F Rendu

Summary

Country: France

Publications

  1. ncbi request reprint The platelet release reaction: granules' constituents, secretion and functions
    F Rendu
    U428 INSERM, Faculte de Pharmacie, 4 avenue de l Observatoire, 75006 Paris, France
    Platelets 12:261-73. 2001
  2. ncbi request reprint Fc receptor-mediated platelet activation is dependent on phosphatidylinositol 3-kinase activation and involves p120(Cbl)
    A Saci
    INSERM U428, Faculte de Pharmacie, Universite Paris V, 75270 Paris, France
    J Biol Chem 274:1898-904. 1999
  3. ncbi request reprint Thiosulfinates inhibit platelet aggregation and microparticle shedding at a calpain-dependent step
    F Rendu
    U 428 INSERM, Faculte de Pharmacie, Universite Rene Descartes Paris V, France
    Thromb Haemost 86:1284-91. 2001

Collaborators

  • A Saci
  • C Bachelot-Loza
  • S Pain

Detail Information

Publications3

  1. ncbi request reprint The platelet release reaction: granules' constituents, secretion and functions
    F Rendu
    U428 INSERM, Faculte de Pharmacie, 4 avenue de l Observatoire, 75006 Paris, France
    Platelets 12:261-73. 2001
    ..Typical platelet disorders resulting from a storage granule abnormality are referred to as a storage pool defect and are characterized by a prolonged bleeding time...
  2. ncbi request reprint Fc receptor-mediated platelet activation is dependent on phosphatidylinositol 3-kinase activation and involves p120(Cbl)
    A Saci
    INSERM U428, Faculte de Pharmacie, Universite Paris V, 75270 Paris, France
    J Biol Chem 274:1898-904. 1999
    ..Our results suggest that Cbl is involved in platelet signal transduction by the recruitment of PI 3-K to the FcgammaRIIa pathway, possibly by increasing PI 3-K activity...
  3. ncbi request reprint Thiosulfinates inhibit platelet aggregation and microparticle shedding at a calpain-dependent step
    F Rendu
    U 428 INSERM, Faculte de Pharmacie, Universite Rene Descartes Paris V, France
    Thromb Haemost 86:1284-91. 2001
    ..Calpain activation was inhibited by TSs independently of fibrinogen binding. Thus, TSs represent a new category of platelet inhibitors, acting on calpain-induced events...