Membrane Alterations Induced by Amphiphiles

1989 ◽  
Vol 16 (3) ◽  
pp. 274-280
Author(s):  
Boris Isomaa ◽  
Henry Hägerstrand ◽  
Gun I.L. Paatero

Amphiphilic compounds with distinct apolar and polar parts are readily intercalated into the erythrocyte membrane. When intercalated into the membrane, amphiphiles are probably orientated so that the polar head is at the polar-apolar interface of the lipid bilayer and the hydrophobic part within the apolar core of the bilayer. However, by virtue of their difference in molecular shape from the bulk lipids of the lipid bilayer, it is possible that the intercalated amphiphiles are partly segregated from bulk lipids and accumulate at protein-lipid interfaces in the bilayer, where the packing of the bilayer lipids may be less ordered. Our studies show that amphiphiles, when intercalated into the erythrocyte membrane, trigger alterations in several membrane-connected functions. Some of the alterations induced (decreased osmotic fragility, increased passive potassium fluxes) seem to be due to non-specific interactions of the amphiphiles with the membrane, whereas other functions (ion transport mediated by membrane proteins, regulation of cell shape) seem to be sensitive to particular features of the amphiphiles. Our studies indicate that the intercalation of amphiphiles into the erythrocyte membrane must involve rearrangements within the lipid bilayer. We have suggested that, when intercalated into the lipid bilayer, amphiphiles trigger a rapid formation of non-bilayer phases, which protect the bilayer against a collapse and bring about a trans-bilayer redistribution of intercalated amphiphiles as well as of bilayer lipids. At high sublytic concentrations, this process may also involve a release of microvesicles from the membrane.

2005 ◽  
Vol 127 (38) ◽  
pp. 13316-13323 ◽  
Author(s):  
Lucia Becucci ◽  
Maria Rosa Moncelli ◽  
Renate Naumann ◽  
Rolando Guidelli

2015 ◽  
Vol 93 (4) ◽  
pp. 385-395 ◽  
Author(s):  
Chandrabose Sureka ◽  
Thiyagarajan Ramesh ◽  
Vavamohaideen Hazeena Begum

The aim of the present study was to investigate the protective effects of Sesbania grandiflora flower (SGF) extract on erythrocyte membrane in Streptozotocin (STZ)-induced diabetic rats. Adult male albino rats of Wistar strain, weighing 190–220 g, were made diabetic by an intraperitonial administration of STZ (45 mg/kg). Normal and diabetic rats were treated with SGF, and diabetic rats were also treated with glibenclamide as drug control, for 45 days. In this study plasma insulin and haemoglobin levels were decreased and blood glucose, glycosylated haemoglobin, protein oxidation, lipid peroxidation markers, and osmotic fragility levels were increased in diabetic rats. Moreover, erythrocytes antioxidant enzymes such as superoxide dismutase, catalase, glutathione peroxide, glutathione reductase, glutathione-S-transferase, and glucose-6-phosphate dehydrogenase activities and non-enzymatic antioxidants such as vitamin C, vitamin E, reduced glutathione (GSH), and oxidized glutathione (GSSG) levels were altered. Similarly, the activities of total ATPases, Na+/K+-ATPase, Ca2+-ATPase, and Mg2+-ATPase were also decreased in the erythrocytes of diabetic rats. Administration of SGF to STZ-induced diabetic rats reduced blood glucose and glycosylated haemoglobin levels with increased levels of insulin and haemoglobin. Moreover, SGF reversed the protein and lipid peroxidation markers, osmotic fragility, membrane-bound ATPases activities, and antioxidant status in STZ-induced diabetic rats. These results suggest that SGF could provide a protective effect on diabetes by decreasing oxidative stress-associated diabetic complications.


1999 ◽  
Vol 159 (3) ◽  
pp. 204-213 ◽  
Author(s):  
Anna Y. Bogdanova ◽  
Leila V. Virkki ◽  
Gennadii P. Gusev ◽  
Mikko Nikinmaa

Sangyo Igaku ◽  
1989 ◽  
Vol 31 (6) ◽  
pp. 440-441
Author(s):  
Keiko TAKAHASHI ◽  
Hiroshi YAMAUCHI ◽  
Yukio YAMAMURA ◽  
Yoshiro KUDOU

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Cyril Badaut ◽  
Pimnitah Visitdesotrakul ◽  
Aurélie Chabry ◽  
Pascal Bigey ◽  
Bernard Tornyigah ◽  
...  

AbstractThe Plasmodium falciparum erythrocyte-membrane-protein-1 (PF3D7_1150400/PF11_0521) contains both domain cassette DC13 and DBLβ3 domain binding to EPCR and ICAM-1 receptors, respectively. This type of PfEMP1 proteins with dual binding specificity mediate specific interactions with brain micro-vessels endothelium leading to the development of cerebral malaria (CM). Using plasma collected from children at time of hospital admission and after 30 days, we study an acquisition of IgG response to PF3D7_1150400/PF11_0521 DC13 and DBLβ3_D4 recombinant constructs, and five peptides located within these constructs, specifically in DBLα1.7_D2 and DBLβ3_D4 domains. We found significant IgG responses against the entire DC13, PF11_0521_DBLβ3_D4 domain, and peptides. The responses varied against different peptides and depended on the clinical status of children. The response was stronger at day 30, and mostly did not differ between CM and uncomplicated malaria (UM) groups. Specifically, the DBLβ3 B3-34 peptide that contains essential residues involved in the interaction between PF11_0521 DBLβ3_D4 domain and ICAM-1 receptor demonstrated significant increase in reactivity to IgG1 and IgG3 antibodies at convalescence. Further, IgG reactivity in CM group at time of admission against functionally active (ICAM-1-binding) PF11_0521 DBLβ3_D4 domain was associated with protection against severe anemia. These results support development of vaccine based on the PF3D7_1150400/PF11_0521 structures to prevent CM.


1989 ◽  
Vol 257 (2) ◽  
pp. C270-C276 ◽  
Author(s):  
S. Tongyai ◽  
Y. Rayssiguier ◽  
C. Motta ◽  
E. Gueux ◽  
P. Maurois ◽  
...  

The erythrocyte membrane was investigated in weanling male rats pair fed with magnesium-deficient and control diets for 8 days. Fluorescence polarization studies revealed a 15% increase in the fluidity of membranes from deficient rats. A similar increase in the fluidity of liposomes indicated that protein was not involved. The change was associated with decreased osmotic fragility of intact erythrocytes; the cells lost their biconcavity and had a flattened appearance with surface irregularities. Analysis of the membranes showed decreased amounts of magnesium, cholesterol, and sphingomyelin in the deficient group. The reduced ratios of cholesterol to phospholipid and sphingomyelin to phosphatidylcholine were consistent with the increased fluidity. Addition of physiological amounts of magnesium to the medium rigidified membranes incubated in tris(hydroxymethyl)-aminomethane buffer, and this was prevented by the presence of EDTA. Cross-incubation experiments with erythrocyte ghosts and plasma from the two groups of rats showed that magnesium-deficient plasma increased the fluidity of control ghosts and control plasma rigidified ghosts from magnesium-deficient rats. Addition of sufficient magnesium chloride to raise the magnesium content of deficient plasma to normal had no significant effect. These results show that the increased fluidity of the erythrocyte membrane in magnesium deficiency is due to physicochemical exchange with the plasma. Although magnesium can directly influence membrane fluidity, the change during its deficiency in vivo is mainly mediated indirectly via disturbances in lipid metabolism.


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