Thrombospondin-1 (TSP-1), a new bone morphogenetic protein-2 and -4 (BMP-2/4) antagonist identified in pituitary cells

Autor: Corinne Henriquet, Martine Pugnière, Ida Boulay, Céline Sallon, Grégoire Harichaux, Delphine Logeart-Avramoglou, Philippe Monget, Catherine Taragnat, Valérie Labas, Sylvie Canepa, Isabelle Callebaut, Xavier Cayla, Joël Fontaine
Přispěvatelé: Physiologie de la reproduction et des comportements [Nouzilly] (PRC), Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur] (IFCE)-Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS), Institut de minéralogie, de physique des matériaux et de cosmochimie (IMPMC), Muséum national d'Histoire naturelle (MNHN)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de recherche pour le développement [IRD] : UR206-Centre National de la Recherche Scientifique (CNRS), Sorbonne Université (SU), Université Pierre et Marie Curie - Paris 6 (UPMC), Muséum national d'Histoire naturelle (MNHN), Institut de Recherche pour le Développement (IRD [France-Ouest]), Bioingénierie et Bioimagerie Ostéo-articulaires, Biomécanique et Biomatériaux Ostéo-Articulaires (B2OA (UMR_7052)), École nationale vétérinaire - Alfort (ENVA)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Université Paris Diderot - Paris 7 (UPD7), PRES Sorbonne Paris Cité, Université de Montpellier (UM), Institut de Recherche en Cancérologie de Montpellier (IRCM - U1194 Inserm - UM), CRLCC Val d'Aurelle - Paul Lamarque-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Plateforme d'Imagerie Cellulaire, Institut National de la Recherche Agronomique (INRA), Plateforme d'Analyse Intégrative des Biomolécules, Institut National de Recherche Agronomique, French 'Region Centre', Ministere de la Recherche et de la Technologie, Taragnat, Catherine, Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de recherche pour le développement [IRD] : UR206-Muséum national d'Histoire naturelle (MNHN)-Centre National de la Recherche Scientifique (CNRS), École nationale vétérinaire d'Alfort (ENVA)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université de Tours-Institut Français du Cheval et de l'Equitation [Saumur]-Institut National de la Recherche Agronomique (INRA), Institut de recherche pour le développement [IRD] : UR206-Centre National de la Recherche Scientifique (CNRS)-Muséum national d'Histoire naturelle (MNHN)-Université Pierre et Marie Curie - Paris 6 (UPMC), Sorbonne Universités, Université Pierre et Marie Curie (Paris 6), CRLCC Val d'Aurelle - Paul Lamarque-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS)
Jazyk: angličtina
Rok vydání: 2017
Předmět:
0301 basic medicine
Models
Molecular
Cellular differentiation
mass spectrum analysis
Bone Morphogenetic Protein 2
Bone Morphogenetic Protein 4
thrombospondin
Biochemistry
Thrombospondin 1
Mice
ovin
Genes
Reporter
spectrométrie de masse
C3H10T1/2 cells
microbial culture
Cells
Cultured
culture cellulaire
Chemistry
bone morphogenetic protein (BMP)
pituitary gland
bone morphogenetic protein antagonist
brebis
Recombinant Proteins
3. Good health
Cell biology
Bone morphogenetic protein 7
embryonic structures
Female
Chordin
surface plasmon resonance (SPR)
Animals
Inbred Strains
Autre (Sciences du Vivant)
[SDV.OT]Life Sciences [q-bio]/Other [q-bio.OT]
animal structures
Recombinant Fusion Proteins
Bone morphogenetic protein
Response Elements
Bone morphogenetic protein 2
Cell Line
reproduction
03 medical and health sciences
Paracrine signalling
bone morphogenetic proteins
Animals
Humans
Protein Interaction Domains and Motifs
Molecular Biology
Sheep
Domestic
Thrombospondin
structural model
Sequence Homology
Amino Acid
Computational Biology
gimmers
Cell Biology
030104 developmental biology
hypophyse
bmp
Zdroj: Journal of Biological Chemistry
Journal of Biological Chemistry, 2017, 292 (37), pp.15352-15368. ⟨10.1074/jbc.M116.736207⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2017, 292 (37), pp.15352-15368. ⟨10.1074/jbc.M116.736207⟩
Journal of Biological Chemistry 37 (292), 15352-15368. (2017)
ISSN: 0021-9258
1083-351X
Popis: Remerciements :INRA, UMR PRC 0085, Plateforme CIRE, 37380 NouzillyStephane Fabre and Alan McNeilly for helpful discussionYves Combarnous for helpful suggestions, Maxime Capelle and Marie Champion for technical assistanceElodie Chaillou for critical reading of the manuscript; Bone morphogenetic proteins (BMPs) regulate diverse cellular responses during embryogenesis and in adulthood including cell differentiation, proliferation and death in various tissues. In the adult pituitary, BMPs participate in the control of hormone secretion and cell proliferation suggesting a potential endocrine/paracrine role for BMPs, but some of the mechanisms are unclear. Here, using a bioactivity test based on embryonic cells (C3H10T1/2) transfected with a BMP-responsive element, we sought to determine whether pituitary cells secrete BMPs or BMP antagonists. Interestingly, we found that pituitary-conditioned medium contains a factor that inhibits action of BMP-2 and -4. Combining surface plasmon resonance (SPR) and high-resolution mass spectrometry helped pinpoint this factor as thrombospondin-1 (TSP-1). SPR and co-immunoprecipitation confirmed that recombinant human TSP-1 can bind BMP-2 and -4 and antagonize their effects on C3H10T1/2 cells. Moreover, TSP-1 inhibited the action of serum BMPs. We also report that the von Willebrand type C (VWC) domain of TSP-1 is likely responsible for this BMP-2/4 binding activity, an assertion based on sequence similarity that TSP-1 shares with the VWC domain of Crossveinless 2 (CV-2), a BMP antagonist and member of the chordin family. In summary, we identified for the first time TSP-1 as a BMP-2/-4 antagonist and presented structural basis for the physical interaction between TSP-1 and BMP-4. We propose that TSP-1 could regulate bioavailability of BMPs, either produced locally or reaching the pituitary via the blood circulation. In conclusion, our findings provide new insights into the involvement of TSP-1 in the BMP-2/-4 mechanisms of action.
Databáze: OpenAIRE
Externí odkaz: