◽  
Vol 224 (1) ◽  
pp. 285-290 ◽  
Author(s):  
S Scott ◽  
S A Pendlebury ◽  
C Green
Keyword(s):  
Phospholipase A2 ◽  
Erythrocyte Membrane ◽  
Human Erythrocytes ◽  
The Other ◽  
Erythrocyte Membranes ◽  
Erythrocyte Ghosts ◽  
Lipid Organization

The aminophospholipids of microvesicles released from human erythrocytes on storage or prepared from erythrocyte ghosts by shearing under pressure are susceptible to the action of 2,4,6-trinitrobenzenesulphonic acid. The aminophospholipids of the former vesicles are also susceptible to attack by phospholipase A2. Under the same conditions, the aminophospholipids of erythrocytes undergo little reaction. This suggests that the phospholipids in microvesicle membranes are more randomly distributed than those in erythrocyte membranes. Measurements have also been made of the ability of filipin to react with the cholesterol of sealed and unsealed erythrocyte ghosts and of microvesicles prepared from them. From the initial rates of reaction, it was concluded that there is no preferential transfer of cholesterol molecules from one side of the bilayer to the other during the formation of the microvesicles.

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