Diabetes Mellitus Alters the Effect of Peptide and Protein Ligands on Membrane Fluidity of Blood Platelets

1996 ◽  
Vol 75 (01) ◽  
pp. 147-153 ◽  
Author(s):  
Cezary Watala ◽  
Krzysztof Gwoździński ◽  
Elżbieta Pluskota ◽  
Tadeusz Pietrucha ◽  
Bogdan Walkowiak ◽  
...  
Keyword(s):  
Diabetes Mellitus ◽  
Membrane Proteins ◽  
Membrane Fluidity ◽  
Lipid Bilayer ◽  
Membrane Lipid ◽  
Platelet Membrane ◽  
Lipid Fluidity ◽  
Platelet Membranes ◽  
Membrane Lipid Bilayer ◽  
Membrane Lipid Fluidity

SummaryThe increased nonenzymatic glycosylation of platelet membrane proteins has been suggested to underlie platelet hypersensitivity in diabetes and the relationship of this to the reduced membrane lipid fluidity has been reported. As the modulation in membrane fluidity may determine the degree of accessibility of membrane receptors, the consequent alterations in membrane lipid-protein interactions in diabetes mellitus may also underlie the differentiated effects of various thrombotic and fibrinolytic agents on platelet membrane lipid bilayer.In the present study we employed electron paramagnetic resonance and fluorescence spectroscopy to explore the ligand-induced platelet membrane fluidity changes in diabetic state, i.e. under conditions when the membrane architecture is considerably altered.The yield of the excimer formation of pyrenemaleimide (PM), which depends directly upon the collisional rate and distances between molecules, was elevated in diabetic platelet membranes, thus pointing to the occurrence of some constraints in the structure/conformation of platelet membrane proteins in diabetes mellitus. Such an immobilization of PM was accompanied by the significant elevation in membrane protein gly-cation in diabetic platelets. The effects of various interacting ligands on platelet membrane fluidity were significantly lower in diabetic platelets, and the differences were much more distinct at the lower depths of a lipid bilayer. Nevertheless, the alterations in membrane lipid fluidity observed upon the interaction of a given ligand occurred with an approximately equal frequency in control and diabetic platelets. Moreover, the probability that these alterations were less profound in diabetic platelets was the same for all types of ligands studied. In diabetic patients the interaction of RGDS and tissue-type plasminogen activator with platelet membranes resulted in much smaller reductions of the h+1/h0 parameters in 5-DOXYL-Ste acid-labelled platelets, thus indicating a lesser rigidization of membrane lipid bilayer in diabetes. Likewise, the fluidizing effect of both fibrinogen itself and fibrinogen-derived peptides containing γ-chain carboxy-terminal sequence H-12-V was less pronounced in diabetic platelet membranes.

Platelet membrane lipid fluidity and intraplatelet calcium mobilization in type 2 diabetes mellitus

2009 ◽  
Vol 61 (5) ◽  
pp. 319-326 ◽  
Author(s):  
Cezary Watala ◽  
Magdalena Boncer ◽  
Jacek Golański ◽  
Wiktor Koziołkiewicz ◽  
Zygmunt Trojanowski ◽  
...  
Keyword(s):  
Diabetes Mellitus ◽  
Type 2 Diabetes ◽  
Type 2 Diabetes Mellitus ◽  
Membrane Lipid ◽  
Calcium Mobilization ◽  
Platelet Membrane ◽  
Lipid Fluidity ◽  
Membrane Lipid Fluidity

scholarly journals Anomalous behavior of water inside the SecY translocon

2015 ◽  
Vol 112 (29) ◽  
pp. 9016-9021 ◽  
Author(s):  
Sara Capponi ◽  
Matthias Heyden ◽  
Ana-Nicoleta Bondar ◽  
Douglas J. Tobias ◽  
Stephen H. White
Keyword(s):  
Membrane Proteins ◽  
Lipid Bilayer ◽  
Pyrococcus Furiosus ◽  
Hydrophobic Effect ◽  
Accessible Surface Area ◽  
Anomalous Behavior ◽  
Membrane Lipid ◽  
Nascent Chain ◽  
Membrane Lipid Bilayer ◽  
Dynamics Simulations

The heterotrimeric SecY translocon complex is required for the cotranslational assembly of membrane proteins in bacteria and archaea. The insertion of transmembrane (TM) segments during nascent-chain passage through the translocon is generally viewed as a simple partitioning process between the water-filled translocon and membrane lipid bilayer, suggesting that partitioning is driven by the hydrophobic effect. Indeed, the apparent free energy of partitioning of unnatural aliphatic amino acids on TM segments is proportional to accessible surface area, which is a hallmark of the hydrophobic effect [Öjemalm K, et al. (2011) Proc Natl Acad Sci USA 108(31):E359–E364]. However, the apparent partitioning solvation parameter is less than one-half the value expected for simple bulk partitioning, suggesting that the water in the translocon departs from bulk behavior. To examine the state of water in a SecY translocon complex embedded in a lipid bilayer, we carried out all-atom molecular-dynamics simulations of the Pyrococcus furiosus SecYE, which was determined to be in a “primed” open state [Egea PF, Stroud RM (2010) Proc Natl Acad Sci USA 107(40):17182–17187]. Remarkably, SecYE remained in this state throughout our 450-ns simulation. Water molecules within SecY exhibited anomalous diffusion, had highly retarded rotational dynamics, and aligned their dipoles along the SecY transmembrane axis. The translocon is therefore not a simple water-filled pore, which raises the question of how anomalous water behavior affects the mechanism of translocon function and, more generally, the partitioning of hydrophobic molecules. Because large water-filled cavities are found in many membrane proteins, our findings may have broader implications.

Effects of Proteus mirabilis Lipopolysaccharides with Different O-Polysaccharide Structures on the Plasma Membrane of Human Erythrocytes

2008 ◽  
Vol 63 (5-6) ◽  
pp. 460-468 ◽  
Author(s):  
Michał Arabski ◽  
Krzysztof Gwoździński ◽  
Beata Sudak ◽  
Wiesław Kaca
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Erythrocyte Membrane ◽  
Osmotic Fragility ◽  
Membrane Lipid ◽  
Membrane Properties ◽  
Physical Parameters ◽  
Chemical Structures ◽  
Lipid Fluidity ◽  
Membrane Lipid Fluidity

The effects of O33 and O49 P. mirabilis lipopolysaccharides (LPSs) on human erythrocyte membrane properties were examined. Physical parameters of the plasma membrane, such as membrane lipid fluidity, physical state of membrane proteins, and osmotic fragility, were determined. The fluidity of the lipids was estimated using three spin-labeled stearic acids of doxyl derivatives: 5-doxylstearic acid, 12-doxylstearic acid, and 16-doxylstearic acid. All the applied labels locate to different depths of the lipid layer and provide information on the ordering of phospholipid fatty acyl chain mobility. LPSs O49 increased the membrane lipid fluidity in the polar region of the lipid bilayer as indicated by spin-labeled 5-doxylstearic acid. An increase in fluidity was also observed in the deeper region using 12-doxylstearic acid only for O33 LPSs. The highest concentration of O33 LPSs (1 mg/ml) increased the motion of membrane proteins detected by the spin-label residue of iodoacetamide. These results showed different actions of O33 and O49 LPSs on the plasma membrane due to the different chemical structures of O-polysaccharides. P. mirabilis O33 and O49 LPSs did not induce changes in the membrane cytoskeleton, osmotic fragility and lipid peroxidation of erythrocytes. On the other hand a rise in the content of carbonyl compounds was observed for the highest concentrations of O33 LPS. This result indicated protein oxidation in the erythrocyte membrane. Lipid A, the hydrophobic part of LPS, did not change the membrane lipid fluidity and osmotic fragility of erythrocytes. Smooth and rough forms of P. mirabilis LPSs were tested for their abilities for complement-mediated immunohemolysis of erythrocytes. Only one out of seven LPSs used was a potent agent of complement-mediated hemolysis. It was rough, Ra-type of P. mirabilis R110 LPS. The O-polysaccharide-dependent scheme of reaction is presented.

scholarly journals Reversible penetration of α-glutathione S-transferase into biological membranes revealed by photosensitized labelling in situ

1998 ◽  
Vol 335 (3) ◽  
pp. 597-604 ◽  
Author(s):  
Natasha MEREZHINSKAYA ◽  
Gemma A. J. KUIJPERS ◽  
Yossef RAVIV
Keyword(s):  
Influenza Virus ◽  
Membrane Proteins ◽  
Lipid Bilayer ◽  
Biological Membranes ◽  
Membrane Lipid ◽  
Integral Membrane Proteins ◽  
Glutathione S Transferase ◽  
Membrane Lipid Bilayer ◽  
Influenza Virus Haemagglutinin ◽  
Virus Haemagglutinin

Fluorescent lipid analogue 3,3´-dioctadecyloxacarbocyanine incorporated into biological membranes was used to induce photoactivation of a hydrophobic probe 5-[125I]iodonaphthyl-1-azide (125INA) by energy transfer and to thereby confine subsequent radiolabelling of proteins to the lipid bilayer. This approach was applied in bovine chromaffin cells to discover cytosolic proteins that reversibly penetrate into membrane domains. α-Glutathione S-transferase (α-GST) was identified as the only labelled protein in bovine chromaffin-cell cytosol, indicating that it inserts reversibly into the membrane lipid bilayer. The selectivity of the labelling towards the lipid bilayer is demonstrated by showing that influenza virus haemagglutinin becomes labelled by 125INA only after the insertion of this protein into the target membrane. The molar 125INA:protein ratio was used as a quantitative criterion for evaluation of the penetration of proteins into the membrane lipid bilayer. This ratio was calculated for four integral membrane proteins and four soluble proteins that interact with biological membranes. The values for four integral membrane proteins (erythrocyte anion transporter, multidrug transporter gp-170, dopamine transporter and fusion-competent influenza virus haemagglutinin) were 1, 8, 2 and 2, respectively, whereas for soluble proteins (annexin VII, protein kinase C, BSA and influenza virus haemagglutinin) the values were 0.002, 0, 0.002 and 0.02, respectively. The molar ratio for α-GST was found to be 1, compatible with the values obtained for integral membrane proteins.

Decreased Platelet Membrane Fluidity Due to Glycation or Acetylation of Membrane Proteins

1992 ◽  
Vol 68 (05) ◽  
pp. 577-582 ◽  
Author(s):  
Peter D Winocour ◽  
Cezary Watala ◽  
Dennis W Perry ◽  
Raelene L Kinlough-Rathbone
Keyword(s):  
Membrane Proteins ◽  
Membrane Fluidity ◽  
High Glucose ◽  
Acetyl Chloride ◽  
Cell Function ◽  
Platelet Membrane ◽  
Molar Ratio ◽  
Diabetic Patients ◽  
Platelet Membranes

SummaryPlatelets from diabetic subjects and animals are hypersensitive to agonists in vitro. Membrane fluidity modulates cell function and previously we observed reduced membrane fluidity in platelets from diabetic patients associated with hypersensitivity to thrombin. We previously reported that decreased fluidity of isolated platelet membranes from diabetic patients is associated with increased glycation of platelet membrane proteins, but not with any change in the cholesterol to phospholipid molar ratio. We have now examined in vitro whether incubation of platelet membranes in a high glucose medium causes sufficient glycation to reduce membrane fluidity. Incubation of platelet membranes from control subjects in a high glucose (16.1 mM) medium for 10 days at 37° C led to an increase in the extent of glycation of membrane proteins and a decrease in membrane fluidity (indicated by an increase in steady state fluorescence polarization); most of the changes occurred within the first 3 days of incubation. Incubation of platelet membranes with 5.4 mM glucose had less effect. In contrast, incubation of platelet membranes with the same concentrations of 1–0-methylglucose did not cause a change in either the extent of glycation of proteins or membrane fluidity. We also determined if acetylation by aspirin or acetyl chloride of the sites available for glycation on platelet membrane proteins leads to a similar reduction in membrane fluidity. Pretreatment of platelet membranes with aspirin or acetyl chloride diminished the extent of glycation that occurred when platelet membranes were subsequently incubated with glucose, but membrane fluidity was reduced even in the absence of glucose; subsequent incubation with glucose caused no further reduction in membrane fluidity. Similar results were obtained when red blood cells were incubated with high concentrations of glucose or methyl glucose either with or without pretreatment with aspirin or acetyl chloride. Further experiments using platelet membranes showed that the reduction in membrane fluidity due to aspirin was independent of its acetylating effect on platelet cyclo-oxygenase. Ingestion of aspirin also caused a reduction in membrane fluidity of platelets. Therefore, glycation of platelet membrane proteins reduces membrane fluidity, but the effect results from occupation of the sites available for glycation and not the presence of glucose moieties per se at these sites. Acetylation of platelet membrane proteins either in vitro or in vivo also reduces membrane fluidity; this effect is not associated with platelet hypersensitivity to thrombin.

scholarly journals PHLIP ARG-Mutant Interactions with the Membrane Lipid Bilayer

2021 ◽  
Vol 120 (3) ◽  
pp. 232a
Author(s):  
Hannah M. Visca ◽  
Oleg A. Andreev ◽  
Yana K. Reshetnyak
Keyword(s):  
Lipid Bilayer ◽  
Membrane Lipid ◽  
Membrane Lipid Bilayer

Time-Course of Changes in the Plasma–Membrane Lipid Bilayer and Cellular Ultrastructure Induced by Tumour Necrosis Factor-α in K 562 and Daudi Cells

1995 ◽  
Vol 23 (4) ◽  
pp. 254-263 ◽  
Author(s):  
M Marutaka ◽  
H Iwagaki ◽  
K Mizukawa ◽  
N Tanaka ◽  
K Orita
Keyword(s):  
Plasma Membrane ◽  
Cell Membrane ◽  
Membrane Fluidity ◽  
Time Course ◽  
Membrane Lipid ◽  
Plasma Membrane Lipid ◽  
Membrane Lipid Bilayer ◽  
Cell Membrane Fluidity ◽  
K 562 Cells ◽  
Factor Α

The time-course of changes in the plasma-membrane lipid bilayer induced by tumour necrosis factor-α (TNF) were investigated in cultured cells using spin-label electron-spin-resonance techniques. Treatment of K 562 cells, a human chronic myelocytic leukaemia cell line, in suspension culture with TNF for up to 6 h caused an initial increase in cell-membrane fluidity, which returned to the control level after 12 h of treatment. After 24 h of treatment, the cell-membrane fluidity had decreased and this decrease was maintained after 48 h of treatment. In Daudi cells, a human malignant lymphoma cell line, TNF, did not induce any changes in cell-membrane fluidity, indicating that the effect of TNF on membrane structure is cell-specific. The early and transient change in membrane fluidity in K 562 cells is probably related to signal generation, while the later, persistent change may reflect the phenotype of TNF-treated cells, in particular, changes in the plasma membrane-cytoplasmic complex. Histochemical electron microscopic studies indicated that the membrane fluidity changes induced by TNF have an ultrastructural correlate.

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