Basic fibroblast growth factor upregulates cyclooxygenase-2 in I407 cells through p38 MAP kinase

2003 ◽  
Vol 284 (2) ◽  
pp. G269-G279 ◽  
Author(s):  
Teresa G. Tessner ◽  
Filipe Muhale ◽  
Suzanne Schloemann ◽  
Steven M. Cohn ◽  
Aubrey Morrison ◽  
...  
Keyword(s):  
Growth Factor ◽  
Map Kinase ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Mrna Stability ◽  
P38 Map Kinase ◽  
Fibroblast Growth ◽  
P38 Inhibitor ◽  
Cox 2 ◽  
Sb 203580

The intestinal cell line I407 responds to basic fibroblast growth factor (bFGF) by upregulating cyclooxygenase-2 (COX-2) mRNA and protein expression and increasing PGE2production. bFGF treatment of I407 cells results in phosphorylation of p38, and the p38 inhibitor SB-203580 abrogates bFGF-induced PGE2 synthesis. Wild-type p38α (p38αWT) and dominant-negative p38α (p38αDN) stable transfectant clones of I407 cells were used to examine the role of the p38 MAP kinase pathway in the events controlling PGE2 synthesis after treatment with bFGF. Treatment of p38αWT clones with bFGF resulted in increased COX-2 protein levels and PGE2 synthesis similar to those seen in bFGF-treated control-transfected cells. In contrast, the p38αDN clones failed to upregulate COX-2 protein or increase PGE2 synthesis when treated with bFGF. Exogenous arachidonate did not restore PGE2 synthesis by p38αDN cells. bFGF treatment increased COX-2 mRNA stability, and the p38 inhibitor SB-203580 attenuated COX-2 mRNA stability in bFGF-treated I407 cells. These data demonstrate a crucial role for p38α in growth factor-induced PGE2 synthesis by intestinal cells. Furthermore, they indicate that p38 activity is required at a step distal to arachidonate release, most likely COX-2 upregulation, because exogenous arachidonate did not restore PGE2 synthesis.

scholarly journals Involvement of SAPK/JNK in basic fibroblast growth factor-induced vascular endothelial growth factor release in osteoblasts

2003 ◽  
Vol 177 (1) ◽  
pp. 101-107 ◽  
Author(s):  
H Tokuda ◽  
K Hirade ◽  
X Wang ◽  
Y Oiso ◽  
O Kozawa
Keyword(s):  
Vascular Endothelial Growth Factor ◽  
Growth Factor ◽  
Map Kinase ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
P38 Map Kinase ◽  
Vascular Endothelial ◽  
Fibroblast Growth ◽  
Endothelial Growth Factor ◽  
Vegf Release

We previously reported that basic fibroblast growth factor (FGF-2) activates p44/p42 mitogen-activated protein (MAP) kinase resulting in the stimulation of vascular endothelial growth factor (VEGF) release in osteoblast-like MC3T3-E1 cells and that FGF-2-activated p38 MAP kinase negatively regulates VEGF release. In the present study, we investigated the involvement of stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) in FGF-2-induced VEGF release in these cells. FGF-2 markedly induced the phosphorylation of SAPK/JNK. SP600125, an inhibitor of SAPK/JNK, markedly reduced the FGF-2-induced VEGF release. SP600125 suppressed the FGF-2-induced phosphorylation of SAPK/JNK without affecting the phosphorylation of p44/p42 MAP kinase or p38 MAP kinase induced by FGF-2. PD98059, an inhibitor of upstream kinase of p44/p42 MAP kinase, or SB203580, an inhibitor of p38 MAP kinase, failed to affect the FGF-2-induced phosphorylation of SAPK/JNK. A combination of SP600125 and SB203580 suppressed the FGF-2-stimulated VEGF release in an additive manner. These results strongly suggest that FGF-2 activates SAPK/JNK in osteoblasts, and that SAPK/JNK plays a part in FGF-2-induced VEGF release.

scholarly journals p38 MAP kinase regulates IL-1β responses in cultured airway smooth muscle cells

2000 ◽  
Vol 279 (5) ◽  
pp. L932-L941 ◽  
Author(s):  
Johanne D. Laporte ◽  
Paul E. Moore ◽  
Thomas Lahiri ◽  
Igor N. Schwartzman ◽  
Reynold A. Panettieri ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Map Kinase ◽  
Airway Smooth Muscle ◽  
Signal Transduction Pathway ◽  
P38 Map Kinase ◽  
Airway Smooth Muscle Cells ◽  
P38 Inhibitor ◽  
Mitogen Activated Protein ◽  
Cox 2 ◽  
Sb 203580

We have previously reported that interleukin (IL)-1β causes β-adrenergic hyporesponsiveness in cultured human airway smooth muscle (HASM) cells by increasing cyclooxygenase (COX)-2 expression. The purpose of this study was to determine whether p38 mitogen-activated protein (MAP) kinase is involved in these events. IL-1β (2 ng/ml for 15 min) increased p38 phosphorylation fourfold. The p38 inhibitor SB-203580 (3 μM) decreased IL-1β-induced COX-2 by 70 ± 7% ( P < 0.01). SB-203580 had no effect on PGE2 release in control cells but caused a significant (70–80%) reduction in PGE2 release in IL-1β-treated cells. IL-1β increased the binding of nuclear proteins to the oligonucleotides encoding the consensus sequences for activator protein (AP)-1 and nuclear factor (NF)-κB, but SB-203580 did not affect this binding, suggesting that the mechanism of action of p38 was not through AP-1 or NF-κB activation. The NF-κB inhibitor MG-132 did not alter IL-1β-induced COX-2 expression, indicating that NF-κB activation is not required for IL-1β-induced COX-2 expression in HASM cells. IL-1β attenuated isoproterenol-induced decreases in HASM stiffness as measured by magnetic twisting cytometry, and SB-203580 abolished this effect. These results are consistent with the hypothesis that p38 is involved in the signal transduction pathway through which IL-1β induces COX-2 expression, PGE2 release, and β-adrenergic hyporesponsiveness.

scholarly journals Serum induction of the fibroblast growth factor-binding protein (FGF-BP) is mediated through ERK and p38 MAP kinase activation and C/EBP-regulated transcription

Oncogene ◽  
2001 ◽  
Vol 20 (14) ◽  
pp. 1730-1738 ◽  
Author(s):  
Violaine K Harris ◽  
Benjamin L Kagan ◽  
Ranjan Ray ◽  
Christine M Coticchia ◽  
Emmanuelle D Liaudet-Coopman ◽  
...  
Keyword(s):  
Growth Factor ◽  
Map Kinase ◽  
Fibroblast Growth Factor ◽  
Binding Protein ◽  
P38 Map Kinase ◽  
Fibroblast Growth ◽  
Kinase Activation ◽  
Factor Binding

Basic Fibroblast Growth Factor is Involved in Bisphenol S Induced Proliferation of Hemangioma Cells

2020 ◽  
Author(s):  
Dahai Liu ◽  
Yubo Hui ◽  
Junrong Wang ◽  
Cong Ye ◽  
Jianshi Du
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Mrna Stability ◽  
Fibroblast Growth ◽  
Bisphenol S ◽  
Down Regulation ◽  
Endocrine Disrupting Compound ◽  
Common Benign Tumor ◽  
Targeted Inhibition

Abstract BackgroundThe hyperproliferation of mesoblastic vascular tissues can lead to the incidence of hemangioma (IHA), which is the most common benign tumor in infants. Estrogenic signals can trigger the progression of HA via activation of gene transcription.ResultsWe found that bisphenol S (BPS), one widely spread endocrine disrupting compound (EDC), can induce the proliferation of HA cells and trigger the G1 to S transition of cell cycle. Among the tested cytokines, BPS can up regulate of basic fibroblast growth factor (bFGF). Targeted inhibition of bFGF via its neutralization antibody can reverse BPS induced cell proliferation. Mechanistically, BPS can increase the mRNA expression of bFGF via increasing the transcription and mRNA stability. The activation of p65 and down regulation of miR-155-5p were responsible for BPS induced transcription and mRNA stability of bFGF, respectively. Conclusions: BPS can increase the expression of bFGF via activation of p65 and down regulation of miR-155-5p, which resulted in the proliferation of HA cells.

scholarly journals Stimulation of C2C12 myoblast growth by basic fibroblast growth factor and insulin-like growth factor 1 can occur via mitogen-activated protein kinase-dependent and -independent pathways.

1996 ◽  
Vol 16 (11) ◽  
pp. 5964-5973 ◽  
Author(s):  
D J Milasincic ◽  
M R Calera ◽  
S R Farmer ◽  
P F Pilch
Keyword(s):  
Growth Factor ◽  
Map Kinase ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Kinase Inhibitor ◽  
Cellular Responses ◽  
Fibroblast Growth ◽  
Map Kinase Cascade ◽  
Mitogen Activated Protein ◽  
Kinase Cascade

It is now well-recognized that the mitogen-activated protein (MAP) kinase cascade facilitates signaling from an activated tyrosine kinase receptor to the nucleus. In fact, an increasing number of extracellular effectors have been reported to activate the MAP kinase cascade, with a significant number of cellular responses attributed to this activation. We set out to explore how two extracellular effectors, basic fibroblast growth factor (bFGF) and insulin-like growth factor 1 (IGF-1), which have both been reported to activate MAP kinase, generate quite distinct cellular responses in C2C12 myoblasts. We demonstrate here that bFGF, which is both a potent mitogen and inhibitor of myogenic differentiation, is a strong MAP kinase agonist. By contrast, IGF-1, which is equally mitogenic for C2C12 cells but ultimately enhances the differentiated phenotype, is a weak activator of the MAP kinase cascade. We further demonstrate that IGF-1 is a potent activator of both insulin receptor substrate IRS-1 tyrosyl phosphorylation and association of IRS-1 with activated phosphatidylinositol 3-kinase (PI 3-kinase). Finally, use of the specific MAP kinase kinase inhibitor, PD098059, and wortmannin, a PI 3-kinase inhibitor, suggests the existence of an IGF-1-induced, MAP kinase-independent signaling event which contributes to the mitogenic response of this factor, whereas bFGF-induced mitogenesis appears to strongly correlate with activation of the MAP kinase cascade.

scholarly journals Divergence in the anti-apoptotic signalling pathways used by nerve growth factor and basic fibroblast growth factor (bFGF) in PC12 cells: rescue by bFGF involves protein kinase Cδ

2000 ◽  
Vol 352 (1) ◽  
pp. 175-182 ◽  
Author(s):  
Maribeth M. WERT ◽  
H. Clive PALFREY
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Protein Kinase ◽  
Map Kinase ◽  
Fibroblast Growth Factor ◽  
Pc12 Cells ◽  
Basic Fibroblast Growth Factor ◽  
Dominant Negative ◽  
Signalling Pathways ◽  
Fibroblast Growth

The mechanisms whereby nerve growth factor (NGF) and basic fibroblast growth factor (bFGF) block apoptosis in serum-deprived PC12 cells were investigated. NGF, but not bFGF, strongly activated Akt/protein kinase B, a downstream effector of phosphoinositide (phosphatidylinositol) 3-kinase (PI 3-kinase). In addition, inhibition of PI 3-kinase by LY294002 partially blocked inhibition of apoptosis by NGF, but not that by bFGF, suggesting divergence in NGF and bFGF anti-apoptotic signalling pathways. Both growth factors strongly activated mitogen-activated protein (MAP) kinases, but blockade of signalling through this pathway, either by the expression of dominant-negative Ras or by treatment with the MAP kinase/ERK kinase (MEK) inhibitor U0126, partially inhibited only bFGF, but not NGF, anti-apoptotic signalling. Use of isoform-specific protein kinase C (PKC) inhibitors such as bisindoylmaleimide-I and Gö 6983 suggested that PKCδ is a likely component of bFGF trophic signalling. A role for PKCδ was confirmed in PC12 cells expressing a dominant-negative PKCδ fragment, in which reversal of apoptosis by bFGF was partially blocked. The PKCδ signal was not mediated by the MAP kinase cascade, as bFGF activation of this pathway was not affected in cells expressing the dominant-negative PKCδ fragment. Full inhibition of bFGF anti-apoptotic signalling occurred when both the PKCδ and Ras/MAP kinase pathways were inhibited. Together, these data demonstrate that inhibition of apoptosis by bFGF in PC12 cells operates differently from that mediated by NGF, requiring the addition of signals from both the Ras/MAP kinase and PKC signalling pathways.

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