scholarly journals Solubilization of Giant Vesicles Composed of Erythrocyte Lipid Extracts and of Ternary Lipid Mixtures by Triton X-100

2014 ◽  
Vol 106 (2) ◽  
pp. 501a-502a
Author(s):  
Bruna R. Casadei ◽  
Amanda C. Caritá ◽  
Cleyton C. Domingues ◽  
Eneida de Paula ◽  
Karin A. Riske
eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Kamila Oglęcka ◽  
Padmini Rangamani ◽  
Bo Liedberg ◽  
Rachel S Kraut ◽  
Atul N Parikh

Giant lipid vesicles are closed compartments consisting of semi-permeable shells, which isolate femto- to pico-liter quantities of aqueous core from the bulk. Although water permeates readily across vesicular walls, passive permeation of solutes is hindered. In this study, we show that, when subject to a hypotonic bath, giant vesicles consisting of phase separating lipid mixtures undergo osmotic relaxation exhibiting damped oscillations in phase behavior, which is synchronized with swell–burst lytic cycles: in the swelled state, osmotic pressure and elevated membrane tension due to the influx of water promote domain formation. During bursting, solute leakage through transient pores relaxes the pressure and tension, replacing the domain texture by a uniform one. This isothermal phase transition—resulting from a well-coordinated sequence of mechanochemical events—suggests a complex emergent behavior allowing synthetic vesicles produced from simple components, namely, water, osmolytes, and lipids to sense and regulate their micro-environment.


Langmuir ◽  
2014 ◽  
Vol 31 (1) ◽  
pp. 378-386 ◽  
Author(s):  
Bruno Mattei ◽  
Ana D. C. França ◽  
Karin A. Riske
Keyword(s):  

2009 ◽  
Vol 96 (3) ◽  
pp. 161a ◽  
Author(s):  
Laura Rodriguez Arriaga ◽  
John Ipsen ◽  
Alejandra Garcia ◽  
Steffen Härtel ◽  
Francisco Monroy ◽  
...  

2012 ◽  
Vol 1818 (3) ◽  
pp. 666-672 ◽  
Author(s):  
Christopher K. Haluska ◽  
Mauricio S. Baptista ◽  
Adjaci U. Fernandes ◽  
André P. Schroder ◽  
Carlos M. Marques ◽  
...  

Langmuir ◽  
2017 ◽  
Vol 33 (29) ◽  
pp. 7312-7321 ◽  
Author(s):  
Amanda C. Caritá ◽  
Bruno Mattei ◽  
Cleyton C. Domingues ◽  
Eneida de Paula ◽  
Karin A. Riske

2014 ◽  
Vol 106 (11) ◽  
pp. 2417-2425 ◽  
Author(s):  
Bruna R. Casadei ◽  
Cleyton C. Domingues ◽  
Eneida de Paula ◽  
Karin A. Riske

Author(s):  
S.W. French ◽  
N.C. Benson ◽  
C. Davis-Scibienski

Previous SEM studies of liver cytoskeletal elements have encountered technical difficulties such as variable metal coating and heat damage which occurs during metal deposition. The majority of studies involving evaluation of the cell cytoskeleton have been limited to cells which could be isolated, maintained in culture as a monolayer and thus easily extracted. Detergent extraction of excised tissue by immersion has often been unsatisfactory beyond the depth of several cells. These disadvantages have been avoided in the present study. Whole C3H mouse livers were perfused in situ with 0.5% Triton X-100 in a modified Jahn's buffer including protease inhibitors. Perfusion was continued for 1 to 2 hours at ambient temperature. The liver was then perfused with a 2% buffered gluteraldehyde solution. Liver samples including spontaneous tumors were then maintained in buffered gluteraldehyde for 2 hours. Samples were processed for SEM and TEM using the modified thicarbohydrazide procedure of Malich and Wilson, cryofractured, and critical point dried (CPD). Some samples were mechanically fractured after CPD.


1990 ◽  
Vol 63 (02) ◽  
pp. 303-311
Author(s):  
Tone Børsum

SummaryHuman endothelial cells isolated from umbilical cordswere solubilized in Triton X-100 and examined by crossedimmunoelec-trophoresis using rabbit antiserum against endothelial cells. Endogenous labelling of the endothelialcell proteins with 14Cmannose followed by crossed immunoelectrophoresis and autoradiography revealed about 10 immunoprecipitates. Four of these endothelial cell glycoproteins were labelled by lactoperoxidase catalyzed iodination and thus were surface located. Three of the surface located glycoproteins showed reduced electrophoretic mobility after incubation of the endothelial cells with neuraminidase and were therefore sialoglycoproteins. Amphiphilicity of endothelial cell glycoproteins was studied by crossed hydrophobic interaction immunoelectrophoresis with phenyl-Sepharose in the intermediate gel. Amphiphilic proteins also show increasing electrophoretic migration velocity with decreasing concentration of Triton X-100 in the first dimension gels. Five of the endothelial cell glycoproteins were shown to be amphiphilic using these two techniques.Two monoclonal antibodies against the platelet glycoprotein complex Ilb-IIIa and glycoprotein IlIa, respectively, reacted with the same precipitate of endothelial cells. When a polyclonal antibody against the platelet glycoprotein complex Ilb-IIIa was incorporated into the intermediate gel the position of two endothelial cell precipitates were lowered. One of these was a sialoglycoprotein.


1974 ◽  
Vol 32 (02/03) ◽  
pp. 457-464
Author(s):  
Paul C. French ◽  
Jan J. Sixma ◽  
Holm Holmsen

SummaryAdenine uptake into isolated platelet membranes had about the same Km (151 ± 21 • 9 nM) as uptake into intact cells (159 ± 21 nM) and was also competitively inhibited by papaverine and hypoxanthine. No uptake occurred at 0° and accumulated adenine was converted to AMP. AMP was not firmly bound to protein as judged by chromatography of triton X-100 solubilized membranes on Sephadex G25. The pH optimum for adenine uptake was at pH 5-5. Exogenous 5-phosphoribosyl-l-pyrophos- phate strongly stimulated uptake. These data may be explained by uptake of adenine by facilitated diffusion followed by conversion to AMP by adenine phosphoribosyltransferase but group translocation cannot be entirely excluded.


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