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Biomedical subjects

E Bertoli

Publications and source records attributed to E Bertoli.

At least 91 records · Page 5Linked to original sources

Effect of general anesthesia on syncytiotrophoblast plasma membranes from human placenta.

This investigation shows that a general anesthetic produces similar effects in vivo and in vitro. Anesthesia with a barbituric drug, Thiopental, induces an increase in membrane fluidity and a decrease in the activity of acetylcholinesterase in syncytiotrophoblast plasma membranes (SPM) obtained from placentas after caesarean section. The same effects can be reproduced in vitro after anesthetic addition to the isolated plasma membranes. Morphological and freeze-fracturing studies also suggest that membrane protein components are affected by anesthetics.

Acetylcholinesterase↗

Altered properties of platelet membrane in childhood obesity.

Using 1-(4-trimethylammoniumphenyl)-6-phenyl-1,3,5,hexatriene (TMA-DPH) as fluorescent probe, we have studied platelet membrane fluidity and thrombin induced exocytosis in ten obese children and fifteen controls. Our results indicate a decrease of membrane fluidity, as shown by an increase of fluorescence anisotropy, in platelets from obese patients in comparison with the controls. Associated with the changes in membrane fluidity, platelets of obese subjects showed a decreased sensitivity to thrombin stimulation.

Adolescent↗

Erythrocyte membrane heterogeneity studied using 1,6-diphenyl-1,3,5-hexatriene fluorescence lifetime distribution.

The fluorescence decay of 1,6-diphenyl-1,3,5-hexatriene has been used to characterize the structural organization of erythrocyte membranes. At 37 degrees C a large fraction of the decay (0.96) is associated with a lifetime value of 11.31 ns, while a minor fraction has a short lifetime of 2.63 ns. The distribution analysis approach has shown that the 11 ns component can be described using a Lorentzian distribution function having a full width at half maximum of 0.27 ns. The width of this component is associated with the membrane structural organization since liposomes from erythrocyte total lipid extract exhibit a narrower width. Moreover the distribution width is sensitive to different treatments of erythrocyte membrane.

Diphenylhexatriene↗

Changes of membrane fluidity in erythrocytes of obese children: a spin label study.

Red blood cells depend on circulating lipoproteins for the turnover of membrane phospholipids. Thus abnormalities in lipid and lipoprotein metabolism are frequently associated with changes in composition and fluidity of erythrocyte membranes. Using the electron spin resonance technique we studied the physical state of erythrocyte membranes from 15 obese children with a body mass index ranging from 22.8 to 34 kg . m-2 and slight alterations of plasma lipids. The spin labels used, 5-doxylstearate and 16-doxylstearate, have shown an increase of the order parameter and of the correlation time, respectively. These observations indicate a decrease of fluidity at the surface and in the hydrophobic core of erythrocyte membranes from obese subjects. The results are statistically significant and they are discussed in relation to clinical aspects of childhood obesity. Studies on erythrocyte membrane molecular organization could represent a sensitive way to find out small metabolic alterations hardly detectable with compositional studies.

Adolescent↗

Fluidizing effect of endogenous ubiquinone in bovine heart mitochondrial membranes.

Extraction of endogenous ubiquinone from lyophilized beef heart mitochondria results in increases of both the order parameter of the spin label 5-NS and of the rotational correlation time of 16-NS; reconstitution with the pentane extract results in restoration of the original spectral parameters. On the other hand, addition of purified ubiquinone homologs restores the original spectra only in the case of 16-NS, whereas the order parameter of 5-NS is restored by addition of mixed phospholipids. The same amounts of ubiquinone homologs incorporated in mixed phospholipid vesicles induce much lower effects. It is suggested that ubiquinone in mitochondria is intercalated with the lipid chains of the membrane in such a way to perturb the fluidity of the hydrophobic core.

Animals↗

Characterization of sulphydryl groups of the mitochondrial phosphate translocator by a maleimide spin label.

A maleimide spin label strongly inhibits the phosphate/H+ symporter of rat liver mitochondria. While inducing half-maximal inhibition of transport, the spin label reacts preferentially with the SH groups of the carrier, which are at least of two types. One type of SH group is localized close to the surface of the membrane and its environment does not significantly influence the mobility of the probe. The second type of SH group is buried in the membrane, is not accessible to ascorbate or chromium oxalate and its environment greatly restricts the motion of the probe.

Animals↗

The reconstitution of oxidative phosphorylation in mitochondria isolated from a ubiquinone-deficient mutant of Saccharomyces cerevisiae.

Mitochondria, isolated from the ubiquinone-deficient nuclear mutant of Saccharomyces cerevisiae E3-24, are practically unable to oxidize exogenous substrates. Respiratory activity, coupled to ATP synthesis, can, however, be reconstituted by the simple addition of ethanolic solutions of ubiquinones. A minimal length of the isoprenoid side chain (greater than or equal to 3) was required for the restoration. Saturation of the reconstitution required a large amount of exogeneous ubiquinone, in excess over the normal content present in the mitochondria of the wild type strain. A similar pattern of reconstituted activities could be also obtained using sonicated inverted particles. Mitochondria and sonicated particles are also able to carry out a dye-mediated electron flow coupled to ATP synthesis in the absence of added ubiquinone, using ascorbate or succinate as electron donor. This demonstrates that the energy conserving mechanism at the third coupling site of the respiratory chain is fully independent of the presence of the large mobile pool of ubiquinone in the membrane.

Adenosine Triphosphate↗

Electron paramagnetic resonance studies on the fluidity and surface dynamics of egg phosphatidylcholine vesicles containing gangliosides.

The influence of different gangliosides (GM1, GD1a, GT1b) on the fluidity and surface dynamics of phosphatidylcholine small unilamellar vesicles was studied by electron paramagnetic resonance. 5- and 16-nitroxystearic acid, sounding respectively the region close to the surface and that close to the hydrophobic core of the vesicle, were employed as spin-label probes. The signals released by 5-nitroxystearic acid showed that the presence of gangliosides reduced the mobility of the hydrocarbon chains around the probe. The effect increased by increasing ganglioside concentration, and diminished from GM1 to GD1a and GT1b. The decrease of membrane fluidity was also monitored by the 16-nitroxystearic acid probe. On addition of Ca2+ the fluidity of ganglioside-containing vesicles (as signalled by the 5-nitroxystearic acid probe) promptly decreased, therefore returning slowly to the original value. It is suggested that gangliosides cause strong side-side head group interactions on the bilayer surface--between ganglioside oligosaccharide chains and between ganglioside and phosphatidylcholine polar portions--which lead the lipid chains to assembly in a more rigid fashion. The influence of Ca2+ is interpreted as due to lateral phase separation in the vesicle membrane. This phenomenon can be related to the formation or stabilization of ganglioside clusters on the vesicle surface.

Animals↗

Interaction between ubiquinone and ATPase in mitochondrial membranes.

The extraction of ubiquinone from mitochondrial membranes produces alterations of ATPase activity including a reversible loss of oligomycin sensitivity which is restored by long-chain Q-homologs, Short-chain ubiquinones like Q3 produce a loss of oligomycin and dicyclohexyl carbodiimide (DCCD) sensitivity in submitochondrial particles. The effect shows uncompetitive or noncompetitive Kinetics with respect to oligomycin or DCCD respectively. Long-chain ubiquinones have a competitive effect with Q3, thus restoring oligomycin sensitivity; they behave, however, in about the same way as Q3 in lowering the DCCD sensitivity in submitochondrial particles. On the basis of these observations we suggest that ubiquinone may be a physiological modulator of ATPase activity in the mitochondrial membrane.

Adenosine Triphosphatases↗