Metabolism of n-6 fatty acids by NIH-3T3 cells transfected with the ras oncogene

1994 ◽  
Vol 139 (1) ◽  
pp. 71-81 ◽  
Author(s):  
R. J. de Antueno ◽  
R. C. Cantrill ◽  
Y-S. Huang ◽  
G. W. Ells ◽  
M. Elliot ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Ras Oncogene ◽  
3T3 Cells ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

scholarly journals Alpha B-crystallin expression in mouse NIH 3T3 fibroblasts: glucocorticoid responsiveness and involvement in thermal protection.

1993 ◽  
Vol 13 (3) ◽  
pp. 1824-1835 ◽  
Author(s):  
A Aoyama ◽  
E Fröhli ◽  
R Schäfer ◽  
R Klemenz
Keyword(s):  
Heat Shock ◽  
Thermal Protection ◽  
Cell Clone ◽  
Ectopic Expression ◽  
Small Heat Shock Protein ◽  
Ras Oncogene ◽  
3T3 Cells ◽  
3T3 Fibroblasts ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

alpha B-crystallin, a major soluble protein of vertebrate eye lenses, is a small heat shock protein which transiently accumulates in response to heat shock and other kinds of stress in mouse NIH 3T3 fibroblasts. Ectopic expression of an alpha B-crystallin cDNA clone renders NIH 3T3 cells thermoresistant. alpha B-crystallin accumulates in response to the synthetic glucocorticoid hormone dexamethasone. Dexamethasone-treated NIH 3T3 cells become thermoresistant to the same extent as they accumulate alpha B-crystallin. A cell clone in which alpha B-crystallin is superinduced upon heat shock acquires augmented thermotolerance. Expression of the ras oncogene causes a rapid but transient accumulation of alpha B-crystallin within 1 day. Later, sustained ras oncogene expression suppresses the dexamethasone-mediated alpha B-crystallin accumulation. Thus, oncogenic transformation triggered by the ras oncogene interferes with hormone-mediated accumulation of alpha B-crystallin and concomitant acquisition of thermoresistance. Other known heat shock proteins do not accumulate in response to ectopic alpha B-crystallin expression or to dexamethasone treatment. These results indicate that alpha B-crystallin can protect NIH 3T3 fibroblasts from thermal shock.

Identifying the factors and signal pathways necessary for anchorage-independent growth of Ha-ras oncogene-transformed NIH/3T3 cells

Life Sciences ◽  
2003 ◽  
Vol 73 (10) ◽  
pp. 1265-1274 ◽  
Author(s):  
Tsuey-Yu Chang ◽  
Wen-Jiuan Tsai ◽  
Chao-Kai Chou ◽  
Nan-Haw Chow ◽  
Tzeng-Horng Leu ◽  
...  
Keyword(s):  
Signal Pathways ◽  
Ras Oncogene ◽  
3T3 Cells ◽  
Anchorage Independent Growth ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

scholarly journals A human Ki-ras oncogene encodes two transforming p21 proteins.

1986 ◽  
Vol 6 (4) ◽  
pp. 1326-1328 ◽  
Author(s):  
M S McCoy ◽  
R A Weinberg
Keyword(s):  
Ras Oncogene ◽  
3T3 Cells ◽  
Ras Gene ◽  
P21 Protein ◽  
Nih 3T3 ◽  
P21 Proteins ◽  
Nih 3T3 Cells

The human Ki-ras gene was previously reported to contain two alternative fourth exons which encode two distinct p21 proteins differing only at their carboxy termini. The present study shows that either p21 protein is able on its own to transform NIH 3T3 cells to a tumorigenic state.

scholarly journals Depletion of c-myc with specific antisense sequences reverses the transformed phenotype in ras oncogene-transformed NIH 3T3 cells.

1991 ◽  
Vol 11 (7) ◽  
pp. 3699-3710 ◽  
Author(s):  
M D Sklar ◽  
E Thompson ◽  
M J Welsh ◽  
M Liebert ◽  
J Harney ◽  
...  
Keyword(s):  
Nude Mice ◽  
Growth Rates ◽  
Monolayer Culture ◽  
Soft Agar ◽  
Ras Oncogene ◽  
Minimum Level ◽  
3T3 Cells ◽  
Sense Orientation ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

ras oncogene-transformed NIH 3T3 cells expressing glucocorticoid-inducible antisense c-myc cDNA transcripts at levels sufficient to deplete c-myc protein lost their transformed morphology and the ability to grow in soft agar; their ability to form tumors in nude mice was also impaired. These changes were dependent on the continuous expression of the antisense sequences. No major effects on plating efficiencies, growth rates in monolayer culture, or immortalization were observed in the revertant cells, indicating that the observed effects were not a toxic consequence of c-myc protein depletion. Transfection with the same vector expressing c-myc in the sense orientation or other control vectors had no effect on transformation. These results suggest that a certain minimum level of expression of c-myc is required for the maintenance of ras transformation in NIH 3T3 cells.

Transformed NIH 3T3 cells expressing human melanoma N-ras oncogene metastasize to lymph node in nude mice

1989 ◽  
Vol 7 (4) ◽  
pp. 391-403 ◽  
Author(s):  
J. Jouanneau ◽  
M. Longuet ◽  
S. Bertrand
Keyword(s):  
Lymph Node ◽  
Nude Mice ◽  
Human Melanoma ◽  
Ras Oncogene ◽  
3T3 Cells ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

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)

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