scholarly journals Independent transcriptional regulation of a single VL30 element by epidermal growth factor and activators of protein kinase C.

1988 ◽  
Vol 8 (5) ◽  
pp. 2247-2250 ◽  
Author(s):  
K D Rodland ◽  
L L Muldoon ◽  
T H Dinh ◽  
B E Magun
Keyword(s):  
Transcriptional Regulation ◽  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Epidermal Growth Factor ◽  
Cell Line ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Epidermal Growth ◽  
Stimulation Of

A single VL30 element present in the RVL-3 cell line was transcriptionally induced by both epidermal growth factor (EGF) and the protein kinase C (pkC) activators 12-O-tetradecanoylphorbol-13-acetate (TPA) and sn-1,2-dioctanoylglycerol within 5 min of stimulation. Following TPA-induced depletion of protein kinase C activity, EGF stimulation of VL30 transcription and accumulation was unaffected while TPA effects were inhibited, implying that EGF and TPA act by separable pathways.

Independent transcriptional regulation of a single VL30 element by epidermal growth factor and activators of protein kinase C

1988 ◽  
Vol 8 (5) ◽  
pp. 2247-2250
Author(s):  
K D Rodland ◽  
L L Muldoon ◽  
T H Dinh ◽  
B E Magun
Keyword(s):  
Transcriptional Regulation ◽  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Epidermal Growth Factor ◽  
Cell Line ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Epidermal Growth ◽  
Stimulation Of

A single VL30 element present in the RVL-3 cell line was transcriptionally induced by both epidermal growth factor (EGF) and the protein kinase C (pkC) activators 12-O-tetradecanoylphorbol-13-acetate (TPA) and sn-1,2-dioctanoylglycerol within 5 min of stimulation. Following TPA-induced depletion of protein kinase C activity, EGF stimulation of VL30 transcription and accumulation was unaffected while TPA effects were inhibited, implying that EGF and TPA act by separable pathways.

scholarly journals Epidermal growth factor stimulation of stromelysin mRNA in rat fibroblasts requires induction of proto-oncogenes c-fos and c-jun and activation of protein kinase C.

1990 ◽  
Vol 10 (8) ◽  
pp. 4284-4293 ◽  
Author(s):  
S E McDonnell ◽  
L D Kerr ◽  
L M Matrisian
Keyword(s):  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Epidermal Growth Factor ◽  
Kinase Activation ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Epidermal Growth ◽  
Rat Fibroblasts ◽  
Stimulation Of

Stromelysin (transin) is a secreted metalloprotease that is transcriptionally induced by a variety of growth factors and oncogenes. We examined the necessity of specific secondary (protein kinase C) and tertiary (c-fos and c-jun protein products) messengers in the transactivation of stromelysin gene expression by epidermal growth factor (EGF). Rat-1 fibroblasts exposed to antisense c-fos DNA or RNA demonstrated that c-fos expression was necessary for complete EGF induction of stromelysin expression. Similar results demonstrating the necessity of c-jun protein in the EGF induction of stromelysin were obtained. We also demonstrated that protein kinase C activation is required for the EGF induction of stromelysin, since phorbol ester desensitization of C kinase proteins abolished the ability of EGF to induce stromelysin mRNA, protein, and promoter activity. In reconstitution experiments, neither c-fos, c-jun, nor C kinase activation alone induced significant stromelysin expression. Overexpression of c-fos and c-jun was able to induce stromelysin to a level similar to that of the growth factor, and stimulation of protein kinase C activity augmented this induction. The data suggest that the EGF induction of stromelysin in rat fibroblasts procedes through a pathway involving c-fos, c-jun, and protein kinase C.

Epidermal growth factor stimulation of stromelysin mRNA in rat fibroblasts requires induction of proto-oncogenes c-fos and c-jun and activation of protein kinase C

1990 ◽  
Vol 10 (8) ◽  
pp. 4284-4293
Author(s):  
S E McDonnell ◽  
L D Kerr ◽  
L M Matrisian
Keyword(s):  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Epidermal Growth Factor ◽  
Kinase Activation ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Epidermal Growth ◽  
Rat Fibroblasts ◽  
Stimulation Of

Stromelysin (transin) is a secreted metalloprotease that is transcriptionally induced by a variety of growth factors and oncogenes. We examined the necessity of specific secondary (protein kinase C) and tertiary (c-fos and c-jun protein products) messengers in the transactivation of stromelysin gene expression by epidermal growth factor (EGF). Rat-1 fibroblasts exposed to antisense c-fos DNA or RNA demonstrated that c-fos expression was necessary for complete EGF induction of stromelysin expression. Similar results demonstrating the necessity of c-jun protein in the EGF induction of stromelysin were obtained. We also demonstrated that protein kinase C activation is required for the EGF induction of stromelysin, since phorbol ester desensitization of C kinase proteins abolished the ability of EGF to induce stromelysin mRNA, protein, and promoter activity. In reconstitution experiments, neither c-fos, c-jun, nor C kinase activation alone induced significant stromelysin expression. Overexpression of c-fos and c-jun was able to induce stromelysin to a level similar to that of the growth factor, and stimulation of protein kinase C activity augmented this induction. The data suggest that the EGF induction of stromelysin in rat fibroblasts procedes through a pathway involving c-fos, c-jun, and protein kinase C.

scholarly journals Rapid stimulation of amyloid precursor protein release by epidermal growth factor: role of protein kinase C

1997 ◽  
Vol 327 (1) ◽  
pp. 245-249 ◽  
Author(s):  
Barbara E. SLACK ◽  
Jeffrey BREU ◽  
Lisa MUCHNICKI ◽  
Richard J. WURTMAN
Keyword(s):  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Epidermal Growth Factor ◽  
Amyloid Precursor Protein ◽  
Egf Receptor ◽  
A431 Cells ◽  
Kinase C ◽  
Epidermal Growth ◽  
Stimulation Of

The amyloid precursor protein (APP) of Alzheimer's disease is a transmembrane protein that is cleaved by an uncharacterized enzyme known as α-secretase within its extracellular/intraluminal domain after the activation of guanine nucleotide-binding protein-coupled receptors linked to phosphoinositide hydrolysis. The secretory process results in the release of large soluble derivatives of APP (APPs), and, when elicited by muscarinic receptor activation, exhibits both protein kinase C (PKC)-dependent and tyrosine phosphorylation-dependent components [Slack, Breu, Petryniak, Srivastava and Wurtman (1995) J. Biol. Chem. 270, 8337–8344]. In this report we examine the regulation of the release of APPs by epidermal growth factor (EGF) receptors, which possess intrinsic tyrosine kinase activity, and are coupled to a variety of effectors including phosphoinositide-specific phospholipase Cγ. In A431 cells, EGF caused time-dependent and dose-dependent increases in the formation of inositol phosphates in cultures prelabelled with myo-[3H]inositol, and in the release of APPs into the culture medium; the two responses exhibited similar time courses and EC50 values for EGF. Concomitant with these effects, there were concentration-dependent (3–300 ng/ml) increases in the phosphorylation of tyrosine residues in several proteins, including the EGF receptor itself. The specific PKC antagonist GF 109203X decreased the effect of EGF by approx. 35% at a concentration that abolished the stimulation of the release of APPs by the PKC activator PMA. Tyrphostin AG 1478, an inhibitor of EGF receptor tyrosine kinase, abolished the EGF-induced release of APPs. These results demonstrate that in A431 cells, activation of the EGF receptor stimulates α-secretase activity by a mechanism that is partly dependent on PKC activity.

Effects of phenothiazines on binding and processing of epidermal growth factor in 3T3 cells

1986 ◽  
Vol 251 (6) ◽  
pp. C904-C911 ◽  
Author(s):  
R. Selinfreund ◽  
P. H. Lin ◽  
J. L. Cooper ◽  
W. Wharton
Keyword(s):  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Epidermal Growth Factor ◽  
Rapid Decrease ◽  
3T3 Cells ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Rapid Reversal ◽  
Epidermal Growth

Chlorpromazine (CPZ) or the functionally related N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide caused a rapid decrease in binding of 125I-epidermal growth factor (EGF) that was due to a specific decrease in receptor affinity. The decrease in ligand binding was observed when cells were exposed to CPZ at either 4 degrees C or 37 degrees C but a rapid reversal of CPZs effects was observed only during a 37 degrees C incubation. In contrast to the decrease in 125I-EGF binding seen after short (30 min) accumulations at 37 degrees C, the presence of CPZ caused a large increase in the amount of cell-associated radioactivity after longer periods (over 1 h) of accumulation. Although the CPZ-induced effect was similar in extent to that observed after the addition of methylamine, the increased accumulation after CPZ was probably not due to a nonspecific ionic neutralization of the lysosomes. CPZ did not lower EGF binding in cultures chronically treated with a phorbol ester to reduce protein kinase C levels, although the CPZ-induced increases in accumulation were still observed in cells with reduced protein kinase C activity.

Epidermal Growth Factor Activates Protein Kinase C in the Human Endometrial Cancer Cell Line HEC-1-A

1997 ◽  
Vol 67 (1) ◽  
pp. 46-50 ◽  
Author(s):  
Patrick Connor ◽  
Francisco Talavera ◽  
Jae-Seong Kang ◽  
James Burke ◽  
James Roberts ◽  
...  
Keyword(s):  
Endometrial Cancer ◽  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Epidermal Growth Factor ◽  
Cell Line ◽  
Cancer Cell Line ◽  
Endometrial Cancer Cell ◽  
Kinase C ◽  
Epidermal Growth
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