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8. Enhancement of endothelial cAMP accumulation by adenine nucleotides: role of methylxanthine-sensitive sites

Author

Cote, S., Van Sande, J., and Boeynaems, J.-M.

Subjects
Adenylic acid -- Physiological aspects, Cyclic adenylic acid -- Research, Vascular endothelium -- Research, Biological sciences
Abstract

Changes in the adenosine 3',5'-cyclic monophosphate (cAMP) system in aortic endothelial cells due to adenine nucleotides were investigated. Experiments involved the measurement of cAMP and inositol phosphate accumulation of bovine aortic endothelial cells. Results were subjected to statistical analysis. The stimulatory effect of adenosine triphosphate on the cAMP system in endothelial cells was demonstrated.

Published
1993

11. 11 The cAMP in thyroid

Author

Uyttersprot, N., primary, Allgeier, A., additional, Baptist, M., additional, Christophe, D., additional, Coppee, F., additional, Coulonval, K., additional, Deleu, S., additional, Depoortere, F., additional, Dremier, S., additional, Lamy, F., additional, Ledent, C., additional, Maenhaut, C., additional, Miot, F., additional, Panneels, V., additional, Parma, J., additional, Parmentier, M., additional, Pirson, I., additional, Pohl, V., additional, Roger, P., additional, Savonet, V., additional, Taton, M., additional, Tonacchera, M., additional, van Sande, J., additional, Wilkin, F., additional, Vassart, G., additional, and Dumont, J.E., additional

Published
1997
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12. TSH receptor and disease

Author

Tonacchera, M., Van Sande, J., Parma, J., Duprez, L., Cetani, F., Costagliola, S., Dumont, J. E., and Vassart, G.

Published
1996

17. AMPK antagonizes hepatic glucagon-stimulated cyclic AMP signalling via phosphorylation-induced activation of cyclic nucleotide phosphodiesterase 4B

Author

UCL - SSS/DDUV - Institut de Duve, Johanns, Manuel, Lai, Y.-C., Hsu, M.-F., Jacobs, R., Vertommen, D., Van Sande, J., Dumont, J. E., Woods, A., Carling, D., Hue, L., Viollet, B., Foretz, M., Rider, Mark, UCL - SSS/DDUV - Institut de Duve, Johanns, Manuel, Lai, Y.-C., Hsu, M.-F., Jacobs, R., Vertommen, D., Van Sande, J., Dumont, J. E., Woods, A., Carling, D., Hue, L., Viollet, B., Foretz, M., and Rider, Mark

Abstract

Biguanides such as metformin have previously been shown to antagonize hepatic glucagon-stimulated cyclic AMP (cAMP) signalling independently of AMP-activated protein kinase (AMPK) via direct inhibition of adenylate cyclase by AMP. Here we show that incubation of hepatocytes with the small-molecule AMPK activator 991 decreases glucagon-stimulated cAMP accumulation, cAMP-dependent protein kinase (PKA) activity and downstream PKA target phosphorylation. Moreover, incubation of hepatocytes with 991 increases the Vmax of cyclic nucleotide phosphodiesterase 4B (PDE4B) without affecting intracellular adenine nucleotide concentrations. The effects of 991 to decrease glucagon-stimulated cAMP concentrations and activate PDE4B are lost in hepatocytes deleted for both catalytic subunits of AMPK. PDE4B is phosphorylated by AMPK at three sites, and by site-directed mutagenesis, Ser304 phosphorylation is important for activation. In conclusion, we provide a new mechanism by which AMPK antagonizes hepatic glucagon signalling via phosphorylation-induced PDE4B activation.

Published
2016

18. Stimulation by iodide of [H.sub.2][O.sub.2] generation in thyroid slices from several species

Author

CORVILAIN, B., COLLYN, L., VAN SANDE, J., and DUMONT, J. E.

Subjects
Thyroid hormones -- Research, Iodides -- Research, Thyroid gland -- Research, Biological sciences
Abstract

Corvilain, B., L. Collyn, J. Van Sande, and J. E. Dumont. Stimulation by iodide of [H.sub.2][O.sub.2] generation in thyroid slices from several species. Am J Physiol Endocrinol Metab 278: E692-E699, 2000.--The regulation of thyroid metabolism by iodide involves numerous inhibitory effects. However. in unstimulated dog thyroid slices, a small inconstant stimulatory effect of iodide on [H.sub.2][O.sub.2] generation is observed. The only other stimulatory effect reported with iodide is on [1-[sup.14]C]glucose oxidation, i.e., on the pentose phosphate pathway. Because we have recently demonstrated that the pentose phosphate pathway is controlled by [H.sub.2][O.sub.2] generation, we study here the effect of iodide on basal [H.sub.2][O.sub.2] generation in thyroid slices from several species. Our data show that in sheep, pig, bovine, and to a lesser extent dog thyroid, iodide had a stimulatory effect on [H.sub.2][O.sub.2] generation. In horse and human thyroid, an inconstant effect was observed. We demonstrate in dogs that the stimulatory effect of iodide is greater in thyroids deprived of iodide, raising the possibility that differences in thyroid iodide pool may account, at least in part, for the differences between the different species studied. This represents the first demonstration of an activation by iodide of a specialized thyroid function. In comparison with conditions in which an inhibitory effect of iodide on [H.sub.2][O.sub.2] generation is observed, the stimulating effect was observed for lower concentrations and for a shorter incubation time with iodide. Such a dual control of [H.sub.2][O.sub.2] generation by iodide has the physiological interest of promoting an efficient oxidation of iodide when the substrate is provided to a deficient gland and of avoiding excessive oxidation of iodide and thus synthesis of thyroid hormones when it is in excess. The activation of [H.sub.2][O.sub.2] generation may also explain the well described toxic effect of acute administration of iodide on iodine-depleted thyroids. Wolff-Chaikoff effect; thyroid hormone synthesis; iodide toxicity; pentose phosphate pathway

Published
2000

19. AMPK antagonizes hepatic glucagon-stimulated cyclic AMP signalling via phosphorylation-induced activation of cyclic nucleotide phosphodiesterase 4B

Author

Johanns, M., primary, Lai, Y.-C., additional, Hsu, M.-F., additional, Jacobs, R., additional, Vertommen, D., additional, Van Sande, J., additional, Dumont, J. E., additional, Woods, A., additional, Carling, D., additional, Hue, L., additional, Viollet, B., additional, Foretz, M, additional, and Rider, M H, additional

Published
2016
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20. Cell biology of HO generation in the thyroid: Investigation of the control of dual oxidases (DUOX) activity in intact ex vivo thyroid tissue and cell lines

Author

Massart, C., Hoste, C., Virion, A., Ruf, J., Dumont, J.E., Van Sande, J., University of Brussels, Génomes et cancer (GC (FRE2939)), and Université Paris-Sud - Paris 11 (UP11)-Institut Gustave Roussy (IGR)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Regulatory pathways, Physiological and pharmacological probes, In vitro quasi physiological model, Thyroid hormone synthesis, Iodide oxidation
Abstract

International audience; HO generation by dual oxidase (DUOX) at the apex of thyroid cells is the limiting factor in the oxidation of iodide and the synthesis of thyroid hormones. Its characteristics have been investigated using different in vitro models, from the most physiological thyroid slices to the particulate fraction isolated from transfected DUOX expressing CHO cells. Comparison of the models shows that some positive controls are thyroid specific (TSH) or require the substructure of the in vivo cells (MβCD). Other controls apply to all intact cell models such as the stimulation of the PIP phospholipase C pathway by ATP acting on purinergic receptors, the activation of the Gq protein downstream (NaF), or surrogates of the intracellular signals generated by this cascade (phorbol esters for protein kinase C, Ca ionophore for Ca). Still, other controls, exerted by intracellular Ca or its substitute Mn, the intracellular pH, or arachidonate bear directly on the enzyme. Iodide acts at the apical membrane of the cell through an oxidized form, presumably iodohexadecanal. Cooling of the cells to 22°C blocks the activation of the PIP phospholipase C cascade. All these effects are reversible. Their kinetics and concentration-effect characteristics have been defined in the four models. A general scheme of the thyroid signalling pathways regulating this metabolism is proposed. The probes characterized could be applied to other HO producing cells and to pathological material.

Published
2011

26. Roles of hydrogen peroxide in thyroid physiology and disease

Author

UCL - MD/MNOP - Département de morphologie normale et pathologique, Song, Y., Driessens, N., Costa, M., De Deken, X., Detours, V., Corvilain, B., Maenhaut, C., Miot, F., Van Sande, J., Many, Marie-Christine, Dumont, J. E., UCL - MD/MNOP - Département de morphologie normale et pathologique, Song, Y., Driessens, N., Costa, M., De Deken, X., Detours, V., Corvilain, B., Maenhaut, C., Miot, F., Van Sande, J., Many, Marie-Christine, and Dumont, J. E.

Abstract

Context: The long-lived thyroid cell generates, for the synthesis of thyroid hormones, important amounts of H2O2 that are toxic in other cell types. This review analyzes the protection mechanisms of the cell and the pathological consequences of disorders of this system. Evidence Acquisition: The literature on H2O2 generation and disposal, thyroid hormone synthesis, and their control in the human thyroid is analyzed. Evidence Synthesis: In humans, H2O2 production by dual-oxidases and consequently thyroid hormone synthesis by thyroperoxidase are controlled by the phospholipase C-Ca2+-diacylglycerol arm of TSH receptor action. H2O2 in various cell types, and presumably in thyroid cells, is a signal, a mitogen, a mutagen, a carcinogen, and a killer. The various protection mechanisms of the thyroid cell against H2O2 are analyzed. They include the separation of the generating enzymes ( dual-oxidases), their coupling to thyroperoxidase in a proposed complex, the thyroxisome, and H2O2 degradation systems. Conclusions: It is proposed that various pathologies can be explained, at least in part, by overproduction and lack of degradation of H2O2 ( tumorigenesis, myxedematous cretinism, and thyroiditis) and by failure of the H2O2 generation or its positive control system ( congenital hypothyroidism).

Published
2007

27. TSH receptor and disease

Author

Tonacchera, Massimo, VAN SANDE, J, Parma, J, Duprez, L, Cetani, F, Costagliola, S, Dumont, Je, and Vassart, G.

Published
1996

28. Activating mutations of the TSH receptor gene cause thyroid diseases

Author

Vassart G, Van Sande J, Parma J, Massimo Tonacchera, Duprez L, Swillens S, and Dumont J

Subjects
Structure-Activity Relationship, Gene Expression Regulation, Genes, Mutation, Humans, Receptors, Thyrotropin, Thyroid Neoplasms, Hyperthyroidism, Germ-Line Mutation
Abstract

Spontaneous mutations have been identified in the gene encoding the thyrotropin receptor, the effect of which is to activate the receptor in the absence of hormone. When they occur within thyrocytes (somatic mutations) activating mutations cause clonal expansion of the cells into a hyperfunctional thyroid adenoma (toxic nodule). Our results demonstrate that this pathophysiologic mechanism accounts for the majority of toxic adenomas (9 mutations found out of 11 adenomas). The remaining cases are probably secondary to mutations in the G protein Gs. When similar mutations are present in the germ line, they cause a form of non-autoimmune hyperthyroidism transmitted as an autosomal dominant trait. Mutations of the tsh receptor gene have been found in five different families, including that corresponding to the original description of the syndrome by J. Leclère (Nancy). Structure/function studies of the various mutant receptors will contribute to our understanding of the mecanisms involved in the activation of G protein-coupled receptors.

Published
1996

29. Sphingolipid-cholesterol domains (lipid rafts) in normal human and dog thyroid follicular cells are not involved in thyrotropin receptor signaling

Author

UCL - MD/MNOP - Département de morphologie normale et pathologique, Costa, MJ, Song, Y., Macours, P, Massart, C, Many, Marie-Christine, Costagliola, S, Dumont, JE, Van Sande, J., Vanvooren, V, UCL - MD/MNOP - Département de morphologie normale et pathologique, Costa, MJ, Song, Y., Macours, P, Massart, C, Many, Marie-Christine, Costagliola, S, Dumont, JE, Van Sande, J., and Vanvooren, V

Abstract

Partition of signaling molecules in sphingolipid-cholesterol-enriched membrane domains, among which are the caveolae, may contribute to signal transduction efficiency. In normal thyroid, nothing is known about a putative TSH/cAMP cascade compartmentation in caveolae or other sphingolipid-cholesterol-enriched membrane domains. In this study we show for the first time that caveolae are present in the apical membrane of dog and human thyrocytes: caveolin-1 mRNA presence is demonstrated by Northern blotting in primary cultures and that of the caveolin-1 protein by immunohistochemistry performed on human thyroid tissue. The TSH receptor located in the basal membrane can therefore not be located in caveolae. We demonstrate for the first time by biochemical methods the existence of sphingolipid-cholesterol-enriched domains in human and dog thyroid follicular cells that contain caveolin, flotillin-2, and the insulin receptor. We assessed a possible sphingolipid-cholesterol-enriched domains compartmentation of the TSH receptor and the alpha subunit of the heterotrimeric G(s) and G(q) proteins using two approaches: Western blotting on detergent-resistant membranes isolated from thyrocytes in primary cultures and the influence of 10 mM methyl-beta-cyclodextrin, a cholesterol chelator, on basal and stimulated cAMP accumulation in intact thyrocytes. The results from both types of experiments strongly suggest that the TSH/cAMP cascade in thyroid cells is not associated with sphingolipid-cholesterol-enriched membrane domains.

Published
2004

31. Molecular Genetics of the Thyrotropin Receptor

Author

Vassart, G., primary, Brabant, G., additional, Costagliola, S., additional, Danguy, D., additional, Gérard, C., additional, Libert, F., additional, Ludgate, M., additional, Maenhaut, C., additional, Parmentier, M., additional, Paschke, R., additional, Perret, J., additional, van Sande, J., additional, and Dumont, J. E., additional

Published
2009
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42. The Na

Author

Vroye, L., primary, Beauwens, R., additional, Van Sande, J., additional, Daloze, D., additional, Braekman, J. C., additional, and Golstein, P. E., additional

Published
1997
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48. The G Protein–coupled Receptor Family and One of Its Members, the TSH Receptora

Author

VASSART, G., primary, DESARNAUD, F., additional, DUPREZ, L., additional, EGGERICKX, D., additional, LABBÉ, O., additional, LIBERT, F., additional, MOLLEREAU, C., additional, PARMA, J., additional, PASCHKE, R., additional, TONACCHERA, M., additional, VANDERHAEGHEN, P., additional, VAN SANDE, J., additional, DUMONT, J., additional, and PARMENTIER, M., additional

Published
1995
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