Recombinant production and properties of binding of the full set of mouse secreted phospholipases A2 to the mouse M-type receptor
Autor: | Gérard Lambeau, Morgane Rouault, Sabine Scarzello, Michael H. Gelb, Fanny Surrel, Eric Boilard, Sofiane Bezzine, Catherine Le Calvez, Farideh Ghomashchi, James G. Bollinger, Alan G. Singer |
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Přispěvatelé: | Institut de pharmacologie moléculaire et cellulaire (IPMC), Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS), Departments of Chemistry and Biochemistry, University of Washington [Seattle], Laboratoire de Biochimie et de Génie Enzymatique des Lipases (ENIS), École Nationale d'Ingénieurs de Sfax | National School of Engineers of Sfax (ENIS), CNRS, ARC, NIGH, FRM, CIHR, Arthristis Society |
Rok vydání: | 2007 |
Předmět: |
MESH: Drosophila
MESH: Rabbits Secreted Phospholipases A2 Receptors Cell Surface Biology Spodoptera medicine.disease_cause Biochemistry Phospholipases A law.invention MESH: Recombinant Proteins 03 medical and health sciences Mice 0302 clinical medicine law medicine Escherichia coli Animals MESH: Animals MESH: Cloning Molecular [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Cloning Molecular Receptor MESH: Mice MESH: Receptors Cell Surface 030304 developmental biology chemistry.chemical_classification 0303 health sciences MESH: Spodoptera MESH: Escherichia coli Ligand Receptors Phospholipase A2 IIf M-Type Receptor Molecular biology Recombinant Proteins Enzyme chemistry 030220 oncology & carcinogenesis Recombinant DNA MESH: Phospholipases A Drosophila Rabbits |
Zdroj: | Biochemistry Biochemistry, American Chemical Society, 2007, 46 (6), pp.1647-62. ⟨10.1021/bi062119b⟩ |
ISSN: | 0006-2960 1520-4995 |
Popis: | To date, 12 secreted phospholipases A2 (sPLA2s) have been identified in the mouse species and divided into three structural collections (I/II/V/X, III, and XII). On the basis of their different molecular properties and tissue distributions, each sPLA2 is likely to exert distinct functions by acting as an enzyme or ligand for specific soluble proteins or receptors, among which the M-type receptor is the best-characterized target. Here, we present the properties of binding of the full set of mouse sPLA2s to the mouse M-type receptor. All enzymes have been produced in Escherichia coli or insect cells, and their properties of binding to the cloned and native M-type receptor have been determined. sPLA2s IB, IIA, IIE, IIF, and X are high-affinity ligands (K0.5 = 0.3-3 nM); sPLA2s IIC and V are low-affinity ligands (K0.5 = 30-75 nM), and sPLA2s IID, III, XIIA, and XIIB bind only very weakly or do not bind to the M-type receptor (K0.5 > 100 nM). Three exogenous parvoviral group XIII PLA2s and two fungal group XIV sPLA2s do not bind to the receptor. Together, these results indicate that the mouse M-type receptor is selective for only a subset of mouse sPLA2s from the group I/II/V/X structural collection. Binding of mouse sPLA2s to a recombinant soluble mouse M-type receptor leads in all cases to inhibition of enzymatic activity, and the extent of deglycosylation of the receptor decreases yet does not abolish sPLA2 binding. The physiological meaning of binding of sPLA2 to the M-type receptor is discussed on the basis of our current knowledge of sPLA2 functions. |
Databáze: | OpenAIRE |
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