Overexpression of phospholipase C-gamma in NIH 3T3 fibroblasts results in increased phosphatidylinositol hydrolysis in response to platelet-derived growth factor and basic fibroblast growth factor

1990 ◽  
Vol 10 (11) ◽  
pp. 6069-6072
Author(s):  
A Cuadrado ◽  
C J Molloy
Keyword(s):  
Growth Factor ◽  
Phospholipase C ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Platelet Derived Growth Factor ◽  
Phosphoinositide Metabolism ◽  
Fibroblast Growth ◽  
3T3 Fibroblasts ◽  
Phospholipase C Gamma ◽  
Nih 3T3

Overexpression of phospholipase C-gamma in fibroblasts led to increased tyrosine phosphorylation of this enzyme in response to platelet-derived growth factor and basic fibroblast growth factor. This correlated with increased phosphoinositide release but not with enhanced mitogenicity. Thus, phospholipase C-gamma-mediated phosphoinositide metabolism may not be limiting in the signaling pathways initiated by these growth factors.

scholarly journals Overexpression of phospholipase C-gamma in NIH 3T3 fibroblasts results in increased phosphatidylinositol hydrolysis in response to platelet-derived growth factor and basic fibroblast growth factor.

1990 ◽  
Vol 10 (11) ◽  
pp. 6069-6072 ◽  
Author(s):  
A Cuadrado ◽  
C J Molloy
Keyword(s):  
Growth Factor ◽  
Phospholipase C ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Platelet Derived Growth Factor ◽  
Phosphoinositide Metabolism ◽  
Fibroblast Growth ◽  
3T3 Fibroblasts ◽  
Phospholipase C Gamma ◽  
Nih 3T3

Overexpression of phospholipase C-gamma in fibroblasts led to increased tyrosine phosphorylation of this enzyme in response to platelet-derived growth factor and basic fibroblast growth factor. This correlated with increased phosphoinositide release but not with enhanced mitogenicity. Thus, phospholipase C-gamma-mediated phosphoinositide metabolism may not be limiting in the signaling pathways initiated by these growth factors.

scholarly journals Direct activation of phospholipase C-gamma by fibroblast growth factor receptor is not required for mesoderm induction in Xenopus animal caps.

1994 ◽  
Vol 14 (5) ◽  
pp. 3006-3012 ◽  
Author(s):  
A J Muslin ◽  
K G Peters ◽  
L T Williams
Keyword(s):  
Growth Factor ◽  
Phospholipase C ◽  
Fibroblast Growth Factor ◽  
Mammalian Cells ◽  
Platelet Derived Growth Factor ◽  
Mesoderm Induction ◽  
Fibroblast Growth ◽  
Gamma Activation ◽  
Fgf Receptor ◽  
Phospholipase C Gamma

Members of the fibroblast growth factor (FGF) family induce mesoderm formation in explants of Xenopus embryonic ectoderm (animal caps). Recent studies have been directed at determining signaling pathways downstream of the FGF receptor that are important in mesoderm induction. We have recently shown that a point mutation in the FGF receptor changing tyrosine 766 to phenylalanine (Y/F mutation) abolishes phospholipase C-gamma (PLC-gamma) activation in mammalian cells. To explore the role of PLC-gamma activation in FGF-stimulated mesoderm induction, we constructed two chimeric receptors, each consisting of the extracellular portion of the platelet-derived growth factor beta receptor, with one having the transmembrane and intracellular portions of the wild-type FGF receptor 1 (PR-FR wt) and the other having the corresponding region of the Y/F766 mutant FGF receptor 1 (PR-FR Y/F766). When expressed in Xenopus oocytes, only PR-FR wt was able to mediate PLC gamma phosphorylation, inositol-1,4,5-trisphosphate accumulation, and calcium efflux in response to platelet-derived growth factor stimulation. However, both receptors mediated mesoderm induction in Xenopus animal caps as measured by cap elongation, muscle-specific actin mRNA induction, and skeletal muscle formation. These results demonstrate that PLC gamma activation by the FGF receptor is not required for FGF-stimulated mesoderm induction.

The erbB-2 mitogenic signaling pathway: tyrosine phosphorylation of phospholipase C-gamma and GTPase-activating protein does not correlate with erbB-2 mitogenic potency

1991 ◽  
Vol 11 (4) ◽  
pp. 2040-2048
Author(s):  
F Fazioli ◽  
U H Kim ◽  
S G Rhee ◽  
C J Molloy ◽  
O Segatto ◽  
...  
Keyword(s):  
Growth Factor ◽  
Dna Synthesis ◽  
Phospholipase C ◽  
Signaling Pathway ◽  
Tyrosine Phosphorylation ◽  
Platelet Derived Growth Factor ◽  
Mitogenic Signaling ◽  
Gtpase Activating Protein ◽  
3T3 Fibroblasts ◽  
Nih 3T3

The erbB-2 gene product, gp185erbB-2, unlike the structurally related epidermal growth factor (EGF) receptor (EGFR), exhibits constitutive kinase and transforming activity. We used a chimeric EGFR/erbB-2 expression vector to compare the mitogenic signaling pathway of the erbB-2 kinase with that of the EGFR, at similar levels of expression, in response to EGF stimulation. The EGFR/erbB-2 chimera was significantly more active in inducing DNA synthesis than the EGFR when either was expressed in NIH 3T3 cells. Analysis of biochemical pathways implicated in signal transduction by growth factor receptors indicated that both phospholipase C type gamma (PLC-gamma) and the p21ras GTPase-activating protein (GAP) are substrates for the erbB-2 kinase in NIH 3T3 fibroblasts. However, under conditions in which activation of the erbB-2 kinase induced DNA synthesis at least fivefold more efficiently than the EGFR, the levels of erbB-2- or EGFR-induced tyrosine phosphorylation of PLC-gamma and GAP were comparable. In addition, the stoichiometry of tyrosine phosphorylation of these putative substrates by erbB-2 appeared to be at least an order of magnitude lower than that induced by platelet-derived growth factor receptors at comparable levels of mitogenic potency. Thus, our results indicate that differences in tyrosine phosphorylation of PLC-gamma and GAP do not account for the differences in mitogenic activity of the erbB-2 kinase compared with either the EGFR or platelet-derived growth factor receptor in NIH 3T3 fibroblasts.

scholarly journals Sequential Delivery of Basic Fibroblast Growth Factor and Platelet-Derived Growth Factor for Angiogenesis

2011 ◽  
Vol 17 (9-10) ◽  
pp. 1181-1189 ◽  
Author(s):  
Jillian E. Tengood ◽  
Ryan Ridenour ◽  
Ross Brodsky ◽  
Alan J. Russell ◽  
Steven R. Little
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Platelet Derived Growth Factor ◽  
Fibroblast Growth
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