Low M r phosphotyrosine protein phosphatase activity on fibroblast growth factor receptor is not associated with enzyme translocation

FEBS Letters

Rigacci, Stefania²  Bagnoli, Silvia²  Berti, Andrea²  Dello Sbarba, Persio¹  Rovida, Elisabetta¹ 

[1] Department of Experimental Pathology and Oncology, University of Firenze, Viale Morgagni 50, 50134 Firenze, Italy;Department of Biochemical Sciences, University of Firenze, Viale Morgagni 50, 50134 Florence, Italy

关键词: Phosphotyrosine protein phosphatase;    Signal transduction;    Fibroblast growth factor receptor;    Macrophage-colony-stimulating factor receptor;    PTP;    phosphotyrosine protein phosphatase;    EGFr;    epidermal growth factor receptor;    PDGFr;    platelet-derived growth factor receptor;    M-CSFr;    macrophage-colony-stimulating factor receptor;    FGFr;    fibroblast growth factor receptor;    bFGF;    basic FGF;    DMEM;    Dulbecco's modified Eagle's medium;    FCS;    fetal calf serum;    BCA;    bicinchoninic acid;    ECL;    enhanced chemiluminescence;   

DOI  :  10.1016/S0014-5793(99)01234-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Fibroblast growth factor receptor (class IV) shares a certain degree of similarity with class III members like platelet-derived growth factor and macrophage-colony-stimulating factor receptors, which, once activated, are substrates of low M _r phosphotyrosine protein phosphatase. Up until now no phosphotyrosine phosphatase has been shown to act on this receptor in vivo. Here we demonstrate that low M _r phosphotyrosine protein phosphatase is able to reduce receptor tyrosine phosphorylation and cell proliferation in response to basic fibroblast growth factor. Contrary to what was previously observed for platelet-derived growth factor, during cell stimulation with basic fibroblast growth factor, no enzyme redistribution among cellular compartments is observed.

【 授权许可】

Unknown