Abstract 3966: 14-3-3 sigma and 14-3-3 zeta plays an opposite role in cell growth inhibition mediated by transforming growth factor-beta 1

2010 ◽  
Author(s):  
Hye-Young Hong ◽  
Woo-Kwang Jeon ◽  
Sung-Ji Park ◽  
Hyung-Ju Jang ◽  
Ji-Yeon Choi ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cell Growth ◽  
Growth Inhibition ◽  
Transforming Growth Factor Beta ◽  
Transforming Growth Factor ◽  
Cell Growth Inhibition ◽  
Growth Factor Beta

scholarly journals Activation of phospholipase D activity in transforming growth factor-beta-induced cell growth inhibition

Cell Research ◽  
2000 ◽  
Vol 10 (2) ◽  
pp. 139-149 ◽  
Author(s):  
Bing Hong ZHOU ◽  
Jun Song CHEN ◽  
Ming Qiang CHAI ◽  
Sheng ZHAO ◽  
Jun LIANG ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cell Growth ◽  
Growth Inhibition ◽  
Phospholipase D ◽  
Transforming Growth Factor Beta ◽  
Transforming Growth Factor ◽  
Cell Growth Inhibition ◽  
Growth Factor Beta

scholarly journals Association of v-ErbA with Smad4 Disrupts TGF-β Signaling

2009 ◽  
Vol 20 (5) ◽  
pp. 1509-1519 ◽  
Author(s):  
Richard A. Erickson ◽  
Xuedong Liu
Keyword(s):  
Growth Factor ◽  
Cell Growth ◽  
Growth Inhibition ◽  
Transforming Growth Factor ◽  
Mechanistic Explanation ◽  
Transforming Growth Factor Β ◽  
Cell Growth Inhibition ◽  
Erythroleukemia Cells ◽  
Avian Erythroblastosis Virus

Disruption of the transforming growth factor-β (TGF-β) pathway is observed in the majority of cancers. To further understand TGF-β pathway inactivation in cancer, we stably expressed the v-ErbA oncoprotein in TGF-β responsive cells. v-ErbA participates in erythroleukemic transformation of cells induced by the avian erythroblastosis virus (AEV). Here we demonstrate that expression of v-ErbA was sufficient to antagonize TGF-β–induced cell growth inhibition and that dysregulation of TGF-β signaling required that v-ErbA associate with the Smad4 which sequesters Smad4 in the cytoplasm. We also show that AEV-transformed erythroleukemia cells were resistant to TGF-β–induced growth inhibition and that TGF-β sensitivity could be recovered by reducing v-ErbA expression. Our results reveal a novel mechanism for oncogenic disruption of TGF-β signaling and provide a mechanistic explanation of v-ErbA activity in AEV-induced erythroleukemia.

Phospholipase C-mediated hydrolysis of phosphatidylcholine is a target of transforming growth factor beta 1 inhibitory signals

1992 ◽  
Vol 12 (1) ◽  
pp. 302-308
Author(s):  
M T Diaz-Meco ◽  
I Dominguez ◽  
L Sanz ◽  
M M Municio ◽  
E Berra ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cell Growth ◽  
Phospholipase C ◽  
Transforming Growth Factor Beta ◽  
Transforming Growth Factor ◽  
Tgf Beta ◽  
Transduction Mechanisms ◽  
Growth Factor Beta ◽  
Mitogenic Signal Transduction ◽  
Hydrolysis Of

Cell growth and tumor transformation can be restrained in certain cell systems by the action of transforming growth factor beta (TGF-beta). It has been established that the mechanism whereby TGF-beta 1 inhibits cell growth does not interfere with the triggering of early mitogenic signal transduction mechanisms. Phospholipase C-catalyzed hydrolysis of phosphatidylcholine (PC) is a relatively late step in the cascade activated by growth factors. Therefore, conceivably activation of phospholipase C-catalyzed hydrolysis of PC could be the target of TGF-beta 1 action. In the study reported here, we demonstrate that TGF-beta 1 inhibits the coupling of ras p21 to the activation of PC hydrolysis, which appears to be critical for the antiproliferative effects of TGF-beta 1.

scholarly journals Transforming growth factor-beta induces growth inhibition and IGF-binding protein-3 production in prostatic stromal cells: abnormalities in cells cultured from benign prostatic hyperplasia tissues

2000 ◽  
Vol 164 (2) ◽  
pp. 215-223 ◽  
Author(s):  
P Cohen ◽  
SE Nunn ◽  
DM Peehl
Keyword(s):  
Benign Prostatic Hyperplasia ◽  
Growth Factor ◽  
Growth Inhibition ◽  
Transforming Growth Factor Beta ◽  
Transforming Growth Factor ◽  
Fold Increase ◽  
Prostatic Hyperplasia ◽  
Igf Binding ◽  
Growth Factor Beta ◽  
Igfbp 3

The IGF axis has been implicated in the pathogenesis of benign prostatic hyperplasia (BPH) via the paracrine action of IGFs and IGF-binding proteins (IGFBPs). In this study, we examined the regulation of cell growth and IGFBP-3 secretion by transforming growth factor-beta (TGF-beta) in prostatic stromal cell (PC-S) cultures from histologically normal tissues and tissues from BPH. PC-S cultures were treated with varying doses of TGF-beta1. Forty-eight hour conditioned media (CM) from these cultures were subjected to Western immunoblotting and ligand blotting for detection and quantification of IGFBPs. IGFBPs-2, -3 and -4 were detected in the CM from normal PC-S cultures. In CM from BPH PC-S, IGFBP-3 levels were 2-fold lower at baseline than in the normal PC-S CM, in addition to the differences in IGFBPs-2 and -5 which we have previously reported. In response to TGF-beta1, a 15-fold increase in the levels of IGFBP-3 was observed in normal PC-S CM, while a mere 2-fold increase was observed in BPH PC-S CM (P<0.001). These findings were confirmed by specific immunoblotting and immunocytochemistry. IGFBP-3 mRNA levels detected by Northern blotting of total RNA extracted from similar cultures showed the induction of IGFBP-3 expression by TGF-beta1 in normal PC-S and its lack of induction in BPH PC-S. Cell growth inhibition in response to TGF-beta1 correlated with the IGFBP-3 concentrations found in CM. Normal PC-S showed a 60% decrease in cell number after 10 days in media with 1 ng/ml TGF-beta1, compared with the untreated control. The decrease in proliferation observed in comparably treated BPH cells was only 20% (P<0.001). In conclusion, BPH PC-S had a reduced IGFBP-3 response to TGF-beta1 and demonstrated decreased TGF-beta1-induced growth inhibition relative to normal PC-S. We hypothesize that in normal PC-S, TGF-beta exerts its anti-proliferative effects by stimulating the production of IGFBP-3, which acts as an inhibitory factor, either by inhibiting IGFs or directly by interacting with cells, and that this process is altered in BPH PC-S.

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