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Vol. 12, Issue 7, 2171-2183, July 2001
and
*Instituto de Investigaciones Biomédicas and
Prolactin (PRL) is a pleiotropic cytokine promoting cellular
proliferation and differentiation. Because PRL activates the Src family
of tyrosine kinases (SFK), we have studied the role of these kinases in
PRL cell proliferation signaling. PRL induced [3H]thymidine incorporation upon transient transfection
of BaF-3 cells with the PRL receptor. This effect was inhibited by
cotransfection with the dominant negative mutant of c-Src
(K>A295/Y>F527, SrcDM). The role of SFK in PRL-induced proliferation
was confirmed in the BaF-3 PRL receptor-stable transfectant, W53 cells,
where PRL induced Fyn and Lyn activation. The SFK-selective inhibitors
PP1/PP2 and herbimycin A blocked PRL-dependent cell proliferation by
arresting the W53 cells in G1, with no evident apoptosis. In parallel,
PP1/PP2 inhibited PRL induction of cell growth-related genes
c-fos, c-jun, c-myc, and
odc. These inhibitors have no effect on PRL-mediated activation of Ras/Mapk and Jak/Start pathways. In contrast, they inhibited the PRL-dependent stimulation of the SFKs substrate Sam68,
the phosphorylation of the tyrosine phosphatase Shp2, and the
PI3K-dependent Akt and p70S6k serine kinases. Consistently, transient
expression of SrcDM in W53 cells also blocked PRL activation of Akt.
These results demonstrate that activation of SFKs is required for cell
proliferation induced by PRL.
Centro de Investigaciones Biológicas, Consejo
Superior de Investigaciones Científicas, Madrid 28029, Spain
Corresponding author. E-mail address:
jmartin{at}iib.uam.es.
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