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Vol. 60, Issue 5, 924-933, November 2001
Consorzio Mario Negri Sud, Istituto di Ricerche Farmacologiche
"Mario Negri", Santa Maria Imbaro, Italy (L.S., M.S., G.M.D.); and
Istituto Neurologico Mediterraneo Neuromed, Pozzilli, Italy (L.I.,
L.C., A.D.B.)
The involvement of mitogen-activated protein (MAP) kinases in the
mitogenic effect of thyrotropin (TSH) is not fully elucidated. In
FRTL-5 cells, we found that the MAP kinase kinase (MEK) inhibitors UO126 and PD98059 substantially decreased TSH-induced DNA synthesis, indicating that MAP kinases are involved in the TSH-stimulated proliferative response. Accordingly, TSH, forskolin (FSK) and 8-bromo-cAMP induced a rapid (3 min) and transient activation of
ERK1/2, as assessed by phosphorylation of myelin basic protein and
ERK1/2. This effect was cAMP-dependent and protein kinase A
(PKA)-independent. The activation of Rap1 and B-Raf was involved in the
mechanism of MAP kinase stimulation by TSH. TSH induced rapid (3 min) GDP/GTP exchange and activation of Rap1. After a 3-min exposure to
FSK, B-Raf was recruited to a vesicular compartment, where it
colocalized with Rap1. Both activation of Rap1 and translocation of
B-Raf were PKA-independent. The Rap1 dominant negative Rap1N17 significantly reduced TSH-stimulated but not insulin-like growth factor
1-stimulated ERK1/2 phosphorylation, whereas the Ras dominant negative RasN17 inhibited the effect of both agonists. In conclusion, our results document that TSH increases intracellular cAMP, which rapidly stimulates MAP kinase cascade independent of PKA. This novel
mechanism could integrate other pathways involved in TSH-stimulated proliferative response.
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