The Platelet-Activating Factor Receptor Activates the Extracellular Signal-Regulated Kinase Mitogen-Activated Protein Kinase and Induces Proliferation of Epidermal Cells through an Epidermal Growth Factor-Receptor-Dependent Pathway

Marques, Sílvio Alencar; Dy, Lady C.; Southall, Michael D.; Yi, Quiaofang; Smietana, E. V.A.; Kapur, Reuben; Marques, Mariangela; Travers, Jeffrey B.; Spandau, Dan F.

doi:10.1124/jpet.300.3.1026

Cited by 57 publications

(40 citation statements)

References 41 publications

(50 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Therefore, it seems that NE-induced p38 MAPK activation is independent of EGFR transactivation in rabbit VSMC. This is similar to the report that platelet-activating factor-induced EGFR transactivation does not contribute to p38 MAPK activation by this agonist in epidermal cells (Marques et al, 2002), but is in contrast to the report of Eguchi et al (2001), which demonstrated EGFR-dependent p38 MAPK activation in rat VSMC. To reconcile the differences between these findings, the contribution of EGFR to the activation of p38 MAPK by NE and angiotensin II was compared in rabbit and rat VSMC using the EGFR kinase inhibitor AG1478.…”

Section: Discussioncontrasting

confidence: 57%

Norepinephrine-Induced Stimulation of p38 Mitogen-Activated Protein Kinase Is Mediated by Arachidonic Acid Metabolites Generated by Activation of Cytosolic Phospholipase A₂ in Vascular Smooth Muscle Cells

Kalyankrishna

Malik²

2003

J Pharmacol Exp Ther

View full text Add to dashboard Cite

p38 mitogen-activated protein kinase (MAPK) is activated by norepinephrine (NE) in the vasculature and is implicated in vascular smooth muscle hypertrophy, contraction, and cell migration. NE promotes influx of Ca 2ϩ and activates cytosolic phospholipase A 2 (cPLA 2 ) in vascular smooth muscle cells (VSMC). The purpose of this study was to determine the contribution of cPLA 2 -generated arachidonic acid (AA) and its metabolites to the activation of p38 MAPK measured by its phosphorylation, in response to NE in rabbit VSMC. NE-induced p38 MAPK activation was found to be mediated through the stimulation of ␣-1 and ␣-2 adrenergic receptors, was dependent on extracellular Ca 2ϩ , and was attenuated by an inhibitor of cPLA 2 (pyrrolidine-1). Moreover, the cPLA 2 product, AA, activated p38 MAPK in VSMC. p38 MAPK activation elicited by NE was decreased significantly by the lipoxygenase (LO) inhibitor baicalein, and to a lesser extent by the cytochrome P450 inhibitor 17-octadecynoic acid, but was not affected by the cyclooxygenase inhibitor indomethacin. The LO metabolites of AA, namely 5(S)-hydroxyeicosatetraenoic acid (HETE), 12(S)-HETE, and 15(S)-HETE and the cytochrome P450 metabolite 20-HETE, activated p38 MAPK. NE-induced p38 MAPK stimulation was found to be independent of phospholipase D (PLD) activation in rabbit VSMC. Transactivation of the epidermal growth factor receptor (EGFR) by NE also did not contribute to p38 MAPK activation. These data suggest that cPLA 2 -generated AA and its LO metabolites mediate NE-induced p38 MAPK stimulation in rabbit VSMC by a mechanism that is independent of PLD and EGFR activation.

show abstract

Section: Discussioncontrasting

confidence: 57%

Norepinephrine-Induced Stimulation of p38 Mitogen-Activated Protein Kinase Is Mediated by Arachidonic Acid Metabolites Generated by Activation of Cytosolic Phospholipase A₂ in Vascular Smooth Muscle Cells

Kalyankrishna

Malik²

2003

J Pharmacol Exp Ther

View full text Add to dashboard Cite

show abstract

“…ERK1/2 MAPK and p38 MAPK activation, as well as increased proliferation was induced by PAF in human epidermal KB cells transduced with PAFR gene [66]. These studies suggested that PAF-induced activation of ERK1/2 MAPK occurred via matrix metalloproteinase (MMP)-dependent cleavage of heparin-binding epidermal growth factor (HB-EGF) and subsequent activation of EGF receptor [66]. In contrast, in human melanoma cells, PAF (at nano-molar concentrations) does not stimulate ERK1/2 MAPK phosphorylation (our unpublished data).…”

Section: Paf and Pafr-mediated Signal Transduction Pathwaysmentioning

confidence: 98%

“…In Chinese hamster ovarian cells (CHO), PAF has been shown to trigger phosphorylation of ERK1/2 MAPK in a PKCdependent, RAS-independent manner [64,65]. ERK1/2 MAPK and p38 MAPK activation, as well as increased proliferation was induced by PAF in human epidermal KB cells transduced with PAFR gene [66]. These studies suggested that PAF-induced activation of ERK1/2 MAPK occurred via matrix metalloproteinase (MMP)-dependent cleavage of heparin-binding epidermal growth factor (HB-EGF) and subsequent activation of EGF receptor [66].…”

Section: Paf and Pafr-mediated Signal Transduction Pathwaysmentioning

confidence: 99%

Inflammation and melanoma growth and metastasis: The role of platelet-activating factor (PAF) and its receptor

Melnikova

Bar‐Eli

2007

Cancer Metastasis Rev

View full text Add to dashboard Cite

An inflammatory tumor microenvironment fosters tumor growth, angiogenesis and metastatic progression. Platelet-activating factor (PAF) is an inflammatory biolipid produced from membrane glycerophospholipids. Through the activity of its G-protein coupled receptor, PAF triggers a variety of pathological reactions including tumor neo-angiogenesis. Several groups have demonstrated that inhibiting PAF-PAF receptor pathway at the level of a ligand or receptor results in an effective inhibition of experimental tumor growth and metastasis. In particular, our group has recently demonstrated that PAF receptor antagonists can effectively inhibit the metastatic potential of human melanoma cells in nude mice. Furthermore, we showed that PAF stimulated the phosphorylation of CREB and ATF-1 in metastatic melanoma cells, which resulted in overexpression of MMP-2 and MT1-MMP. Our data indicate that PAF acts as a promoter of melanoma metastasis in vivo. Since only metastatic melanoma cells overexpress CREB/ATF-1, we propose that these cells are better equipped to respond to PAF within the tumor microenvironment when compared to their non-metastatic counterparts.

show abstract

“…Keratinocytes also express PAFreceptors and activation of the epidermal PAF-receptor results in the expression of numerous cytokines including IL-1, IL-6, IL-8, IL-10, TNF-α, prostaglandins, and PAF itself [22][23][24] . Moreover, the epidermal PAF-R can transactivate the epidermal growth factor receptor which can induce a mild proliferative response 25 . It should be noted that the phenotype of a transgenic mouse which overexpressed the PAF-R (by using an actin promoter) included a hyperproliferative dermatitis 26 .…”

Section: Platelet-activating Factor and Keratinocyte Functionmentioning

confidence: 99%

Oxidized glycerophosphocholines as biologically active mediators for ultraviolet radiation-mediated effects

Konger

Marathe

Yao

et al. 2008

Prostaglandins & Other Lipid Mediators

Self Cite

View full text Add to dashboard Cite

Ultraviolet light radiation (UVR) has profound effects upon human skin. Yet, the exact targets for UVR are unclear. Inasmuch as UVR is a known pro-oxidative stressor, one potential target for UVR could be oxidatively modified glycerophosphocholines (GPC). Importantly, recent studies demonstrate that these oxidized GPCs (ox-GPC) are potent agonists for the platelet-activating factor receptor and peroxisome proliferator-activated receptor gamma. This review discusses these new biologically active lipids and their down-stream receptor targets that provide a unique system of biosensors for detecting and responding to UVR photo-oxidation.

show abstract

The Platelet-Activating Factor Receptor Activates the Extracellular Signal-Regulated Kinase Mitogen-Activated Protein Kinase and Induces Proliferation of Epidermal Cells through an Epidermal Growth Factor-Receptor-Dependent Pathway

Cited by 57 publications

References 41 publications

Norepinephrine-Induced Stimulation of p38 Mitogen-Activated Protein Kinase Is Mediated by Arachidonic Acid Metabolites Generated by Activation of Cytosolic Phospholipase A₂ in Vascular Smooth Muscle Cells

Norepinephrine-Induced Stimulation of p38 Mitogen-Activated Protein Kinase Is Mediated by Arachidonic Acid Metabolites Generated by Activation of Cytosolic Phospholipase A₂ in Vascular Smooth Muscle Cells

Inflammation and melanoma growth and metastasis: The role of platelet-activating factor (PAF) and its receptor

Oxidized glycerophosphocholines as biologically active mediators for ultraviolet radiation-mediated effects

Contact Info

Product

Resources

About

The Platelet-Activating Factor Receptor Activates the Extracellular Signal-Regulated Kinase Mitogen-Activated Protein Kinase and Induces Proliferation of Epidermal Cells through an Epidermal Growth Factor-Receptor-Dependent Pathway

Cited by 57 publications

References 41 publications

Norepinephrine-Induced Stimulation of p38 Mitogen-Activated Protein Kinase Is Mediated by Arachidonic Acid Metabolites Generated by Activation of Cytosolic Phospholipase A2 in Vascular Smooth Muscle Cells

Norepinephrine-Induced Stimulation of p38 Mitogen-Activated Protein Kinase Is Mediated by Arachidonic Acid Metabolites Generated by Activation of Cytosolic Phospholipase A2 in Vascular Smooth Muscle Cells

Inflammation and melanoma growth and metastasis: The role of platelet-activating factor (PAF) and its receptor

Oxidized glycerophosphocholines as biologically active mediators for ultraviolet radiation-mediated effects

Contact Info

Product

Resources

About

Norepinephrine-Induced Stimulation of p38 Mitogen-Activated Protein Kinase Is Mediated by Arachidonic Acid Metabolites Generated by Activation of Cytosolic Phospholipase A₂ in Vascular Smooth Muscle Cells

Norepinephrine-Induced Stimulation of p38 Mitogen-Activated Protein Kinase Is Mediated by Arachidonic Acid Metabolites Generated by Activation of Cytosolic Phospholipase A₂ in Vascular Smooth Muscle Cells