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See detailGlutathione-S-transferase pi expression in toxic epidermal necrolysis: a marker of putative oxidative stress in keratinocytes.
Paquet, Philippe ULg; Pierard, Gérald ULg

in Skin Pharmacology & Physiology (2007), 20(2), 66-70

BACKGROUND: Toxic epidermal necrolysis (TEN) is a dramatic drug-induced emergency related to extensive destruction of the epidermis. There is evidence that its pathomechanism involves impaired ... [more ▼]

BACKGROUND: Toxic epidermal necrolysis (TEN) is a dramatic drug-induced emergency related to extensive destruction of the epidermis. There is evidence that its pathomechanism involves impaired detoxication of xenobiotics. Glutathione-S-transferase pi (GST-pi) is a phase II detoxifying enzyme involved in drug metabolization by human keratinocytes. METHOD: Immunohistochemistry was performed in order to assess the expression of GST-pi in keratinocytes of TEN, other cutaneous adverse drug reactions and bullous pemphigoid. RESULTS: GST-pi was disclosed in the involved epidermis of 16/16 TEN patients. It was present in the cytoplasm of suprabasal keratinocytes. GST-pi was also expressed in the clinically uninvolved skin in a majority (8/12) of TEN patients. By contrast, it was rarely and poorly expressed in the other tested dermatoses. CONCLUSION: The pathomechanism of TEN is not related to an impaired quantitative expression of GST-pi. GST-pi expression is an early event in TEN. As oxidative stress is a major inducer of GST-pi, this mechanism might be involved in TEN. Its GST-pi expression mainly restricted to the suprabasal keratinocytes suggests that the pathomechanisms leading to keratinocyte death in TEN are distinct at different levels of the epidermis. [less ▲]

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See detailGluttony in Emblem books
Von Hoffmann, Viktoria ULg

in Sensory Studies, Picture Gallery (2012)

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See detailGlycemic Variability, Hypoglycemia and Organ Failure in the Glucontrol Study
Penning, Sophie ULg; Le Compte, Aaron J.; Preiser, Jean-Charles et al

in 10th Belgian Day on Biomedical Engineering (2011)

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See detailGlycemic Variability, Hypoglycemia and Organ Failure in the Glucontrol Study
Penning, Sophie ULg; Le Compte, Aaron J.; Preiser, Jean-Charles et al

Poster (2011, December)

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See detailGlycémie délocalisée: Entretien avec le Dr Etienne CAVALIER
Cavalier, Etienne ULg

in Biotribune Magazine (2006), 19(1), 33

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See detailGlycerol Production by fermentation of sucrose
Destain, Jacqueline ULg; Renauld, M.; Rikir, R. et al

Poster (1992, October)

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See detailGlycine receptor activation controls interneuron migration by affecting nuclear translocation and myosin phosphorylation
Avila Macaya, Ariel Salvatore ULg; Nguyen, Laurent ULg

Poster (2012)

Previous studies have described the presence of glycine receptor mRNA during early stages of embryonic cortex development. Here, we have tested the functionality of those receptors in migratory ... [more ▼]

Previous studies have described the presence of glycine receptor mRNA during early stages of embryonic cortex development. Here, we have tested the functionality of those receptors in migratory interneurons and demonstrated their involvement in the control of cell migration. We suggest a mechanism whereby activation of glycine receptors during tangential migration activates voltage gated calcium channels and favors influx of calcium that ultimately affect myosin II activity, a mechanism that fine tune nuclear translocation and thus migration speed. [less ▲]

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See detailGlycine receptor activation influences early cortical development
Avila Macaya, Ariel Salvatore ULg; Nguyen, Laurent ULg

Poster (2011, July 14)

The strychnine-sensitive glycine receptor (GlyR) is a member of the ligand-gated ion channel superfamily. In the adult, the GlyR is known to mediate fast inhibitory neurotransmission in the spinal cord ... [more ▼]

The strychnine-sensitive glycine receptor (GlyR) is a member of the ligand-gated ion channel superfamily. In the adult, the GlyR is known to mediate fast inhibitory neurotransmission in the spinal cord and in the brainstem. The GlyR has also been described in the embryonic cortex after embryonic day 19 (E19) (Flint et al., 1998) where it could participate in developmental processes, but its presence at earlier stages has not been documented. Since other neurotransmitter systems, i.e. GABA and its receptors, are known to be potent signals that control corticogenesis (Nguyen et al., 2001; Ik-Tsen et al., 2007), we wondered if glycine and its GlyR could also fulfill such a function. In this study, we analyze GlyR expression and its physiological function in the early development of the cortex using in vitro cultures of embryonic day 13 slices, patch-clamp and immunocytochemistry. [less ▲]

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See detailThe glycine receptor is functionally expressed in migratory interneurons and influences early cortical development
Avila Macaya, Ariel Salvatore ULg; Nguyen, Laurent ULg

Poster (2011)

The strychnine-sensitive glycine receptor (GlyR) is a member of the ligand-gated ion channel superfamily. In the adult, the GlyR is known to mediate fast inhibitory neurotransmission in the spinal cord ... [more ▼]

The strychnine-sensitive glycine receptor (GlyR) is a member of the ligand-gated ion channel superfamily. In the adult, the GlyR is known to mediate fast inhibitory neurotransmission in the spinal cord and in the brainstem. The GlyR has also been described in the embryonic cortex after embryonic day 19 (E19) (Flint et al., 1998) where it could participate in developmental processes, but its presence at earlier stages has not been documented. Since other neurotransmitter systems, i.e. GABA and its receptors, are known to be potent signals that control corticogenesis (Nguyen et al., 2001; Ik-Tsen et al., 2007), we wondered if glycine and its GlyR could also fulfill such a function. In this study, we analyze GlyR expression and its physiological function in the early development of the cortex using in vitro cultures of embryonic day 13 slices, patch-clamp, two photon microscopy and immunocytochemistry. [less ▲]

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See detailGlycine Receptor α2 Subunit Activation Promotes Cortical Interneuron Migration
Avila Macaya, Ariel Salvatore ULg; Vidal, Pia M; Dear, T Neil et al

in Cell Reports (2013)

Glycine receptors (GlyRs) are detected in the developing CNS before synaptogenesis, but their function remains elusive. This study demonstrates that functional GlyRs are expressed by embryonic cortical ... [more ▼]

Glycine receptors (GlyRs) are detected in the developing CNS before synaptogenesis, but their function remains elusive. This study demonstrates that functional GlyRs are expressed by embryonic cortical interneurons in vivo. Furthermore, genetic disruption of these receptors leads to interneuron migration defects. We discovered that extrasynaptic activation of GlyRs containing the α2 subunit in cortical interneurons by endogenous glycine activates voltage-gated calcium channels and promotes calcium influx, which further modulates actomyosin contractility to fine-tune nuclear translocation during migration. Taken together, our data highlight the molecular events triggered by GlyR α2 activation that control cortical tangential migration during embryogenesis. [less ▲]

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See detailGlycine Triggers an Intracellular Calcium Influx in Oligodendrocyte Progenitor Cells Which Is Mediated by the Activation of Both the Ionotropic Glycine Receptor and Na+-Dependent Transporters
Belachew, Shibeshih ULg; Malgrange, Brigitte ULg; Rigo, Jean-Michel et al

in European Journal of Neuroscience (2000), 12(6), 1924-30

Using fluo-3 calcium imaging, we demonstrate that glycine induces an increase in intracellular calcium concentration ([Ca2+]i) in cortical oligodendrocyte progenitor (OP) cells. This effect results from a ... [more ▼]

Using fluo-3 calcium imaging, we demonstrate that glycine induces an increase in intracellular calcium concentration ([Ca2+]i) in cortical oligodendrocyte progenitor (OP) cells. This effect results from a calcium entry through voltage-gated calcium channels (VGCC), as it is observed only in OP cells expressing such channels, and it is abolished either by removal of calcium from the extracellular medium or by application of an L-type VGCC blocker. Glycine-triggered Ca2+ influx in OP cells actually results from an initial depolarization that is the consequence of the activation of both the ionotropic glycine receptor (GlyR) and Na+-dependent transporters, most probably the glycine transporters 1 (GLYT1) and/or 2 (GLYT2) which are colocalized in these cells. Through this GlyR- and transporter-mediated effect on OP intrcellular calcium concentration [Ca2+]i, glycine released by neurons may, as well as other neurotransmitters, serve as a signal between neurons and OP during development. [less ▲]

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See detailGlycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1
Maurer, Ulrich; Charvet, Céline; Wagman, Allan et al

in Molecular Cell (2006), 21(6), 749-760

We investigated the role of glycogen synthase kinase-3 (GSK-3), which is inactivated by AKT, for its role in the regulation of apoptosis. Upon IL-3 withdrawal, protein levels of MCL-1 decreased but were ... [more ▼]

We investigated the role of glycogen synthase kinase-3 (GSK-3), which is inactivated by AKT, for its role in the regulation of apoptosis. Upon IL-3 withdrawal, protein levels of MCL-1 decreased but were sustained by pharmacological inhibition of GSK-3, which prevented cytochrome c release and apoptosis. MCL-1 was phosphorylated by GSK-3 at a conserved GSK-3 phosphorylation site (S159). S159 phosphorylation of MCL-1 was induced by IL-3 withdrawal or PI3K inhibition and prevented by AKT or inhibition of GSK-3, and it led to increased ubiquitinylation and degradation of MCLA. A phosphorylation-site mutant (MCL-1(S159A)), expressed in IL-3-dependent cells, showed enhanced stability upon IL-3 withdrawal and conferred increased protection from apoptosis compared to wild-type MCL-1. The results demonstrate that the control of MCLA stability by GSK-3 is an important mechanism for the regulation of apoptosis by growth factors, PI3K, and AKT. [less ▲]

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See detailGlycol chitosan improves the efficacy of intranasally administrated replication defective human adenovirus type 5 expressing glycoprotein D of bovine herpesvirus 1
Gogev, S.; de Fays, K.; Versali, Marie-France ULg et al

in Vaccine (2004), 22(15-16), 1946-1953

The ability of two soluble formulations, namely chitosan and glycol chitosan, when used as an intranasal adjuvant, to improve the immunogenicity of an intranasal human adenovirus type 5 replication ... [more ▼]

The ability of two soluble formulations, namely chitosan and glycol chitosan, when used as an intranasal adjuvant, to improve the immunogenicity of an intranasal human adenovirus type 5 replication defective expressing bovine herpesvirus 1 (BoHV-1) glycoprotein D based vaccine, was investigated in cattle. Their adjuvant effects on immune response by increasing clinical and especially virological protection against an intranasal BoHV-1 challenge were then evaluated. The best virological protection was obtained in calves immunized with the vaccine vector adjuvanted with glycol chitosan which decreased the challenge BoHV-1 virus excretion titres by 0.5-1.5 log when compared to those obtained in calves immunized with the vaccine vector alone or adjuvanted with chitosan. A slight difference in clinical scores was observed in calves immunized with the adjuvanted vaccine vector compared to calves immunized with the vaccine vector alone. The obtained data suggest that the tested soluble formulation of glycol chitosan has promising potential use as an intranasal adjuvant for recombinant viral vector vaccines in cattle. (C) 2003 Elsevier Ltd. All rights reserved. [less ▲]

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See detailGlycoprotein B cleavage is important for murid herpesvirus 4 to infect myeloid cells.
Glauser, Daniel L.; Milho, Ricardo; Frederico, Bruno et al

in Journal of Virology (2013)

Glycoprotein B (gB) is a conserved herpesvirus virion component implicated in membrane fusion. As with many - but not all - herpesviruses, the gB of murid herpesvirus 4 (MuHV-4) is cleaved into disulfide ... [more ▼]

Glycoprotein B (gB) is a conserved herpesvirus virion component implicated in membrane fusion. As with many - but not all - herpesviruses, the gB of murid herpesvirus 4 (MuHV-4) is cleaved into disulfide-linked subunits, apparently by furin. Preventing gB cleavage for some herpesviruses causes minor infection deficits in vitro, but what the cleavage contributes to host colonization has been unclear. To address this we mutated the furin cleavage site (R-R-K-R) of the MuHV-4 gB. Abolishing gB cleavage did not affect its expression levels, glycosylation or antigenic conformation. In vitro, mutant viruses entered fibroblasts and epithelial cells normally, but had a significant entry deficit in myeloid cells such as macrophages and bone marrow-derived dendritic cells. The deficit in myeloid cells was not due to reduced virion binding or endocytosis, suggesting that gB cleavage promotes infection at a post-endocytic entry step, presumably viral membrane fusion. In vivo, viruses lacking gB cleavage showed reduced lytic spread in the lungs. Alveolar epithelial cell infection was normal, but alveolar macrophage infection was significantly reduced. Normal long-term latency in lymphoid tissue was established nonetheless. [less ▲]

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See detailGlycoprotein B of Bovine Herpesvirus 4 Is a Major Component of the Virion, Unlike That of Two Other Gammaherpesviruses, Epstein-Barr Virus and Murine Gammaherpesvirus 68
Lomonte, P.; Filée, Patrice ULg; Lyaku, J. R. et al

in Journal of Virology (1997), 71(4), 3332-5

This study reports that in bovine herpesvirus 4, glycoprotein B (gB) is a heterodimer and a major component of the virion, unlike gBs of Epstein-Barr virus (gp110) and murine gammaherpesvirus 68, two ... [more ▼]

This study reports that in bovine herpesvirus 4, glycoprotein B (gB) is a heterodimer and a major component of the virion, unlike gBs of Epstein-Barr virus (gp110) and murine gammaherpesvirus 68, two other gammaherpesviruses. These are new characteristics with regard to the general features of gB in the Gammaherpesvirinae subfamily. [less ▲]

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