scholarly journals NIH-3T3 cells transformed with a ras oncogene exhibit a protein kinase C-mediated inhibition of agonist-stimulated Ca2+ inflow

1990 ◽  
Vol 271 (2) ◽  
pp. 309-315 ◽  
Author(s):  
A J Polverino ◽  
B P Hughes ◽  
G J Barritt
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Foetal Calf Serum ◽  
Ras Oncogene ◽  
Wild Type ◽  
3T3 Cells ◽  
Phorbol Dibutyrate ◽  
Kinase C ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

1. The ability of bombesin or platelet-derived growth factor (PDGF) to stimulate Ca2+ inflow (assessed by measuring changes in the intracellular free Ca2+ concentration in cells loaded with fura-2) in NIH-3T3 cells transformed with the EJ/T24-Ha-ras-1 oncogene is inhibited when compared with the action of the agonists on wild-type cells. 2. The effects of transformation with the ras oncogene are associated with complete inhibition of the ability of bombesin to release Ca2+ from intracellular stores, a substantial decrease in the number of bombesin receptors, no change in the ability of foetal calf serum or ionomycin to release Ca2+ from intracellular stores and the activation of protein kinase C. 3. The effects of transformation with the H-ras oncogene on the ability of bombesin or PDGF to stimulate Ca2+ inflow were mimicked by a 30 min exposure of wild-type cells to phorbol dibutyrate. This action of phorbol dibutyrate was completely blocked by prior treatment of wild-type cells for 24 h with the phorbol ester. 4. It is concluded that one of the actions of the H-ras oncogene in fibroblasts is to inhibit agonist-stimulated Ca2+ inflow by a mechanism which involves the activation of protein kinase C.

Regulation of Na+-H+ exchange in normal NIH-3T3 cells and in NIH-3T3 cells expressing the ras oncogene

1989 ◽  
Vol 256 (4) ◽  
pp. C756-C763 ◽  
Author(s):  
N. E. Owen ◽  
J. Knapik ◽  
F. Strebel ◽  
W. G. Tarpley ◽  
R. R. Gorman
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Inositol Trisphosphate ◽  
Biologically Active ◽  
Ras Oncogene ◽  
3T3 Cells ◽  
Calmodulin Antagonist ◽  
Kinase C ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

Our laboratory and others have demonstrated that Na+-H+ exchange can be regulated by two different pathways; one that is mediated by an inositol trisphosphate-stimulated increase in intracellular calcium activity, and one that is mediated by an increase in protein kinase C activity. To determine whether one of these pathways is more important than the other, or whether one pathway is physiologically relevant, we employed normal NIH-3T3 cells (3T3 cells) and NIH-3T3 cells expressing the EJ human bladder ras oncogene (EJ cells). The EJ cells were chosen because they provide a genetic model that does not exhibit serum- or platelet-derived growth factor (PDGF)-stimulated inositol trisphosphate release or Ca2+ mobilization. It was found that serum- or PDGF-stimulated Na+-H+ exchange was more pronounced in EJ cells than in control 3T3 cells. As expected, serum- or PDGF-stimulated Na+-H+ exchange in 3T3 cells was inhibited by chelating intracellular Ca2+ with the intracellular Ca2+ chelator quin2, by the intracellular Ca2+ antagonist 8-(N,N-diethylamino)octyl 3,4,5-trimethoxybenzoate (TMB-8), and by the calmodulin antagonist trifluoperazine. In contrast, these agents did not inhibit serum- or PDGF-stimulated Na+-H+ exchange in EJ cells. Activators of protein kinase C (e.g., 1-oleoyl-2-acetylglycerol or biologically active phorbol esters) were found to stimulate Na+-H+ exchange in EJ cells to the same extent as serum. However, these agents were considerably less effective than serum in control 3T3 cells. Despite these findings, PDGF did not stimulate diacylglycerol levels in EJ cells.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Both the Catalytic and Regulatory Domains of Protein Kinase C Chimeras Modulate the Proliferative Properties of NIH 3T3 Cells

1997 ◽  
Vol 272 (45) ◽  
pp. 28793-28799 ◽  
Author(s):  
Péter Ács ◽  
Qiming J. Wang ◽  
Krisztina Bögi ◽  
Adriana M. Marquez ◽  
Patricia S. Lorenzo ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
3T3 Cells ◽  
Regulatory Domains ◽  
Kinase C ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

Induction of a mitogen-responsive gene after expression of the Ha-ras oncogene in NIH 3T3 fibroblasts

1989 ◽  
Vol 9 (11) ◽  
pp. 5207-5214
Author(s):  
A K Werenskiold ◽  
S Hoffmann ◽  
R Klemenz
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Transcriptional Level ◽  
3T3 Cells ◽  
Serum Factors ◽  
Kinase C ◽  
Conditional Expression ◽  
T1 Gene ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

A cDNA clone, T1, has been isolated whose corresponding mRNA was transiently expressed at highly elevated levels after conditional expression of the Ha-ras(EJ) gene and after mitogenic activation of quiescent NIH 3T3 cells. Glucocorticoid hormone stimulated substantial T1 expression as well but only in proliferating cells. At least two different signaling pathways participate in the regulation of the T1 gene: a protein kinase C-dependent signal is involved in the response of proliferating NIH 3T3 cells to glucocorticoid in the absence but not the presence of p21ras, whereas a protein kinase C-independent mechanism mediates the response to serum factors. Treatment of cells with the protein kinase inhibitor 2-aminopurine blocked induction of expression of the T1 gene. T1 mRNA accumulation is regulated at the transcriptional level.

Inhibitions of protein kinase C and proto-oncogene expressions in NIH 3t3 cells by apigenin

1996 ◽  
Vol 32 (1) ◽  
pp. 146-151 ◽  
Author(s):  
Ying-Tang Huang ◽  
Min-Liang Kuo ◽  
Jer-Yuh Liu ◽  
Su-Yu Huang ◽  
Jen-Kun Lin
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
3T3 Cells ◽  
Kinase C ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

scholarly journals Induction of a mitogen-responsive gene after expression of the Ha-ras oncogene in NIH 3T3 fibroblasts.

1989 ◽  
Vol 9 (11) ◽  
pp. 5207-5214 ◽  
Author(s):  
A K Werenskiold ◽  
S Hoffmann ◽  
R Klemenz
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Transcriptional Level ◽  
3T3 Cells ◽  
Serum Factors ◽  
Kinase C ◽  
Conditional Expression ◽  
T1 Gene ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

A cDNA clone, T1, has been isolated whose corresponding mRNA was transiently expressed at highly elevated levels after conditional expression of the Ha-ras(EJ) gene and after mitogenic activation of quiescent NIH 3T3 cells. Glucocorticoid hormone stimulated substantial T1 expression as well but only in proliferating cells. At least two different signaling pathways participate in the regulation of the T1 gene: a protein kinase C-dependent signal is involved in the response of proliferating NIH 3T3 cells to glucocorticoid in the absence but not the presence of p21ras, whereas a protein kinase C-independent mechanism mediates the response to serum factors. Treatment of cells with the protein kinase inhibitor 2-aminopurine blocked induction of expression of the T1 gene. T1 mRNA accumulation is regulated at the transcriptional level.

INTERLEUKIN-1β-INDUCED EXPRESSION OF PROTEIN KINASE C (PKC)-δ AND ϵ IN NIH 3T3 CELLS

Cytokine ◽  
1997 ◽  
Vol 9 (8) ◽  
pp. 577-581 ◽  
Author(s):  
Claire L. Varley ◽  
Barry L. Brown ◽  
Nigel Groome ◽  
Pauline R.M. Dobson
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Interleukin 1Β ◽  
3T3 Cells ◽  
Induced Expression ◽  
Kinase C ◽  
Nih 3T3 ◽  
Nih 3T3 Cells
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