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412 results on '"Massart C"'

1. The Black Hole - Bulge Relationship for QSOs at High Redshift

Author

Shields, G. A., Menezes, K. L., Massart, C. A., and Bout, P. Vanden

Subjects
Astrophysics
Abstract

We examine the black hole mass - galaxy bulge relationship in high-redshift QSOs. Black hole masses are derived from the broad emission lines, and the host galaxy stellar velocity dispersion sigma is estimated from the widths of the radio CO emission lines. At redshifts z > 3, the CO line widths are narrower than expected for the black hole mass, indicating that these giant black holes reside in undersized bulges by an order of magnitude or more. The largest black holes (above 10^9 solar masses) evidently grow rapidly in the early universe without commensurate growth of their host galaxies. CO line widths offer a unique opportunity to study AGN host galaxy dynamics at high redshift., Comment: 16 pages, 4 EPS figures, accepted for publication in The Astrophysical Journal

Published
2005
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18. Corrigendum to “Ten-year improvement of insulin resistance and growth with recombinant human insulin-like growth factor 1 in a patient with insulin receptor mutations resulting in leprechaunism” [Diabetes Metab. 41 (2015) 331–337]

Author

de Kerdanet, M., primary, Caron-Debarle, M., additional, Nivot, S., additional, Gaillot, T., additional, Lascols, O., additional, Fremont, B., additional, Bonnaure-Mallet, M., additional, Gie, S., additional, Massart, C., additional, and Capeau, J., additional

Published
2016
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25. 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

32. Tomographies Optiques et NeuroImageries Rhône-alpines chez le petit animal

Author

Mottin, S., Vial, J.C., Montcel, B., Douady, J., Olivier, T., Sanden, B., Moine, B., Lefkir, Y., Appaix, F., Abi-Haidar, D., Massart, C., Palle, S., Cottet, D., Wege, H., Mathevon, N., Maurin, M., Vignal, C., Cespuglio, R., Laboratoire Hubert Curien (LHC), Institut d'Optique Graduate School (IOGS)-Université Jean Monnet - Saint-Étienne (UJM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Spectrométrie Physique (LSP), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherche en Acquisition et Traitement de l'Image pour la Santé (CREATIS), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Jean Monnet - Saint-Étienne (UJM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Grenoble Institut des Neurosciences (GIN), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM), Unité Laboratoire CIC, Centre d'Investigation Clinique [Rennes] (CIC), Université de Rennes (UR)-Hôpital Pontchaillou-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rennes (UR)-Hôpital Pontchaillou-Institut National de la Santé et de la Recherche Médicale (INSERM)-University of Brussels, Université libre de Bruxelles (ULB)-Université libre de Bruxelles (ULB), Ecologie comportementale (EC), École normale supérieure - Paris (ENS-PSL), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université Paris-Sud - Paris 11 (UP11)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Université de Rennes (UR)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université de Bourgogne (UB)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Adaptation et pathogénie des micro-organismes [Grenoble] (LAPM), Neurobiologie des états de veille et de sommeil (EA3734), Université de Lyon-Université de Lyon-Centre Hospitalier le Vinatier [Bron], Montcel, Bruno, Laboratoire Hubert Curien [Saint Etienne] (LHC), Université Jean Monnet [Saint-Étienne] (UJM)-Centre National de la Recherche Scientifique (CNRS)-Institut d'Optique Graduate School (IOGS), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Hospices Civils de Lyon (HCL)-Université Jean Monnet [Saint-Étienne] (UJM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Grenoble-Université Joseph Fourier - Grenoble 1 (UJF), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Hôpital Pontchaillou-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Hôpital Pontchaillou-Institut National de la Santé et de la Recherche Médicale (INSERM)-University of Brussels, University of Brussels-University of Brussels, École normale supérieure - Paris (ENS Paris)-Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université Paris-Sud - Paris 11 (UP11)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Université Claude Bernard Lyon 1 (UCBL), Centre Hospitalier le Vinatier [Bron]-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, Institut d'Optique Graduate School (IOGS)-Université Jean Monnet [Saint-Étienne] (UJM)-Centre National de la Recherche Scientifique (CNRS), Université Jean Monnet [Saint-Étienne] (UJM)-Hospices Civils de Lyon (HCL)-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université Paris-Sud - Paris 11 (UP11)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Université de Rennes 1 (UR1), and Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF)

Subjects
[SDV.IB.IMA] Life Sciences [q-bio]/Bioengineering/Imaging, [SDV.IB.IMA]Life Sciences [q-bio]/Bioengineering/Imaging, imagerieₘethodologie_RMN, [INFO.INFO-IM] Computer Science [cs]/Medical Imaging, categₛt2i, [INFO.INFO-IM]Computer Science [cs]/Medical Imaging, ComputingMilieux_MISCELLANEOUS, Imagerie cérébrale
Abstract

International audience

Published
2009

34. HLA Gene Polymorphism: Class II

Author

Cohen, D., primary, Font, M. P., additional, Legall, I., additional, Marcadet, A., additional, Massart, C., additional, Lalouel, J. M., additional, and Dausset, J., additional

Published
1984
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40. Impact des valeurs de référence de dosage de la PTH de deuxième génération selon la trousse utilisée dans le suivi longitudinal des patients (pts) incidents pris en hémodialyse (HD) d’octobre 2010 à avril 2014 à l’ECHO – Pôle Santé Sud du Mans

Author

Laradi, A., primary, Babinet, F., additional, Cremault, A., additional, Lanoiselee, S., additional, Cavalier, E., additional, Souberbielle, J.-C., additional, Massart, C., additional, Bondu, F., additional, and Martin, L., additional

Published
2014
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45. Proteasome-mediated degradation of integral inner nuclear membrane protein emerin in fibroblasts lacking A-type lamins.

Author

Muchir, A., Massart, C., Engelen, B.G.M. van, Lammens, M.M.Y., Bonne, G., Worman, H.J., Muchir, A., Massart, C., Engelen, B.G.M. van, Lammens, M.M.Y., Bonne, G., and Worman, H.J.

Abstract

Contains fulltext : 49840.pdf (publisher's version ) (Closed access), We previously identified and characterized a homozygous LMNA nonsense mutation leading to the absence of A-type lamins in a premature neonate who died at birth. We show here that the absence of A-type lamins is due to degradation of the aberrant mRNA transcript with a premature termination codon. In cultured fibroblasts from the subject with the homozygous LMNA nonsense mutation, there was a decreased steady-state expression of the integral inner nuclear membrane proteins emerin and nesprin-1alpha associated with their mislocalization to the bulk endoplasmic reticulum and a hyperphosphorylation of emerin. To determine if decreased emerin expression occurred post-translationally, we treated cells with a selective proteasome inhibitor and observed an increase in expression. Our results show that mislocalization of integral inner nuclear membrane proteins to the endoplasmic reticulum in human cells lacking A-type lamins leads to their degradation and provides the first evidence that their degradation is mediated by the proteasome.

Published
2006

46. [Expression of the MDR1 gene in five human cell lines of medullary thyroid cancer and reversion of the resistance to doxorubicine by ciclosporin A and verapamil]

Author

Massart, C., Gibassier, J, Lucas, C., Pourquier, P., Robert, J., University of Brussels, IDvet [Grabels], Laboratoire Aimé Cotton (LAC), École normale supérieure - Cachan (ENS Cachan)-Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), Pourquier, Philippe, and Université libre de Bruxelles (ULB)

Subjects
[SDV]Life Sciences [q-bio], Antineoplastic Agents, Drug Synergism, Drug Resistance, Multiple, [SDV] Life Sciences [q-bio], Verapamil, Doxorubicin, Drug Resistance, Neoplasm, Carcinoma, Medullary, polycyclic compounds, Cyclosporine, Tumor Cells, Cultured, Humans, Thyroid Neoplasms
Abstract

International audience; Medullary thyroid carcinoma (MTC) is frequently resistant to chemotherapy. Multidrug resistance (MDR) is one of the involved mechanisms. In this work we have studied the MDR1 gene expression in five MTC human cell lines that we have isolated and we have compared this expression to that of normal thyroid tissue. We have also tried to reverse the resistance to doxorubicin with verapamil (VRP) and ciclosporin A (CSA). MDR1 ARNm expression was studied and quantified by polymerase chain reaction (PCR) in normal and pathological thyroid tissues. The doxorubicin-induced cytotoxicity was evaluated with the 3,-4,5 dimethylthiazol-2,5 diphenyl tetrazolium bromide (MTT) test, the neutral red (NR) uptake and with total glutathione (GSH) or intracellular lactate dehydrogenase (LDH) measurements. We found an increase of MDR1 ARNm in MTC as compared with normal tissues. Doxorubicin was cytotoxic after a 48-h coincubation with the cells. Three microM CSA and 10 microM VRP reversed the doxorubicin resistance only after a 48-h coincubation, generally followed with a 24 h-post-incubation. In these conditions, the GSH levels were decreased only by VRP in all the five cell lines. In conclusion, a chemoresistance related to the MDR1 gene overexpression was found in the five human MTC lines tested. VRP and CSA reversed the resistance to doxorubicin in all the MTC cell lines tested.

Published
1996

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