Receptor type I and type II binding regions and the peptidyl-prolyl isomerase site of cyclophilin B are required for enhancement of T-lymphocyte adhesion to fibronectin
| Autor: | Marie-Christine Slomianny, Sandrine Durieux, Mathieu Carpentier, Fabrice Allain, Geneviève Spik, Bernard Haendler, Christophe Vanpouille |
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| Přispěvatelé: | Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Université de Lille-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2002 |
| Předmět: |
Models
Molecular T-Lymphocytes MESH: Adjuvants Immunologic MESH: Cell Cycle MESH: Peptidylprolyl Isomerase MESH: DNA Replication Biochemistry MESH: Cyclosporine Jurkat Cells Cyclosporin a MESH: DNA-Directed DNA Polymerase MESH: Fibronectins Prolyl isomerase MESH: Jurkat Cells MESH: Immune Sera MESH: Animals MESH: Cellulose Receptor MESH: Peptide Fragments Glycosaminoglycans chemistry.chemical_classification biology Calcineurin MESH: S Phase MESH: Glycosaminoglycans Peptidylprolyl Isomerase MESH: Saccharomyces cerevisiae MESH: Amino Acid Substitution Endocytosis Amino acid MESH: Mutagenesis Site-Directed MESH: Endocytosis Cyclosporine MESH: Fungal Proteins MESH: Calcineurin MESH: Models Molecular Protein Binding MESH: Cell Nucleus Isomerase activity Receptors Peptide MESH: Binding Competitive MESH: Aphidicolin MESH: Nucleic Acid Denaturation Binding Competitive MESH: G1 Phase MESH: Cell Adhesion Adjuvants Immunologic MESH: Plasmids Cell Adhesion Humans MESH: Protein Binding [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Binding site MESH: Replication Protein A MESH: Mice MESH: Cation Exchange Resins MESH: Receptors Peptide Binding Sites MESH: Humans Binding protein MESH: Chromatography Ion Exchange Peptide Fragments Fibronectins Fibronectin MESH: Growth Inhibitors MESH: DNA Fungal MESH: Proliferating Cell Nuclear Antigen MESH: T-Lymphocytes chemistry Amino Acid Substitution MESH: Binding Sites MESH: DNA Superhelical biology.protein Mutagenesis Site-Directed MESH: Nuclear Proteins MESH: DNA-Binding Proteins MESH: Electrophoresis Polyacrylamide Gel |
| Zdroj: | Biochemistry Biochemistry, American Chemical Society, 2002, 41 (16), pp.5222-9 Biochemistry, 2002, 41 (16), pp.5222-9 |
| ISSN: | 0006-2960 1520-4995 |
| Popis: | Cyclophilin B (CyPB), a cyclosporin A (CsA) binding protein, interacts with two types of binding sites at the surface of T-lymphocytes. The type I sites correspond to functional receptors involved in endocytosis and the type II sites to sulfated glycosaminoglycans (GAGs). Mutational analysis of CyPB has revealed that W128, which is part of the CsA-binding pocket, is implicated in the binding to the functional type I receptors and that two amino acid clusters located in the N-terminus ensure the binding to GAGs. The peptidyl-prolyl isomerase activity of CyPB is not required for receptor binding. We have recently demonstrated that CyPB enhances adhesion of peripheral blood T-lymphocytes to fibronectin, a component of the extracellular matrix. We intended to identify additional amino acids involved in the binding of CyPB to its functional type I receptor and to determine regions responsible for the stimulation of peripheral blood T-lymphocyte adhesion. We determined that residues R76, G77, K132, D155, and D158 of the calcineurin (CN) interacting region were implicated in the recognition of type I receptor but not of GAGs. We also found that two different changes in the N-terminal extension that abated binding to GAGs prevented adhesion of peripheral blood T-lymphocytes to coated CyPB, whereas abbrogation of the PPIase activity had no effect. On the other hand, the adhesion of peripheral blood T-lymphocytes to coated fibronectin was not stimulated by CyPB mutants devoid of either type I receptor or GAGs binding activity or by mutants of the PPIase site. Altogether, the results demonstrate that different regions of CyPB are involved in peripheral blood T-lymphocyte activation and imply a novel important physiological function for peptidyl-prolyl isomerase activity. |
| Databáze: | OpenAIRE |
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