Biochem Biophys Res Commun 1998,
PMID: 9712718
Axmann, A; Seidel, D; Reimann, T; Hempel, U; Wenzel, K W
In fibroblasts transforming growth factor-beta1 (TGF-beta1) regulates cell proliferation and turnover of macromolecular components of the extracellular matrix. Here, intracellular signaling events in growth-inhibited embryonic rat lung fibroblasts (RFL-6) upon stimulation with TGF-beta1 were investigated. TGF-beta1 rapidly induced the activation of c-Raf-1, MEK-1, and MAPK p42 and p44. The activation of this pathway by TGF-beta1 did not depend on autocrine platelet-derived growth factor (PDGF) or basic fibroblast growth factor (bFGF). Inhibition of the binding of growth factors to their tyrosine kinase receptors did not affect MAPK activation by TGF-beta1. Ras activation by TGF-beta1 was significantly lower compared to the activation by PDGF or bFGF. The intracellular transduction of the TGF-beta1 signal was completely suppressed by depletion or inhibition of protein kinase C (PKC). It is shown that calcium-dependent isoforms of PKC are required for MAPK activation by TGF-beta1.
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Text Mining Data
p42 → TGF-beta1: "
TGF-beta1 rapidly
induced the activation of c-Raf-1, MEK-1, and MAPK
p42 and p44
"
MEK-1 → TGF-beta1: "
TGF-beta1 rapidly induced the activation of c-Raf-1, MEK-1 , and MAPK p42 and p44
"
c-Raf-1 → TGF-beta1: "
TGF-beta1 rapidly induced the activation of c-Raf-1 , MEK-1, and MAPK p42 and p44
"
MAPK → TGF-beta1: "
Inhibition of the binding of growth factors to their tyrosine kinase receptors did not affect MAPK activation by TGF-beta1
"
MAPK → TGF-beta1: "
It is shown that calcium dependent isoforms of PKC are required for MAPK activation by TGF-beta1
"
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