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Tumor Biology |
-induced Mitogen-activated Protein Kinase and Nuclear Factor 
B Signaling Pathways1
Unité 6032, "Interactions entre Systèmes Protéiques et Différenciation dans la Cellule Tumorale," Centre National de la Recherche Scientifique, Faculté de Médecine, 13385 Marseille Cedex 5, France
Resistance of cancer cells against apoptosis induced by death factors
contributes to the limited efficiency of immune- and drug-induced
destruction of tumors. We report here that insulin and insulin-like
growth factor-I (IGF-I) fully protect HT29-D4 colon carcinoma cells
from IFN-
/tumor necrosis factor-
(TNF) induced apoptosis.
Survival signaling initiated by IGF-I was not dependent on the
canonical survival pathway involving phosphatidylinositol
3'-kinase. In addition, neither pp70S6K nor protein kinase
C conveyed IGF-I antiapoptotic function. Inhibition of
mitogen-activated protein kinase (MAPK)/extracellular signal-regulated
kinase (ERK) with the MAPK/ERK kinase inhibitor PD098059 and MAPK/p38
with the specific inhibitor SB203580 partially reversed, in a
nonadditive manner, the IGF-I survival effect. Inhibition of nuclear
factor 
B (NF-B) activity by preventing degradation of the
inhibitor of NF-B (IB-) with BAY 11-7082 also blocked in part
the IGF-I antiapoptotic effect. However, the complete reversal of the
IGF-I effect was obtained only when NF-B and either MAPK/ERK or
MAPK/p38 were inhibited together. Because these pathways are also those
used by TNF to signal inflammation and survival, these data point to a
cross talk between IGF-I- and TNF-induced signaling. We further report
that TNF-induced IL-8 production was indeed strongly enhanced upon
IGF-I addition, and this effect was totally abrogated by both MAPK and
NF-B inhibitors. The IGF-I antiapoptotic function was
stimulus-dependent because Fas- and IFN/Fas-induced apoptosis was not
efficiently inhibited by IGF-I. This was correlated with the weak
ability of Fas ligation to enhance IL-8 production in the presence or
absence of IGF-I. These findings indicate that the antiapoptotic
function of IGF-I in HT29-D4 cells is based on the enhancement of the
survival pathways initiated by TNF, but not Fas, and mediated by
MAPK/p38, MAPK/ERK, and NF-B, which act in concert to suppress the
proapoptotic signals. In agreement with this model, we show that it was
possible to render HT29-D4 cells resistant to Fas-induced apoptosis
provided that IGF-I and TNF receptors were activated simultaneously.
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