Size-selective breaking of the core-shell structure of gallium nanoparticles.

Core-shell gallium nanoparticles (Ga NPs) have recently been proposed as an ultraviolet plasmonic material for different applications but only at room temperature. Here, the thermal stability as a function of the size of the NPs is reported over a wide range of temperatures. We analyze the chemical and structural properties of the oxide shell by x-ray photoelectron spectroscopy and atomic force microscopy. We demonstrate the inverse dependence of the shell breaking temperature with the size of the NPs. Spectroscopic ellipsometry is used for tracking the rupture and its mechanism is systematically investigated by scanning electron microscopy, grazing incidence x-ray diffraction and cathodoluminescence. Taking advantage of the thermal stability of the NPs, we perform complete oxidations that lead to homogenous gallium oxide NPs. Thus, this study set the physical limits of Ga NPs to last at high temperatures, and opens up the possibility to achieve totally oxidized NPs while keeping their sphericity.

Tunable plasmonic resonance of gallium nanoparticles by thermal oxidation at low temperaturas.

The effect of the oxidation of gallium nanoparticles (Ga NPs) on their plasmonic properties is investigated. Discrete dipole approximation has been used to study the wavelength of the out-of-plane localized surface plasmon resonance in hemispherical Ga NPs, deposited on silicon substrates, with oxide shell (Ga2O3) of different thickness. Thermal oxidation treatments, varying temperature and time, were carried out in order to increase experimentally the Ga2O3 shell thickness in the NPs. The optical, structural and chemical properties of the oxidized NPs have been studied by spectroscopic ellipsometry, scanning electron microscopy, grazing incidence x-ray diffraction and x-ray photoelectron spectroscopy. A clear redshift of the peak wavelength is observed, barely affecting the intensity of the plasmon resonance. A controllable increase of the Ga2O3 thickness as a consequence of the thermal annealing is achieved. In addition, simulations together with ellipsometry results have been used to determine the oxidation rate, whose kinetics is governed by a logarithmic dependence. These results support the tunable properties of the plasmon resonance wavelength in Ga NPs by thermal oxidation at low temperatures without significant reduction of the plasmon resonance intensity.

Evidence that cytosolic phospholipase A2 is down-regulated by protein kinase C in intact human platelets stimulated with fluoroaluminate.

We reported that protein kinase C (PKC) inhibitors increase the release of arachidonic acid induced by fluoroaluminate (AlF4-), an unspecific G-protein activator, in intact human platelets. Now we demonstrate that this effect is independent of the extracellular Ca2+ concentration and that AlF4(-)-induced release of AA is abolished by BAPTA, an intracellular Ca2+ chelator, even in the presence of GF 109203X, a specific and potent PKC inhibitor. This compound also blocks the liberation of the secretory phospholipase A2 in the extracellular medium, indicating that this enzyme is not involved in the potentiation of arachidonic acid by PKC inhibitors. On the other hand, the latter effect is completely abolished by treatment of platelets with AACOCF3, a specific inhibitor of cytosolic phospholipase A2 (cPLA2). These observations indicate that cPLA2 is responsible for the AlF4(-)-induced release of arachidonic acid by a mechanism that is down-regulated by PKC.

Effect of dermatan sulphate on activated partial thromboplastin time determined with different reagents.

Five widely used activated partial thromboplastin time (APTT) reagents (Actin-FS, Actin-FSL, Hemolab Silimat, IL-Test APTT Ellagic Acid and Thrombofax Activated) were compared for their sensitivity and precision in measuring the effect of dermatan sulphate on blood coagulation. On each of 4 days, aliquots of the same normal human plasma pool were mixed with dermatan sulphate (MF701) at concentrations ranging from 10 to 100 micrograms/ml, and APTT was measured in duplicate with all reagents by a photo-optical coagulometer. The order of testing between and within reagents was changed every day. The relationship of APTT ratio to dermatan sulphate concentration was linear with all the reagents. There were statistically significant differences between reagents in their sensitivity to DS, as reflected by linear regression slopes. IL-Test was the most sensitive reagent. At dermatan sulphate concentrations of 20, 50, and 80 micrograms/ml APTT ratio ranged from 1.5 to 1.7, 1.9 to 2.3 and 2.3 to 2.9, respectively, according to the reagent. The lambda coefficient and coefficient of variation derived from regression analysis, both reflecting assay precision, ranged from 0.57 to 0.71 and from 4.6 to 5.1%, respectively, with all but the least precise reagent. The best sensitivity/precision balance was displayed by IL-Test. The APTT reagent should therefore be standardized, with special regard to sensitivity to DS, when testing the relationship of dermatan sulphate clinical effects to APTT response.

Protein kinase C inhibitors enhance G-protein induced phospholipase A2 activation in intact human platelets.

Washed intact human platelets were prelabelled with [3H]arachidonic acid ([3H]AA) and stimulated with thrombin or with AlF4-, a known unspecific activator of G-proteins. Both stimuli induced the liberation of [3H]AA, the release of beta-thromboglobulin (beta-TG) and platelet aggregation. PMA did not induce liberation of [3H]AA although it induced beta-TG release and aggregation; preincubation with PMA did not modify significantly the amounts of [3H]AA and beta-TG released by thrombin or AlF4-. Different inhibitors of PKC (staurosporine, H-7 and calphostin C) increased the release of [3H]AA and inhibited beta-TG release and aggregation induced by AlF4- but they had no effect when platelets were stimulated with thrombin (0.5 U/ml). Calphostin C was able to release [3H]AA by itself without inducing aggregation of beta-TG release. Okadaic acid (a serine/threonine phosphoprotein phosphatase inhibitor) greatly inhibited the release of [3H]AA, beta-TG and aggregation in AlF4--stimulated platelets. These results indicate the presence of a G-protein mediated mechanism for the activation of a platelet phospholipase A2 which is negatively affected by a protein kinase, sensible to putative inhibitors of protein kinase C, and it is activated by a protein phosphatase, sensible to okadaic acid.