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4 results on '"MESH : Phosphoric Monoester Hydrolases"'

1. Peritoneal Cell-Derived Mast Cells: An In Vitro Model of Mature Serosal-Type Mouse Mast Cells

Author

Michel Arock, Antoine Ribadeau Dumas, Marc Daëron, Karine Roget, Bruno Iannascoli, Cécile Schiffer, Odile Malbec, Allergologie Moléculaire et Cellulaire, Institut Pasteur [Paris] - Institut National de la Santé et de la Recherche Médicale (INSERM), Cytokines, hématopoïèse et réponse immune (CHRI), Université Paris Descartes - Paris 5 (UPD5) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Centre National de la Recherche Scientifique (CNRS), Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and Institut Pasteur [Paris] (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM)

Subjects
Chemokine, MESH : Phosphoric Monoester Hydrolases, Cellular differentiation, Cell, Cell Count, MESH : Cell Count, MESH : Models, Immunological, Immunoglobulin E, MESH: Mice, Knockout, MESH: Down-Regulation, MESH : Down-Regulation, Mice, Serous Membrane, 0302 clinical medicine, Immunology and Allergy, MESH: Animals, Mast Cells, Cells, Cultured, Mice, Knockout, MESH: Immunoglobulin G, 0303 health sciences, education.field_of_study, biology, Inositol Polyphosphate 5-Phosphatases, MESH: Immunoglobulin E, Degranulation, MESH: Peritoneum, Cell Differentiation, MESH: Mast Cells, Mast cell, Cell biology, medicine.anatomical_structure, Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases, MESH : Serous Membrane, MESH: Phosphoric Monoester Hydrolases, [SDV.IMM]Life Sciences [q-bio]/Immunology, MESH : Mast Cells, Peritoneum, MESH : Cell Differentiation, MESH: Cells, Cultured, MESH: Cell Differentiation, MESH : Immunoglobulin G, [SDV.IMM] Life Sciences [q-bio]/Immunology, Immunology, Population, Down-Regulation, MESH: Serous Membrane, MESH : Mice, Inbred C57BL, MESH: Models, Immunological, MESH : Immunoglobulin E, 03 medical and health sciences, Immune system, MESH: Mice, Inbred C57BL, MESH : Cells, Cultured, MESH : Mice, medicine, Animals, education, MESH: Mice, MESH : Peritoneum, 030304 developmental biology, MESH: Cell Count, Models, Immunological, Phosphoric Monoester Hydrolases, Mice, Inbred C57BL, Immunoglobulin G, biology.protein, MESH : Mice, Knockout, MESH : Animals, 030215 immunology
Abstract

Bone marrow-derived mast cells (BMMC) have been used extensively as a mast cell model. BMMC, however, are immature cells that have no known physiological equivalent in tissues. They do not respond to IgG immune complexes. They may therefore not be appropriate for studying the physiopathology of IgE-induced allergies or IgG-induced tissue-specific inflammatory diseases which both depend on mature mast cells. Resident peritoneal mast cells are a minor population of differentiated cells that are not readily purified. They, however, can be expanded in culture to generate large numbers of homogeneous cells. We show here that these peritoneal cell-derived mast cells (PCMC) are mature serosal-type mouse mast cells which retain most morphological, phenotypic, and functional features of peritoneal mast cells. Like peritoneal mast cells, PCMC respond to IgG Abs. IgG immune complex-induced responses depended on FcγRIIIA and were negatively regulated by FcγRIIB. We found that a moderate FcγRIIB-dependent negative regulation, due not to a higher FcγRIIIA/FcγRIIB ratio, but to a relatively inefficient use of the lipid phosphatase SHIP1, determines this property of PCMC. PCMC also respond to IgE Abs. IgE-induced PCMC responses, however, differed quantitatively and qualitatively from BMMC responses. PCMC secreted no or much lower amounts of lipid mediators, chemokines, and cytokines, but they contained and released much higher amounts of preformed granular mediators. PCMC, but not BMMC, also contained and, upon degranulation, released molecules with a potent proteolytic activity. These properties make PCMC a useful new model for understanding the physiopathology of mast cells in IgE- and IgG-dependent tissue inflammation.

Published
2007

2. Bleeding disorders in Lowe syndrome patients: evidence for a link between OCRL mutations and primary haemostasis disorders

Author

Lasne, Dominique, Baujat, Geneviève, Mirault, Tristan, Lunardi, Joël, Grelac, Françoise, Egot, Marion, Salomon, Rémi, Bachelot-Loza, Christilla, Laboratory of molecular mechanisms of hematologic disorders and therapeutic implications (ERL 8254 - Equipe Inserm U1163), Imagine - Institut des maladies génétiques (IMAGINE - U1163), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Risque Thrombotique et Mecanismes de l'Hemostase (U765), Institut des sciences du Médicament -Toxicologie - Chimie - Environnement (IFR71), Institut de Recherche pour le Développement (IRD)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Service de Génétique Médicale [CHU Necker], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-CHU Necker - Enfants Malades [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Laboratoire de biochimie et génétique moléculaire, CHU Grenoble, Service de néphrologie pédiatrique [CHU Necker], Association du Syndrome de Lowe GIS-Maladies Rares INSERM, Roux-Buisson, Nathalie, Laboratoire d'hématologie ( ERL 8254 ), Imagine - Institut des maladies génétiques ( IMAGINE - U1163 ), Centre National de la Recherche Scientifique ( CNRS ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université Paris Descartes - Paris 5 ( UPD5 ) -Centre National de la Recherche Scientifique ( CNRS ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université Paris Descartes - Paris 5 ( UPD5 ), Risque Thrombotique et Mecanismes de l'Hemostase ( U765 ), Institut des sciences du Médicament -Toxicologie - Chimie - Environnement ( IFR71 ), Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Ecole Nationale Supérieure de Chimie de Paris- Chimie ParisTech-PSL ( ENSCP ) -Centre National de la Recherche Scientifique ( CNRS ) -Institut de Recherche pour le Développement ( IRD ) -Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Ecole Nationale Supérieure de Chimie de Paris- Chimie ParisTech-PSL ( ENSCP ) -Centre National de la Recherche Scientifique ( CNRS ) -Institut de Recherche pour le Développement ( IRD ) -Université Paris Descartes - Paris 5 ( UPD5 ) -Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), CHU Necker - Enfants Malades [AP-HP]-Assistance publique - Hôpitaux de Paris (AP-HP), Institut National de la Santé et de la Recherche Médicale (INSERM)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Paris Descartes - Paris 5 (UPD5)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Risque Thrombotique et Mécanismes de l'Hémostase (U765)

Subjects
Male, MESH : Retrospective Studies, MESH : Phosphoric Monoester Hydrolases, MESH : Hemostatic Disorders, MESH: GTPase-Activating Proteins, MESH : Child, Preschool, MESH : Child, MESH: Child, Child, Hemostatic Disorders, GTPase-Activating Proteins, MESH: Genetic Predisposition to Disease, MESH : Infant, MESH: Infant, Child, Preschool, platelets, RhoGAP, MESH: Phosphoric Monoester Hydrolases, [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], Blood Coagulation Tests, MESH : Mutation, MESH: Oculocerebrorenal Syndrome, MESH: Mutation, Adolescent, MESH : Male, MESH : Blood Coagulation Tests, haemostasis disorders, MESH: Hemostatic Disorders, MESH : Adolescent, Humans, MESH : Oculocerebrorenal Syndrome, Genetic Predisposition to Disease, [SDV.NEU] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], Retrospective Studies, MESH: Adolescent, OCRL, MESH: Humans, MESH : Humans, MESH: Blood Coagulation Tests, MESH: Child, Preschool, Infant, MESH : GTPase-Activating Proteins, MESH: Retrospective Studies, Phosphoric Monoester Hydrolases, MESH: Male, Lowe syndrome, Oculocerebrorenal Syndrome, [ SDV.NEU ] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], Mutation, MESH : Genetic Predisposition to Disease
Abstract

International audience; Lowe syndrome (LS) is a rare X-linked disorder caused by mutations in the oculocerebrorenal gene (OCRL), encoding OCRL, a phosphatidylinositol 5-phosphatase with a RhoGAP domain. An abnormal rate of haemorrhagic events was found in a retrospective clinical survey. Herein, we report the results of exploration of haemostasis in six LS patients. All patients had normal coagulation tests but prolonged closure times (CTs) in the PFA-100 system. Healthy donors' blood samples incubated with a RhoA kinase inhibitor had prolonged CTs. This suggests that an aberrant RhoA pathway in platelets contributes to CT prolongation and primary haemostasis disorders in LS.

Published
2010

3. The SH2 domain-containing inositol 5-phosphatase SHIP1 is recruited to the intracytoplasmic domain of human FcgammaRIIB and is mandatory for negative regulation of B cell activation

Author

Marc Daëron, Wolf H. Fridman, Georges Bismuth, Pierre Bruhns, Isabelle Isnardi, Allergologie Moléculaire et Cellulaire, Institut Pasteur [Paris] (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire d'Immunologie Cellulaire et Clinique, Université Pierre et Marie Curie - Paris 6 (UPMC)-IFR58-Institut National de la Santé et de la Recherche Médicale (INSERM), Immunopharmacologie Moléculaire, Institut Cochin (UMR_S567 / UMR 8104), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Detchepare, Christine, Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale ( INSERM ), Université Pierre et Marie Curie - Paris 6 ( UPMC ) -IFR58-Institut National de la Santé et de la Recherche Médicale ( INSERM ), Institut Cochin ( UMR_S567 / UMR 8104 ), and Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ) -Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ) -Centre National de la Recherche Scientifique ( CNRS )

Subjects
MESH: Signal Transduction, Cytoplasm, MESH : Phosphoric Monoester Hydrolases, MESH: Amino Acid Sequence, Lymphocyte Activation, SH2 domain, Mice, chemistry.chemical_compound, MESH: Protein Structure, Tertiary, 0302 clinical medicine, Immunology and Allergy, Inositol, MESH: Animals, Tyrosine, [SDV.IMM.ALL]Life Sciences [q-bio]/Immunology/Allergology, Cells, Cultured, MESH : Receptors, IgG, Sequence Deletion, B-Lymphocytes, 0303 health sciences, MESH : Amino Acid Sequence, breakpoint cluster region, MESH: Sequence Deletion, medicine.anatomical_structure, Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases, MESH: Phosphoric Monoester Hydrolases, GRB2, Signal transduction, MESH : Protein Structure, Tertiary, [SDV.IMM.ALL] Life Sciences [q-bio]/Immunology/Allergology, Signal Transduction, MESH: Cells, Cultured, MESH : Cytoplasm, MESH : Recombinant Fusion Proteins, Recombinant Fusion Proteins, Immunology, Phosphatase, Biology, MESH: Receptors, IgG, MESH : B-Lymphocytes, [ SDV.IMM.ALL ] Life Sciences [q-bio]/Immunology/Allergology, 03 medical and health sciences, MESH: B-Lymphocytes, MESH : Cells, Cultured, MESH : Mice, medicine, MESH: Recombinant Fusion Proteins, Animals, Humans, Amino Acid Sequence, MESH: Lymphocyte Activation, MESH: Mice, MESH : Lymphocyte Activation, B cell, 030304 developmental biology, MESH : Signal Transduction, MESH: Humans, MESH : Sequence Deletion, MESH: Cytoplasm, Receptors, IgG, MESH : Humans, Phosphoric Monoester Hydrolases, Protein Structure, Tertiary, chemistry, Cancer research, biology.protein, MESH : Animals, 030215 immunology
Abstract

Murine FcgammaRIIB were demonstrated to recruit SH2 domain-containing inositol 5-phosphatases (SHIP1/2), when their ITIM is tyrosyl-phosphorylated upon co-aggregation with BCR, and SHIP1 to account for FcgammaRIIB-dependent negative regulation of murine B cell activation. Although human FcgammaRIIB share the same ITIM as murine FcgammaRIIB and similarly inhibit human B cell activation, which among the four known SH2 domain-containing (tyrosine or inositol) phosphatases is/are recruited by human FcgammaRIIB is unclear. Our recent finding that, besides the ITIM, a second tyrosine-based motif is mandatory for murine FcgammaRIIB to recruit SHIP1 challenged the possibility that human FcgammaRIIB recruit this phosphatase. Human FcgammaRIIB indeed lack this motif. Using an experimental model which enabled us to compare human FcgammaRIIB and murine FcgammaRIIB under strictly controlled conditions, we show that SHIP1 is recruited to the intracytoplasmic domain of human FcgammaRIIB and inhibits the same biological responses and intracellular signals as when recruited by murine FcgammaRIIB. Identical results were observed in murine and in human B cells. We demonstrate that SHIP is necessary for human FcgammaRIIB to inhibit BCR signaling, and cannot be replaced by SHP-1 or SHP-2. Although it contains no tyrosine, the C-terminal segment of human FcgammaRIIB was as mandatory as the tyrosine-containing C-terminal segment of murine FcgammaRIIB for SHIP1 to be recruited to the ITIM. This segment, however, did not recruit the adapters Grb2/Grap which were demonstrated to stabilize the recruitment of SHIP1 to the ITIM in murine FcgammaRIIB.

Published
2006

4. Lowe syndrome protein Ocrl1 is translocated to membrane ruffles upon Rac GTPase activation: a new perspective on Lowe syndrome pathophysiology

Author

Fumiko Nagano, Olivier Dorseuil, Véronique Satre, Pierrette Desbois, Joël Lunardi, Adèle Faucherre, Gérard Gacon, Institut Cochin (UMR_S567 / UMR 8104), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Compartimentation et dynamique cellulaires (CDC), Centre National de la Recherche Scientifique (CNRS)-Institut Curie [Paris]-Université Pierre et Marie Curie - Paris 6 (UPMC), Canaux calciques , fonctions et pathologies, Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM), This work was supported by INSERM and CNRS and by grants from the 'Association du Syndrome de Lowe', 'Fe'de'ration des Maladies Orphelines' and 'GIS Maladies Rares' to G.G. and J.L. and from the 'Association pour la Recherche sur le Cancer' to G.G. We also thank the 'Fondation Daniel Ducoin' for support to J.L. A.F. is recipient of fellowships from the 'Association pour la Recherche sur le Cancer' and the 'Fondation pour la Recherche Me'dicale'., Roux-Buisson, Nathalie, Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut Curie [Paris]-Centre National de la Recherche Scientifique (CNRS), Institut Cochin ( UMR_S567 / UMR 8104 ), Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Compartimentation et dynamique cellulaires ( CDC ), Centre National de la Recherche Scientifique ( CNRS ) -INSTITUT CURIE-Université Pierre et Marie Curie - Paris 6 ( UPMC ), and Université Joseph Fourier - Grenoble 1 ( UJF ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Institut National de la Santé et de la Recherche Médicale ( INSERM )

Subjects
MESH: Signal Transduction, MESH: Epidermal Growth Factor, MESH : Molecular Sequence Data, MESH : Phosphoric Monoester Hydrolases, Fluorescent Antibody Technique, RhoGAP domain, MESH: rac GTP-Binding Proteins, Cell membrane, 0302 clinical medicine, MESH : Protein Transport, Epidermal growth factor, MESH: Animals, MESH: Fluorescent Antibody Technique, Genetics (clinical), MESH : Epidermal Growth Factor, 0303 health sciences, Cell migration, General Medicine, rac GTP-Binding Proteins, Cell biology, MESH: COS Cells, Protein Transport, medicine.anatomical_structure, Biochemistry, COS Cells, MESH: Phosphoric Monoester Hydrolases, lipids (amino acids, peptides, and proteins), [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], Lamellipodium, MESH : COS Cells, Signal Transduction, MESH: Enzyme Activation, MESH: Protein Transport, Oculocerebrorenal syndrome, Molecular Sequence Data, Biology, 03 medical and health sciences, Genetics, medicine, Animals, Humans, [SDV.NEU] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], Molecular Biology, Actin, 030304 developmental biology, MESH : Signal Transduction, MESH: Humans, MESH: Molecular Sequence Data, Epidermal Growth Factor, MESH : Humans, MESH : rac GTP-Binding Proteins, medicine.disease, Phosphoric Monoester Hydrolases, Enzyme Activation, MESH : Fluorescent Antibody Technique, [ SDV.NEU ] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], OCRL, MESH : Animals, MESH : Enzyme Activation, 030217 neurology & neurosurgery
Abstract

International audience; Oculocerebrorenal Lowe syndrome is a rare X-linked disorder characterized by bilateral cataract, mental retardation and renal Fanconi syndrome. The Lowe syndrome protein Ocrl1 is a PIP2 5-phosphatase, primarily localized to the trans-Golgi network (TGN), which 'loss of function' mutations result in PIP2 accumulation in patient's cells. Although PIP2 is involved in many cell functions including signalling, vesicle trafficking and actin polymerization, it has been difficult so far to decipher molecular/cellular mechanisms responsible for Lowe syndrome phenotype. We have recently shown that, through its C-terminal RhoGAP domain, Ocrl1 forms a stable complex with Rac GTPase within the cell. In line with this finding, we report here that upon epidermal growth factor induced Rac activation in COS-7 cells, a fraction of Ocrl1 translocates from TGN to plasma membrane and concentrates in membrane ruffles. In order to investigate the functionality of Ocrl1 in plasma membrane, we have analysed PIP2 distribution in human dermal fibroblasts (HDFs) from Lowe patients versus control HDFs. As revealed by both immunodetection and green fluorescent protein-PH binding, PIP2 was found strikingly to accumulate in PDGF induced ruffles in Lowe HDFs when compared with control. This suggests that Ocrl1 is active as a PIP2 5-phosphatase in Rac induced membrane ruffles. Cellular properties such as cell migration and establishment of cell-cell contacts, which depend on ruffling and lamellipodia formation, should be further investigated to understand the pathophysiology of Lowe syndrome.

Published
2005

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