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15 results on '"Gulino, Danielle"'

1. Modeling the Molecular Network Controlling Adhesion Between Human Endothelial Cells: Inference and Simulation Using Constraint Logic Programming

Author

Fanchon, Eric, Corblin, Fabien, Trilling, Laurent, Hermant, Bastien, Gulino, Danielle, Hutchison, David, Series editor, Kanade, Takeo, Series editor, Kittler, Josef, Series editor, Kleinberg, Jon M., Series editor, Mattern, Friedemann, Series editor, Mitchell, John C., Series editor, Naor, Moni, Series editor, Nierstrasz, Oscar, Series editor, Pandu Rangan, C., Series editor, Steffen, Bernhard, Series editor, Sudan, Madhu, Series editor, Terzopoulos, Demetri, Series editor, Tygar, Dough, Series editor, Vardi, Moshe Y., Series editor, Weikum, Gerhard, Series editor, Istrail, Sorin, editor, Pevzner, Pavel, editor, Waterman, Michael, editor, Danos, Vincent, editor, and Schachter, Vincent, editor

Published
2005
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3. ANTI-VE-CADHERIN AUTOANTIBODIESAS A BOMARKER O FVASCULAR ALTERATIONS ASSOCATED WITH DISORDERS

Author

Vilgrain, Isabelle, GULINO, Danielle, Bouillet, Laurence, Biologie du Cancer et de l'Infection (BCI ), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), VILGRAIN, ISABELLE, Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut National de la Santé et de la Recherche Médicale (INSERM)

Subjects
[SDV] Life Sciences [q-bio], [SDV.MHEP] Life Sciences [q-bio]/Human health and pathology, [SDV.IMM] Life Sciences [q-bio]/Immunology, Auto-antibodies, [SDV]Life Sciences [q-bio], Vascular Disorders, [SDV.IMM]Life Sciences [q-bio]/Immunology, antiVE-cadherin antibodies, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
Abstract

The present invention relates to a method for predicting and/or diagnosing vascular alterations associated with a disorder in a patient, comprising a step of detecting or quantifying the presence of anti-VE-cadherin autoantibodies in a biological sample obtained from said patient.The present invention also relates to a kit suitable for carrying out the method of the invention, comprising a solid support coated with at least one VE-cadherin antigen and at least a labelled antibody specifically recognizing antibodies.The inventors have now identified that anti-VE-cadherin autoantibodies is a biomarker for predicting and/or diagnosing, in particular in serum, vascular alterations associated with diverse disorders or diseases. Indeed, they have detected and quantified anti-VE-cadherin autoantibodies in sera of patients affected with various diseases and disorders. They have also characterized these autoantibodies by demonstrating after their purification they may be pathogenic and contribute to vascular injury in several diseases.

Published
2014

6. Modeling the Molecular Network Controlling Adhesion Between Human Endothelial Cells: Inference and Simulation Using Constraint Logic Programming.

Author

Danos, Vincent, Schachter, Vincent, Fanchon, Eric, Corblin, Fabien, Trilling, Laurent, Hermant, Bastien, and Gulino, Danielle

Abstract

Cell-cell adhesion plays a critical role in the formation of tissues and organs. Adhesion between endothelial cells is also involved in the control of leukocyte migration across the endothelium of blood vessels. The most important players in this process are probably identified and the overall organization of the biochemical network can be drawn, but knowledge about connectivity is still incomplete, and the numerical values of kinetic parameters are unknown. This calls for qualitative modeling methods. Our aim in this paper is twofold: (i) to integrate in a unified model the biochemical network and the genetic circuitry. For this purpose we transform our system into a system of piecewise linear differential equations and then use Thomas theory of discrete networks. (ii) to show how constraints can be used to infer ranges of parameter values from observations and, with the same model, perform qualitative simulations. [ABSTRACT FROM AUTHOR]

Published
2005

12. Expression and purification of a soluble functional form of the platelet α11bβ3 integrin.

Author

Gulino, Danielle, Martinez, Pascal, Delachanal, Elisabeth, Concord, Evelyne, Duperray, Alain, Alemany, Mònica, and Marguerie, Gérard

Subjects
*PLATELET glycoprotein GPIIb-IIIa complex, *INTEGRINS, *MEMBRANE proteins, *CARRIER proteins, *PEPTIDES, *FIBRINOGEN
Abstract

Platelet glycoproteins αIIb and β3 are membrane proteins that associate to form a Ca2+-dependent heterodimer which constitutes an inducible member of the integrin family at the surface of the cell. To produce a soluble form of this complex, αIIb and β3 were both deleted of their transmembrane and cytoplasmic domains and were expressed in COS cells. Production of the truncated subunits and their mode of assembly were examined by immunoprecipitation experiments and compared to those of wildtype αIIbβ3. Synthesis and processing of the truncated heterodimer proceeded via a pathway similar to that observed for the wild-type αIIbβ3 in COS cells or in human megakaryocytes. The truncated β3 subunit associated with the Pro-truncated form of the αIIb subunit. This precursor form was not secreted. After proteolytic cleavage of the Pro-truncated αIIb, the mature heterodimer was secreted into the culture supernatant. To quantify the molar ratio of the various secreted soluble forms, an immunocapture assay was designed. All secreted tr-αb subunits associated with tt-β3. In contrast, tr-β3 was produced and secreted in excess as the free form. Immunoreactivity of the wild-type and soluble truncated complexes was identical since all the monoclonal antibodies used reacted with surface-located epitopes on both complexes. This indicated that the soluble truncated heterodimer adopted a native conformation. To purify this soluble heterodimer, tr-αIIbβ3 containing culture supernatant was adsorbed on an RGDW-affinity column and eluted with a solution of the free peptide RGDW. In the RGD-eluted material, the amount of each subunit was stoichiometric, suggesting that the complex was not disrupted during purification. The capacity of the wild-type and truncated RGD-eluted complexes to interact with soluble fibrinogen was compared using a solid-phase immunocapture assay, tr-αIIbβ3 and platelet αIIbβ3 exhibited similar fibrinogen-binding capacity. For both complexes, these interactions were mediated by RGD and γ fibrinogen signals. [ABSTRACT FROM AUTHOR]

Published
1995
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13. Sequence 274-368 in the β3-Subunit of the Integrin αIIbβ3 Provides a Ligand Recognition and Binding Domain for the γ-Chain of Fibrinogen That Is Independent of Platelet Activation

Author

Alemany, Monica, Concord, Evelyne, Garin, Jerome, Vincon, Mathilde, Giles, A., Marguerie, Gέrard, and Gulino, Danielle

Abstract

Several bacterial-expressed recombinant fragments encompassing the extracellular part of the β3 subunit of the integrin αIIbβ3 were shown to recognize and bind soluble and immobilized forms of fibrinogen. Two of them, designated as rIII-11 (03 274-368) and rlll-13 (β3 274-403), did not contain the established RGD-ligand binding sequence. In fact, they interacted, in a Ca2+-independent manner, with the C-terminal part of the fibrinogen gamma chain. Both β3 fragments blocked the participation of fibrinogen in the induction of platelet aggregation induced by adenosine diphosphate. Fragment rlll-13 was recognized by the anti-β3 monoclonal antibody B2A. This antibody, which possesses an epitope exposed on both resting and activated platelets, inhibited fibrinogen binding as well as platelet adhesion and aggregation. In conclusion, the results demonstrate that the 274-368 sequence of the β3 subunit of integrin αIIbβ3 constitutes a fibrinogen ligand binding domain, distinct from the RGD-binding site, that is required for both platelet adhesion and aggregation.

Published
1996
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