Browsing
     by title


0-9 A B C D E F G H I J K L M N O P Q R S T U V W X Y Z

or enter first few letters:   
OK
Full Text
Peer Reviewed
See detailElectron microscopic study of measles virus infection: unusual antibody-triggered redistribution of antigens on giant cells
Hooghe-Peters, Elisabeth L.; Rentier, Bernard ULg; Dubois-Dalcq, Monique

in Journal of Virology (1979), 29(2), 666-676

Vero cells infected with measles virus fuse to form multinucleated cells which incorporated virus- specific antigens in their membrane. The distribution of these antigens was analyzed after a brief ... [more ▼]

Vero cells infected with measles virus fuse to form multinucleated cells which incorporated virus- specific antigens in their membrane. The distribution of these antigens was analyzed after a brief treatment with human anti-measles immunoglobulin G, using autoradiography and immunoperoxidase labeling combined with transmission and scanning electron microscopy. Virus-specific antigens were distributed over the entire surface of giant cells treated at 4°C with human anti-measles immunoglobulin G and labeled Protein A. When cells were shifted to 37°C, labeled antigen-antibody complexes were redistributed in two stages. Patch formation occurred in 5 to 15 min. Later, antigen- antibody complexes became concentrated in a paracentral "ring" rather than typical caps. Patch formation occurred in the presence of metabolic inhibitors, whereas ring formation was inhibited by metabolic inhibitors. These rings contained membrane folds, villi, and viral buds, whereas the rest of the membrane was smooth. In addition, shedding, endocytosis of antigen-antibody complexes, and reexpression of antigens were observed. Antibodies to nonviral membrane antigens induced the same pattern of redistribution. Infected cells treated with anti-measles Fab' fragments maintained a homogeneous distribution of label throughout the experiments. In conclusion, intact immunoglobulins, but not Fab' fragments, were able to induce a dramatic redistribution of viral antigen on the membrane of giant cells infected with measles virus. [less ▲]

Detailed reference viewed: 28 (5 ULg)
Full Text
Peer Reviewed
See detailElectron microscopical investigations of hexagonal phase precipitation in Zn---12 wt% Al---1 wt% Cu and Zn---27 wt% Al---2 wt% Cu alloys
Rachev, P.; Terziev, L.; Lecomte-Beckers, Jacqueline ULg et al

in Acta Metallurgica et Materialia (1991), 39(9), 2177-2182

In Zn---12 wt% Al---1 wt% Cu and Zn---27 wt% Al---2 wt%Cu alloys aged at 100° and 250°C the precipitation of h.c.p. phases was studied by means of transmission electron microscopy. The presence of the ... [more ▼]

In Zn---12 wt% Al---1 wt% Cu and Zn---27 wt% Al---2 wt%Cu alloys aged at 100° and 250°C the precipitation of h.c.p. phases was studied by means of transmission electron microscopy. The presence of the metastable ηm and ηx-phases was established using the Moiré pattern method. The ηm → η phase transition was observed. Screw dislocations are visualized in (114) with b logical and {220} in η phase precipitates by means of Moiré fringes. [less ▲]

Detailed reference viewed: 36 (7 ULg)
Peer Reviewed
See detailElectron microscopy on Banzi Virus particle and its development in the sucking mice brains
Calberg-bacq, C. M.; Rentier-Delrue, Françoise ULg; Osterrieth, P. et al

in Journal of Ultrastructure Research (1975)

Detailed reference viewed: 9 (1 ULg)
Peer Reviewed
See detailElectron microscopy proves Jo-1 antigen to be predominantly cytoplasmic but also nuclear.
Thiry, Marc ULg; Humbel, R.; Dicato, M. et al

in Biomedicine & Pharmacotherapy (1988), 42(7), 469-71

The Jo-1 antigen is a specific marker for autoimmune myositis with an excellent correlation with associated interstitial lung disease. Using an electron microscopy immunogold technique, we were able to ... [more ▼]

The Jo-1 antigen is a specific marker for autoimmune myositis with an excellent correlation with associated interstitial lung disease. Using an electron microscopy immunogold technique, we were able to show that the antigen was predominantly cytoplasmic. [less ▲]

Detailed reference viewed: 12 (1 ULg)
Full Text
Peer Reviewed
See detailElectron partitioning between the two branching quinol-oxidizing pathways in Acanthamoeba castellanii mitochondria during steady-state state 3 respiration.
Jarmuszkiewicz, W.; Sluse-Goffart, C.; Hryniewiecka, L. et al

in Journal of Biological Chemistry (1997), 273(17), 10174-10180

Amoeba mitochondria possess a respiratory chain with two quinol-oxidizing pathways: the cytochrome pathway and the cyanide-resistant alternative oxidase pathway. The ADP/O method, based on the non ... [more ▼]

Amoeba mitochondria possess a respiratory chain with two quinol-oxidizing pathways: the cytochrome pathway and the cyanide-resistant alternative oxidase pathway. The ADP/O method, based on the non-phosphorylating property of alternative oxidase, was used to determine contributions of both pathways in overall state 3 respiration in the presence of GMP (an activator of the alternative oxidase in amoeba) and succinate as oxidizable substrate. This method involves pair measurements of ADP/O ratios plus and minus benzohydroxamate (an inhibitor of the alternative oxidase). The requirements of the method are listed and verified. When overall state 3 respiration was decreased by increasing concentrations of n-butyl malonate (a non-penetrating inhibitor of succinate uptake), the quinone reduction level declined. At the same time, the alternative pathway contribution decreased sharply and became negligible when quinone redox state was lower than 50%, whereas the cytochrome pathway contribution first increased and then passed through a maximum at a quinone redox state of 58% and sharply decreased at a lower level of quinone reduction. This study is the first attempt to examine the steady-state kinetics of the two quinol-oxidizing pathways when both are active and to describe electron partitioning between them when the steady-state rate of the quinone-reducing pathway is varied. [less ▲]

Detailed reference viewed: 14 (4 ULg)
Full Text
Peer Reviewed
See detailElectron photodetachment dissociation of DNA anions with covalently or noncovalently bound chromophores
Gabelica, Valérie ULg; Rosu, Frédéric ULg; De Pauw, Edwin ULg et al

in Journal of the American Society for Mass Spectrometry (2007), 18(11), 1990-2000

Double stranded DNA multiply charged anions coupled to chromophores were subjected to UV-Vis photoactivation. in a quadrupole ion trap mass spectrometer. The chromophores included noncovalently bound ... [more ▼]

Double stranded DNA multiply charged anions coupled to chromophores were subjected to UV-Vis photoactivation. in a quadrupole ion trap mass spectrometer. The chromophores included noncovalently bound minor groove binders (activated in the near UV), noncovalently bound intercalators (activated with visible light), and covalently linked fluorophores and quenchers (activated at their maximum absorption wavelength). We found that the activation of only chromophores having long fluorescence lifetimes did result in efficient electron photodetachment from the DNA complexes. In the case of ethidium-dsDNA complex excited at 500 nm, photodetachment is a multiphoton process. The MS3 fragmentation of radicals produced by photodetachment at lambda = 260 nm (DNA excitation) and by photodetachment at lambda > 300 nm (chromophore excitation) were compared. The radicals keep no memory of the way they were produced. A weakly bound noncovalent ligand (m-amsacrine) allowed probing experimentally that a fraction of the electronic internal energy was converted into vibrational internal energy. This fragmentation channel was used to demonstrate that excitation of the quencher DABSYL resulted in internal conversion, unlike the fluorophore 6-FAM. Altogether, photodetachment of the DNA complexes upon chromophore excitation can be interpreted by the following mechanism: (1) ligands with sufficiently long excited-state lifetime undergo resonant two-photon excitation to reach the level of the DNA excited states, then (2) the excited-state must be coupled to the DNA excited states for photodetachment to occur. Our experiments also pave the way towards photodissociation probes of biomolecule conformation in the gas-phase by Forster resonance energy transfer (FRET). [less ▲]

Detailed reference viewed: 68 (5 ULg)
Full Text
Peer Reviewed
See detailElectron photodetachment dissociation of DNA polyanions in a quadrupole ion trap mass spectrometer
Gabelica, Valérie ULg; Tabarin, Thibault; Antoine, Rodolphe et al

in Analytical Chemistry (2006), 78(18), 6564-6572

We hereby explore the effects of irradiating DNA polyanions stored in a quadrupole ion trap mass spectrometer with an optical parametric oscillator laser between 250 and 285 nm. We studied DNA 6-20-mer ... [more ▼]

We hereby explore the effects of irradiating DNA polyanions stored in a quadrupole ion trap mass spectrometer with an optical parametric oscillator laser between 250 and 285 nm. We studied DNA 6-20-mer single strands and 12-base pair double strands. In all cases, laser irradiation causes electron detachment from the multiply charged DNA anions. Electron photodetachment efficiency directly depends on the number of guanines in the strand, and maximum efficiency is observed between 260 and 275 nm. Subsequent collision-induced dissociation (CID) of the radical anions produced by electron photodetachment results in extensive fragmentation. In addition to neutral losses, a large number of fragments from the w, d, a*, and z* ion series are obtained, contrasting with the w and (a-base) ion series observed in regular CID. The major advantage of this technique, coined electron photodetachment dissociation (EPD) is the absence of internal fragments, combined with good sequence coverage. EPD is therefore a highly promising approach for de novo sequencing of oligonucleotides. EPD of nucleic acids is also expected to give specific radical-induced strand cleavages, with conservation of other fragile bonds, including noncovalent bonds. In effect, preliminary results on a DNA hairpin and on double strands suggest that EPD could also be used to probe intra- and intermolecular interactions in nucleic acids. [less ▲]

Detailed reference viewed: 63 (1 ULg)
See detailElectron Photodetachment of DNA Polyanions: Photoelectron Spectroscopy and UV Action Spectroscopy
Gabelica, Valérie ULg; Rosu, Frédéric ULg; De Pauw, Edwin ULg et al

Conference (2008, April 15)

DNA polyanions trapped in a mass spectrometer undergo electron detachment following irradiation with UV light [1-3]. Electron photodetachment is a 1-photon process, and its efficiency depends on: - The ... [more ▼]

DNA polyanions trapped in a mass spectrometer undergo electron detachment following irradiation with UV light [1-3]. Electron photodetachment is a 1-photon process, and its efficiency depends on: - The nature of the DNA bases: guanine-containing strands are the most prone to electron photodetachment, followed by adenine, cytosine, and finally thymine. - The excitation wavelength: electron detachment is maximum around 260 nm, corresponding to base excitation. - The charge of the polyanion: higher charge state ions undergo more efficient electron detachment because of the Coulombic repulsion. Here we will discuss the electron photodetachment mechanism in the light of the most recent experimental results. Because the base-dependence of electron photodetachment efficiency is correlated with the base ionization potential and is maximum at wavelengths corresponding to the base absorption, we initially proposed that electron photodetachment might occur directly from the base, and that the photodetachment yield was correlated with the electron binding energy to the base [2]. Photoelectron spectroscopy experiments were performed on DNA multiply charged anions with varying base composition to probe how the electron binding energies changes with the base composition. Finally, the electron detachment channel was used to perform UV spectroscopy experiments on large DNA polyanions trapped in the gas phase. Gas-phase UV spectra of DNA duplexes and G-quadruplexes containing up to 24 bases (> 7000 Da) will be presented. [1] V. Gabelica, T. Tabarin, R. Antoine, F. Rosu, I. Compagnon, M. Broyer, E. De Pauw, and P. Dugourd, Anal. Chem. 78, 6564 (2006). [2] V. Gabelica, F. Rosu, T. Tabarin, C. Kinet, R. Antoine, M. Broyer, E. De Pauw, and P. Dugourd, J. Am. Chem. Soc. 129, 4706 (2007). [3] V. Gabelica, F. Rosu, E. De Pauw, R. Antoine, T. Tabarin, M. Broyer, and P. Dugourd, J. Am. Soc. Mass Spectrom. 18, 1990 (2007). [less ▲]

Detailed reference viewed: 53 (2 ULg)
Full Text
Peer Reviewed
See detailAn Electron Spin Resonance (Esr) Study on the Mechanism of Ascorbyl Radical Production by Metal-Binding Proteins
Mouithys-Mickalad, Ange ULg; Deby, Carol; Dupont, Ginette ULg et al

in Biometals (1998), 11(2), 81-8

The mechanism of ascorbate oxidation by metal-binding proteins (ceruloplasmin, albumin and transferrin) was investigated in vitro and in isolated plasma by the measurement of the ascorbyl free radicals ... [more ▼]

The mechanism of ascorbate oxidation by metal-binding proteins (ceruloplasmin, albumin and transferrin) was investigated in vitro and in isolated plasma by the measurement of the ascorbyl free radicals (AFR) by electron spin resonance (ESR). In plasma of 13 healthy volunteers, a spontaneous and variable production of AFR was detected, which was increased by a 10(-4) M ascorbate overloading; however, this increase was not correlated to the intensity of the spontaneous AFR signal. The addition of Cu2+ and ceruloplasmin to plasma increased the ESR signal, while the addition of transferrin decreased the signal intensity in a dose-dependent manner. In vitro, we demonstrated that ascorbate was oxidized by human serum albumin and by ceruloplasmin, and that this oxidase-like activity was lost by trypsin or heat treatment of these proteins. These two proteins positively interacted in the oxidation of ascorbate, since addition of crude albumin to a solution of ascorbate and ceruloplasmin increased the intensity of ESR signal in a dose-dependent manner. The treatment of albumin by a metal chelator (DDTC) abolished these positive interactions. The respective roles of copper and iron in ascorbate oxidation were studied and showed a dose-dependent effect of these ions on ascorbate oxidation. The role of iron was confirmed by the inhibiting effect of metal-free transferrin on iron-dependent ascorbate oxidation. Concerted actions between iron carrying albumin and copper carrying ceruloplasmin appear responsible for the production of AFR in vitro and in vivo. [less ▲]

Detailed reference viewed: 27 (3 ULg)
Peer Reviewed
See detailElectron Spin Resonance Evidence of the Generation of Superoxide Anion, Hydroxyl Radical and Singlet Oxygen During the Photohemolysis of Human Erythrocytes with Bacteriochlorin A
Hoebeke, Maryse ULg; Schuitmaker, H. J.; Jannink, L. E. et al

in Photochemistry & Photobiology (1997), 66(4), 502-8

Photodynamic therapy with bacteriochlorin a (BCA) as sensitizer induces damage to red blood cells in vivo. To assess the extent of the contributuion of reactive oxygen species (ROS) and to determine a ... [more ▼]

Photodynamic therapy with bacteriochlorin a (BCA) as sensitizer induces damage to red blood cells in vivo. To assess the extent of the contributuion of reactive oxygen species (ROS) and to determine a possible reaction mechanism, competition experiments with assorted ROS quenching or/and enhancing agents were performed in human erythrocytes as model system and in phosphate buffer. In the erythrocyte experiments, a 2% suspension was incubated with BCA for 1 h, washed with phosphate-buffered saline, resuspended and subsequently illuminated with a diode laser using a fluence rate of 2.65 mW/cm2. Potassium leakage and hemolysis were light and BCA dose dependent. Adding tryptophan (3.3 mM), azide (1 mM) or histidine (10 mM) to the erythrocyte suspension before illumination delayed the onset of K-leakage and hemolysis suggesting a type II mechanism. The D2O did not affect K-leakage nor photohemolysis. Adding mannitol (13.3 mM) or glycerol (300 nM) also caused a delay in the onset of K-leakage and hemolysis, suggesting the involvement of radicals. In phosphate buffer experiments, it was shown using electron spin resonance (ESR) associated with spin-trapping techniques that BCA is able to generate O2-. and OH. radicals without production of aqueous electron. Visible or UV irradiation of the dye in the presence of the spin trap 5,5-dimethyl-1-pyrroline-N-oxide (DMPO) gave an ESR spectrum characteristic of the DMPO-hydroxyl radical spin adduct DMPO-OH. Addition of ethanol or sodium formate produced supplementary hyperfine splittings due to the respective CH3CHOH. and CO2-. radical adducts, indicating the presence of free OH.. Production of DMPO-OH was partly inhibited by superoxide dismutase (SOD), catalase and desferrioxamine, suggesting that the iron-catalyzed decomposition of H2O2 was partly involved in the formation of one part of the observed OH.. The complementary inhibition of DMPO-OH production by azide and 9,10-anthracenedipropionic acid (ADPA) was consistent with 1O2 production by BCA followed by reaction of 1O2 with DMPO and decay of the intermediate complex to form DMPO-OH and free OH.. All our results seem to indicate that BCA is a 50%/50% type 1/type 2 sensitizer in buffered aqueous solutions and confirmed that the dye-induced hemolysis of erythrocytes was cell caused by a mixed type 1/type 2 mechanism. [less ▲]

Detailed reference viewed: 25 (3 ULg)
See detailElectron spin resonance study of basteriochlorin a incorporation into membranes models
Hoebeke, Maryse ULg; Damoiseau, X.; Schuitmaker, H. et al

Conference (1999)

Detailed reference viewed: 5 (1 ULg)
See detailElectron spin resonance study of basteriochlorin a incorporation into membranes models
Hoebeke, Maryse ULg; Damoiseau, X.; Schuitmaker, H. et al

Conference (1999)

Detailed reference viewed: 4 (1 ULg)
Peer Reviewed
See detailElectron tomography of metaphase nucleolar organizer regions: evidence for a twisted-loop organization.
Heliot, L.; Kaplan, H.; Lucas, L. et al

in Molecular Biology of the Cell (1997), 8(11), 2199-216

Metaphase nucleolar organizer regions (NORs), one of four types of chromosome bands, are located on human acrocentric chromosomes. They contain r-chromatin, i.e., ribosomal genes complexed with proteins ... [more ▼]

Metaphase nucleolar organizer regions (NORs), one of four types of chromosome bands, are located on human acrocentric chromosomes. They contain r-chromatin, i.e., ribosomal genes complexed with proteins such as upstream binding factor and RNA polymerase I, which are argyrophilic NOR proteins. Immunocytochemical and cytochemical labelings of these proteins were used to reveal r-chromatin in situ and to investigate its spatial organization within NORs by confocal microscopy and by electron tomography. For each labeling, confocal microscopy revealed small and large double-spotted NORs and crescent-shaped NORs. Their internal three-dimensional (3D) organization was studied by using electron tomography on specifically silver-stained NORs. The 3D reconstructions allow us to conclude that the argyrophilic NOR proteins are grouped as a fiber of 60-80 nm in diameter that constitutes either one part of a turn or two or three turns of a helix within small and large double-spotted NORs, respectively. Within crescent-shaped NORs, virtual slices reveal that the fiber constitutes several longitudinally twisted loops, grouped as two helical 250- to 300-nm coils, each centered on a nonargyrophilic axis of condensed chromatin. We propose a model of the 3D organization of r-chromatin within elongated NORs, in which loops are twisted and bent to constitute one basic chromatid coil. [less ▲]

Detailed reference viewed: 14 (0 ULg)