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.

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.

scholarly journals Effects of n-Octyl-β-D-Glucopyranoside on Human and Rat Erythrocyte Membrane Stability Against Hemolysis

2012 ◽  
Vol 5 (1) ◽  
pp. 1-5 ◽  
Author(s):  
Cesare Sblano ◽  
Silvia Micelli ◽  
Daniela Meleleo
Keyword(s):  
Erythrocyte Membrane ◽  
Practical Importance ◽  
Human Erythrocytes ◽  
Erythrocyte Membranes ◽  
Ionic Surfactant ◽  
Hypotonic Medium ◽  
Rat Erythrocytes ◽  
Biphasic Effect ◽  
Dose Dependent

The practical importance for the pharmaceutical and cosmetics industries of the interactions between biological membranes and surfactant molecules has led to intensive research within this area. The interactions of non-ionic surfactant n-octyl-β-D-glucopyranoside (OG) with the human and rat erythrocyte membranes were studied. The in vitro hemolytic and antihemolytic activities were determined by employing a method in which both erythrocytes were added to the hypotonic medium containing OG at different concentrations, and the amount of haemoglobin released was determined. noctyl- β-D-glucopyranoside was found to have a biphasic effect on both types of erythrocyte membrane. We also investigated the interactions of OG with the erythrocyte membrane in isotonic medium; the dose-dependent curves show similar behaviour in both human and rat erythrocytes. Our results showed that OG has greater antihemolytic potency on rat than on human erythrocytes; furthermore, rat erythrocytes were more sensitive than human erythrocytes to hypotonic shock. How the different lipoprotein structure of these erythrocytes determines a difference in antihemolytic activity is discussed.

scholarly journals On the mechanism of ATP-induced shape changes in the human erythrocyte membranes: the role of ATP

1977 ◽  
Vol 73 (3) ◽  
pp. 647-659 ◽  
Author(s):  
W Birchmeier ◽  
SJ Singer
Keyword(s):  
Erythrocyte Membrane ◽  
Preceding Paper ◽  
State Level ◽  
Protein Molecule ◽  
Erythrocyte Membranes ◽  
Erythrocyte Ghosts ◽  
Intact Cells ◽  
Peptide Cleavage ◽  
Biochemical Effects ◽  
Shape Changes

In the preceding paper (Sheetz, M. and S.J. Singer. 1977. J Cell Biol. 73:638-646) it was shown that erythrocyte ghosts undergo pronounced shape changes in the presence of mg-ATP. The biochemical effects of the action of ATP are herein examined. The biochemical effects of the action of ATP are herein examined. Phosphorylation by ATP of spectrin component 2 of the erythrocyte membrane is known to occur. We have shown that it is only membrane protein that is significantly phosphorylated under the conditions where the shape changes are produced. The extent of this phosphorylation rises with increasing ATP concentration, reaching nearly 1 mol phosphoryle group per mole of component 2 at 8mM ATP. Most of this phosphorylation appears to occur at a single site on the protein molecule, according to cyanogen bromide peptide cleavage experiments. The degree of phosphorylation of component 2 is apparently also regulated by a membrane-bound protein phosphatase. This activity can be demonstrated in erythrocyte ghosts prepared from intact cells prelabeled with [(32)P]phosphate. In addition to the phosphorylation of component 2, some phosphorylation of lipids, mainly of phosphatidylinositol, is also known to occur. The ghost shape changes are, however, shown to be correlated with the degree of phosphorylation of component 2. In such experiment, the incorporation of exogenous phosphatases into ghosts reversed the shape changes produced by ATP, or by the membrane-intercalating drug chlorpromazine. The results obtained in this and the preceding paper are consistent with the proposal that the erythrocyte membrane possesses kinase and phosphates activities which produce phosphorylation and dephosphorylation of a specific site on spectrin component 2 molecules; the steady-state level of this phosphorylation regulates the structural state of the spectrin complex on the cytoplasmic surface of the membrane, which in turn exerts an important control on the shape of the cell.

scholarly journals Interaction of Catechins with Human Erythrocytes

Molecules ◽  
2020 ◽  
Vol 25 (6) ◽  
pp. 1456
Author(s):  
Katarzyna Naparlo ◽  
Grzegorz Bartosz ◽  
Ireneusz Stefaniuk ◽  
Bogumil Cieniek ◽  
Miroslaw Soszynski ◽  
...  
Keyword(s):  
Lipid Peroxidation ◽  
Oxidative Damage ◽  
Stearic Acid ◽  
Erythrocyte Membrane ◽  
Membrane Lipid ◽  
Human Erythrocytes ◽  
Erythrocyte Membranes ◽  
Spin Labels ◽  
Protective Effects ◽  
Protein Thiol

The aim of this study was to characterize the interaction of chosen catechins ((+)-catechin, (−)-epigallocatechin (EGC), and (−)-epigallocatechin gallate (EGCG)) with human erythrocytes and their protective effects against oxidative damage of erythrocytes. Uptake of the catechins by erythrocytes was studied by fluorimetry, their interaction with erythrocyte membrane was probed by changes in erythrocyte osmotic fragility and in membrane fluidity evaluated with spin labels, while protection against oxidative damage was assessed by protection against hemolysis induced by permanganate and protection of erythrocyte membranes against lipid peroxidation and protein thiol group oxidation. Catechin uptake was similar for all the compounds studied. Accumulation of catechins in the erythrocyte membrane was demonstrated by the catechin-induced increase in osmotic resistance and rigidification of the erythrocyte membrane detected by spin labels 5-doxyl stearic acid and 16-doxyl stearic acid. (−)-Epigallocatechin and EGCG inhibited erythrocyte acetylcholinesterase (mixed-type inhibition). Catechins protected erythrocytes against permanganate-induced hemolysis, oxidation of erythrocyte protein thiol groups, as well as membrane lipid peroxidation. These results contribute to the knowledge of the beneficial effects of catechins present in plant-derived food and beverages.

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 Optical-rotatory-dispersion studies of compounds related to cholesterol in liposomes and the membranes of erythrocyte ‘ghosts’

1973 ◽  
Vol 135 (1) ◽  
pp. 63-71 ◽  
Author(s):  
Jonathan R. Green ◽  
Peter A. Edwards ◽  
Colin Green
Keyword(s):  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Optical Rotatory Dispersion ◽  
Rotatory Dispersion ◽  
Erythrocyte Membranes ◽  
Optical Rotatory ◽  
Erythrocyte Ghosts ◽  
Polar Solvents ◽  
Human Erythrocyte Membranes ◽  
Do So

1. Steroid molecules containing the α,β-unsaturated oxo group in various positions were incorporated with egg phosphatidylcholine into liposomes and into human erythrocyte membranes. 2. The liposomes formed contained 0.3–0.94mol of steroid/mol of phospholipid and the steroids replaced 19–76% of the erythrocyte membrane sterol. 3. The optical rotatory dispersion (o.r.d.) spectra of the steroids in these structures were compared with those obtained in solvents of different polarity. 4. The o.r.d. spectra of cholesta-4,6-dien-3-one and 3-hydroxycholest-3-en-2-one in liposomes resembled those obtained with polar solvents such as ethanol or triethyl phosphate–water (1:1, v/v). 5. The o.r.d. spectra of 3-hydroxycholest-7-en-6-one and 3-hydroxycholest-5-en-7-one in liposomes resembled those obtained with moderately polar solvents such as dioxan. 6. The o.r.d. spectrum of 3-hydroxycholest-8(14)-en-15-one in liposomes resembled those obtained with non-polar solvents such as cyclohexane. 7. 3-Hydroxycholest-3-en-2-one did not exchange with erythrocyte membrane cholesterol, but the other steroids did do so and the o.r.d. spectra of the membranes containing them closely resembled those obtained with liposomes. 8. From the results, the position of sterol molecules with respect to the phospholipid molecules in liposomes and membranes of human erythrocyte ‘ghosts’ can be deduced.

scholarly journals A carbohydrate-deficient membrane glycoprotein in human erythrocytes of phenotype S-s-

1977 ◽  
Vol 165 (1) ◽  
pp. 157-161 ◽  
Author(s):  
M J A Tanner ◽  
D J Anstee ◽  
P A Judson
Keyword(s):  
Blood Group ◽  
Arachis Hypogaea ◽  
Human Erythrocyte ◽  
Structure And Function ◽  
Human Erythrocytes ◽  
Erythrocyte Membranes ◽  
Membrane Glycoprotein ◽  
Blood Group Antigens ◽  
And Function ◽  
Normal Erythrocyte

1. We investigated the membranes of human erythrocytes which completely lack the blood-group antigens S and s (denoted as S-s-) as part of a study of the structure and function of the surface glycoproteins of the human erythrocyte. 2. The S-s-erythrocyte-membrane glycoprotein PAS-3 band was much less intensely stained in comparison with that of the glycoprotein from normal erythrocyte membranes. The S-s-membrane glycoprotein PAS-4 band also showed decreased staining. 3. Examination with the lectins from Maclura aurantiaca (Osage orange) and Arachis hypogaea (groundnut) showed that the PAS-3 glycoprotein of S-s-erythrocyte membranes lacked the receptors for these lectins that are present on glycoprotein PAS-3 from normal erythrocytes. 4. Radioiodination with lactoperoxidase showed the presence of the polypeptide of glycoprotein PAS-3 in S-s-cells, although it was more weakly labelled than the protein in the normal erythrocyte. 5. Our results show that the PAS-3 glycoprotein of S-s-erythrocytes is deficient in some of the carbohydrates present in the protein from normal erythrocytes. Glycoprotein PAS-4 of normal erythrocytes is shown to be a complex containing both glycoproteins PAS-1 and PAS-3.

The effect of various cooling rates on the membrane ultrastructure of frozen human erythrocytes and its relation to the extent of haemolysis after thawing

1981 ◽  
Vol 49 (1) ◽  
pp. 369-382
Author(s):  
S. Fujikawa
Keyword(s):  
Cooling Rate ◽  
Human Erythrocytes ◽  
Ice Crystals ◽  
Erythrocyte Membranes ◽  
Ultrastructural Changes ◽  
Cooling Rates ◽  
Intracellular Ice ◽  
Frozen State ◽  
Membrane Ultrastructure ◽  
Fast Freezing

Human erythrocytes suspended in buffered isotonic saline were frozen to the temperature of liquid nitrogen at various cooling rates of 3, 140, 700, 1800, 3500, 8000 and 11 500 deg. C/min. The membrane ultrastructure in the frozen state and the extent of haemolysis after thawing were examined at each cooling rate. As the cooling rates increased from 3 to 3500 deg. C/min, the extent of lysis gradually decreased, but further increase in cooling rates in excess of 8000 deg. C/min resulted in an abrupt increase of lysis. Membrane-associated vesicles devoid of intramembrane particles (IMPs) were formed in the erythrocyte membranes frozen at cooling rates slower than 1800 deg. C/min. The frequency and size of these vesicles were highly cooling-rate-dependent and they were no longer formed in the erythrocyte membranes frozen at cooling rates faster than 3500 deg. C/min. Another membrane ultrastructural change associated closely with the formation of intracellular ice crystals appeared at cooling rates faster than 8000 deg. C/min. The membrane regions in direct contact with intracellular ice crystals were physically damaged and had an appearance resembling worm-eaten spots. The erythrocytes frozen at a cooling rate of 3500 deg. C/min exhibited ultrastructural integrity of the membrane by avoiding the membrane changes caused by either slow or fast freezing. It is suggested, from the close relation between membrane ultrastructure and the extent of haemolysis, that the ultrastructural integrity of membrane in the frozen state is important for avoiding haemolysis after thawing, and that the membrane ultrastructural changes caused by both slow and fast freezing were responsible for the lysis after thawing.

scholarly journals Human erythrocytes adhering to schistosomula of Schistosoma mansoni lyse and fail to transfer membrane components to the parasite.

1985 ◽  
Vol 101 (1) ◽  
pp. 158-166 ◽  
Author(s):  
J P Caulfield ◽  
C M Cianci
Keyword(s):  
Schistosoma Mansoni ◽  
Erythrocyte Membrane ◽  
Plasma Membranes ◽  
Freeze Fracture ◽  
Human Erythrocytes ◽  
Transmission Microscopy ◽  
Carbocyanine Dyes ◽  
Host Membrane ◽  
Membrane Components ◽  
20 Nm

We studied the adherence of human erythrocytes to larvae of the intravascular parasite Schistosoma mansoni by transmission microscopy, freeze fracture, and fluorescence techniques. In addition, we used the adherent cells to investigate the problem of host antigen acquisition. Schistosomula were cultured for from 24 to 48 h after transformation in order to clear the remnants of the cercarial glycocalyx. In some cases, the worms were preincubated with wheat germ agglutinin to promote adherence of the erythrocytes. The results were similar with and without the lectin except that more cells attached to the lectin-coated parasites. Erythrocytes adhered within a few hours and, unlike neutrophils, did not fuse with the parasite. A layer of 10-20-nm electron dense material separated the outer leaflets of the tegumental and plasma membranes. In addition, many deformed and lysed cells were seen on the parasite surface. The ability of the worm to acquire erythrocyte membrane constituents was tested with carbocyanine dyes, fluorescein covalently conjugated to glycophorin, monoclonal antibodies against B and H blood group glycolipids, and rabbit alpha-human erythrocyte IgG. In summary, glycophorin, erythrocyte proteins, and glycolipids were not transferred to the parasite membrane within 48 h. Carbocyanine dyes were rapidly transferred to the parasite with or without lectin preincubation. Thus, the dye in the worm membrane came from both adherent and nonadherent cells. These studies suggest that, in the absence of membrane fusion, the parasite may acquire some lipid molecules similar in structure to host membrane glycolipids by simple transfer through the medium but that B and H glycolipids and erythrocyte membrane proteins are not transferred from adhering cells to the worm.

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