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3 results on '"MESH: Serum Amyloid P-Component"'

1. Expression of recombinant human complement C1q allows identification of the C1r/C1s-binding sites

Author

Alberto Mantovani, Christine Moriscot, Régis Daniel, Isabelle Bally, Florence Gonnet, Guy Schoehn, Sarah Ancelet, Gérard J. Arlaud, Nicole M. Thielens, Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-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), Unit for Virus Host-Cell Interactions [Grenoble] (UVHCI), Université Joseph Fourier - Grenoble 1 (UJF)-European Molecular Biology Laboratory [Grenoble] (EMBL)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Analyse et Modélisation pour la Biologie et l'Environnement (LAMBE), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Cergy Pontoise (UCP), Université Paris-Seine-Université Paris-Seine-Université d'Évry-Val-d'Essonne (UEVE)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Istituto Clinico Humanitas [Milan] (IRCCS Milan), Humanitas University [Milan] (Hunimed), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-European Molecular Biology Laboratory [Grenoble] (EMBL)-Université Joseph Fourier - Grenoble 1 (UJF), Université Paris-Seine-Université Paris-Seine-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie structurale (IBS - UMR 5075), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Analyse et Modélisation pour la Biologie et l'Environnement (LAMBE - UMR 8587), Université Paris-Seine-Université Paris-Seine-Université d'Évry-Val-d'Essonne (UEVE)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay-Université d'Évry-Val-d'Essonne (UEVE)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Cergy Pontoise (UCP), and Université Paris-Seine-Université Paris-Seine

Subjects
MESH: Complement C1s, MESH: Complement C1r, MESH: Complement C1q, MESH: Protein Structure, Quaternary, MESH: Serum Amyloid P-Component, Gene Expression, MESH: Recombinant Proteins, MESH: Protein Structure, Tertiary, 0302 clinical medicine, Complement Activation, Complement C1q, Complement C1s, MESH: Immunoglobulin G, 0303 health sciences, Multidisciplinary, Complement component 2, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Biological Sciences, MESH: Amino Acid Substitution, Recombinant Proteins, 3. Good health, MESH: Surface Plasmon Resonance, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Serum Amyloid P-Component, C-Reactive Protein, Biochemistry, MESH: Calcium, MESH: HEK293 Cells, Protein Binding, MESH: Gene Expression, MESH: Complement Activation, Mutation, Missense, Biology, 03 medical and health sciences, Classical complement pathway, MESH: C-Reactive Protein, Humans, MESH: Protein Binding, Binding site, Protein Structure, Quaternary, 030304 developmental biology, MESH: Mutation, Missense, Binding Sites, MESH: Humans, Complement C1r, HEK 293 cells, Protein engineering, Surface Plasmon Resonance, Protein Structure, Tertiary, Complement system, HEK293 Cells, Amino Acid Substitution, MESH: Binding Sites, Immunoglobulin G, Calcium, 030215 immunology
Abstract

Complement C1q is a hexameric molecule assembled from 18 polypeptide chains of three different types encoded by three genes. This versatile recognition protein senses a wide variety of immune and nonimmune ligands, including pathogens and altered self components, and triggers the classical complement pathway through activation of its associated proteases C1r and C1s. We report a method for expression of recombinant full-length human C1q involving stable transfection of HEK 293-F mammalian cells and fusion of an affinity tag to the C-terminal end of the C chain. The resulting recombinant (r) C1q molecule is similar to serum C1q as judged from biochemical and structural analyses and exhibits the characteristic shape of a bunch of flowers. Analysis of its interaction properties by surface plasmon resonance shows that rC1q retains the ability of serum C1q to associate with the C1s-C1r-C1r-C1s tetramer, to recognize physiological C1q ligands such as IgG and pentraxin 3, and to trigger C1r and C1s activation. Functional analysis of rC1q variants carrying mutations of LysA59, LysB61, and/or LysC58, in the collagen-like stems, demonstrates that LysB61 and LysC58 each play a key role in the interaction with C1s-C1r-C1r-C1s, with LysA59 being involved to a lesser degree. We propose that LysB61 and LysC58 both form salt bridges with outer acidic Ca 2+ ligands of the C1r and C1s CUB (complement C1r/C1s, Uegf, bone morphogenetic protein) domains. The expression method reported here opens the way for deciphering the molecular basis of the unusual binding versatility of C1q by mapping the residues involved in the sensing of its targets and the binding of its receptors.

Published
2013
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2. M-ficolin interacts with the long pentraxin PTX3: a novel case of cross-talk between soluble pattern-recognition molecules

Author

Gérard J. Arlaud, Christine Moriscot, Andrea Doni, Guy Schoehn, Chantal Dumestre-Pérard, Nicole M. Thielens, Monique Lacroix, Evelyne Gout, Julien Pérard, Alberto Mantovani, Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-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), Unité de Biochimie des Cancers et Biothérapies, CHU Grenoble, Unité Mixte de Thérapie Cellulaire et Tissulaire, Laboratoire Adaptation et pathogénie des micro-organismes [Grenoble] (LAPM), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS), Unit for Virus Host-Cell Interactions [Grenoble] (UVHCI), Université Joseph Fourier - Grenoble 1 (UJF)-European Molecular Biology Laboratory [Grenoble] (EMBL)-Centre National de la Recherche Scientifique (CNRS), Humanitas Clinical and Research Institute, Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF), and Centre National de la Recherche Scientifique (CNRS)-European Molecular Biology Laboratory [Grenoble] (EMBL)-Université Joseph Fourier - Grenoble 1 (UJF)

Subjects
MESH: Signal Transduction, MESH: Serum Amyloid P-Component, Ligands, chemistry.chemical_compound, MESH: Protein Structure, Tertiary, MESH: Mutant Proteins, 0302 clinical medicine, MESH: Lectins, Lectins, MESH: Ligands, Immunology and Allergy, MESH: Immunity, Humoral, 0303 health sciences, biology, MESH: Acetylglucosamine, PTX3, Cell biology, MESH: Surface Plasmon Resonance, Serum Amyloid P-Component, C-Reactive Protein, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, Biochemistry, MESH: Calcium, MESH: N-Acetylneuraminic Acid, Ficolin, Protein Binding, Signal Transduction, MESH: Immune Tolerance, Immunology, MESH: Microscopy, Electron, Acetylglucosamine, 03 medical and health sciences, Tetramer, MESH: C-Reactive Protein, Immune Tolerance, Humans, MESH: Protein Binding, 030304 developmental biology, Innate immune system, MESH: Humans, Pentraxins, Lectin, Surface Plasmon Resonance, N-Acetylneuraminic Acid, Immunity, Humoral, Protein Structure, Tertiary, Sialic acid, Complement system, Microscopy, Electron, chemistry, biology.protein, Calcium, Mutant Proteins, 030215 immunology
Abstract

Ficolins and pentraxins are soluble oligomeric pattern-recognition molecules that sense danger signals from pathogens and altered self-cells and might act synergistically in innate immune defense and maintenance of immune tolerance. The interaction of M-ficolin with the long pentraxin pentraxin 3 (PTX3) has been characterized using surface plasmon resonance spectroscopy and electron microscopy. M-ficolin was shown to bind PTX3 with high affinity in the presence of calcium ions. The interaction was abolished in the presence of EDTA and inhibited by N-acetyl-D-glucosamine, indicating involvement of the fibrinogen-like domain of M-ficolin. Removal of sialic acid from the single N-linked carbohydrate of the C-terminal domain of PTX3 abolished the interaction. Likewise, an M-ficolin mutant with impaired sialic acid-binding ability did not interact with PTX3. Interaction was also impaired when using the isolated recognition domain of M-ficolin or the monomeric C-terminal domain of PTX3, indicating requirement for oligomerization of both proteins. Electron microscopy analysis of the M-ficolin–PTX3 complexes revealed that the M-ficolin tetramer bound up to four PTX3 molecules. From a functional point of view, immobilized PTX3 was able to trigger M-ficolin–dependent activation of the lectin complement pathway. These data indicate that interaction of M-ficolin with PTX3 arises from its ability to bind sialylated ligands and thus differs from the binding to the short pentraxin C-reactive protein and from the binding of L-ficolin to PTX3. The M-ficolin–PTX3 interaction described in this study represents a novel case of cross-talk between soluble pattern-recognition molecules, lending further credit to the integrated view of humoral innate immunity that emerged recently.

Published
2011
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3. Characterization of the long pentraxin PTX3 as a TNFalpha-induced secreted protein of adipose cells

Author

Abderrahim-Ferkoune, Anissa, Bezy, Olivier, Chiellini, Chiara, Grimaldi, Paul, Bonino, Frederic, Chiellini, C., Maffei, M., Moustaid-Moussa, Naima, Pasqualini, Fabio, Mantovani, Alberto, Ailhaud, Gerard, Amri, Ez-Zoubir, Institut de signalisation, biologie du développement et cancer (ISBDC), Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Université Côte d'Azur (UCA), Dept. Nutrition, Pisa, Italy, Université Pise, Génétique du développement normal et pathologique, Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Dept. Nutrition, Pise, Italy, Dept. Nutrition and Agricultural Experiment Station, Knoxville, The University of Tennessee [Knoxville], Department of Immunology and Cell Biology, and Mario Negri Institute

Subjects
MESH: 3T3 Cells, MESH: Serum Amyloid P-Component, Adipose tissue, Mice, Obese, White adipose tissue, Biochemistry, chemistry.chemical_compound, Mice, 0302 clinical medicine, Endocrinology, Adipocyte, MESH: Gene Expression Regulation, Developmental, Adipocytes, MESH: Obesity, MESH: Animals, MESH: Mice, Obese, [SDV.BDD]Life Sciences [q-bio]/Development Biology, 0303 health sciences, biology, Gene Expression Regulation, Developmental, Cell Differentiation, PTX3, 3T3 Cells, Cell biology, Serum Amyloid P-Component, C-Reactive Protein, Adipose Tissue, Adipogenesis, 030220 oncology & carcinogenesis, MESH: Adipose Tissue, MESH: Cell Differentiation, medicine.medical_specialty, MESH: Diabetes Mellitus, Adipose tissue macrophages, QD415-436, tumor necrosis factor α, 03 medical and health sciences, Internal medicine, MESH: C-Reactive Protein, medicine, Diabetes Mellitus, Animals, Obesity, RNA, Messenger, adipocyte protein 2, MESH: Mice, MESH: Adipocytes, 030304 developmental biology, MESH: RNA, Messenger, Tumor Necrosis Factor-alpha, 3T3-L1, Cell Biology, cytokines, chemistry, MESH: Tumor Necrosis Factor-alpha, biology.protein
Abstract

International audience; Exposure of preadipocytes to long-chain fatty acids induces the expression of several markers of adipocyte differentiation. In an attempt to identify novel genes and proteins that are regulated by fatty acids in preadipocytes, we performed a substractive hybridization screening and identified PTX3, a protein of the pentraxin family. PTX3 mRNA expression is transient during adipocyte differentiation of clonal cell lines and is absent in fully differentiated cells. Stable overexpression of PTX3 in preadipocytes has no effect on adipocyte differentiation. In line with this, PTX3 mRNA is expressed in the stromal-vascular fraction of adipose tissue, but not in the adipocyte fraction; however, in 3T3-F442A adipocytes, the PTX3 gene can be reinduced by tumor necrosis factor alpha (TNFalpha) in a dose-dependent manner. This effect is accompanied by PTX3 protein secretion from both 3T3-F442A adipocytes and explants of mouse adipose tissue. PTX3 mRNA levels are found to be higher in adipose tissue of genetically obese mice versus control mice, consistent with their increased TNFalpha levels. In conclusion, PTX3 appears as a TNFalpha-induced protein that provides a new link between chronic low-level inflammatory state and obesity.

Published
2003
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