Thrombin Up-regulates Tissue Factor Pathway Inhibitor-2 Synthesis through a Cyclooxygenase-2-dependent, Epidermal Growth Factor Receptor-independent Mechanism

Neaud, Véronique; Duplantier, Jennifer Gillibert; Mazzocco, Claire; Kisiel, Walter; Rosenbaum, Jean

doi:10.1074/jbc.m306679200

Cited by 37 publications

(32 citation statements)

References 41 publications

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“…Finally, our data highlight the complex network of crosssignaling between the GPCR and MAPK/Erk pathways (46)(47)(48). This PGE 2 -mediated cross-talk can shift the balance between the stimulatory and inhibitory responses in NSCLC toward pro-survival and proliferative phenotypes that ultimately may determine the cancer cell resistance to pharmacologic EGFR inhibition.…”

Section: Discussionmentioning

confidence: 74%

Prostaglandin E2 Activates Mitogen-Activated Protein Kinase/Erk Pathway Signaling and Cell Proliferation in Non–Small Cell Lung Cancer Cells in an Epidermal Growth Factor Receptor–Independent Manner

Krysan¹,

Reckamp

Dalwadi³

et al. 2005

Cancer Research

214

163

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Cyclooxygenase 2 (COX-2) overexpression is found in a wide variety of human cancers and is linked to all stages of tumorigenesis. Elevated tumor COX-2 expression is associated with increased angiogenesis, tumor invasion, suppression of host immunity and promotes tumor cell resistance to apoptosis. Previous reports have linked the COX-2 product prostaglandin E 2 (PGE 2 ) to the abnormal activation of the mitogen-activated protein kinase/Erk kinase pathway. Here we show that PGE 2 is able to rapidly stimulate Erk phosphorylation in a subset of non-small cell lung cancer (NSCLC) cell lines. This effect is not evident in bronchial epithelial cells. In contrast to previous reports in colon cancer, we found that Erk activation as well as cellular proliferation induced by PGE 2 was not inhibited by pretreatment of the cells with epidermal growth factor receptor (EGFR) inhibitors. Activation of the Erk pathway by PGE 2 was also resistant to src kinase inhibitors but sensitive to the protein kinase C inhibition. PGE 2 effects are mediated through four G protein-coupled receptors. Selective inhibition of EP receptors revealed the possible involvement of Ca 2+ -dependent signaling in PGE 2 -mediated activation of Erk. Our data indicate the presence of an EGFR-independent activation of the mitogen-activated protein kinase/Erk pathway by PGE 2 in NSCLC cells. These findings provide evidence for the possible link between tumor COX-2 overexpression and elevated Erk-mediated cancer cell proliferation and migration. Importantly, these findings suggest that COX-2 overexpression may contribute to EGFR inhibitor resistance in NSCLC. (Cancer Res 2005; 65(14): 6275-81)

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Section: Discussionmentioning

confidence: 74%

Prostaglandin E2 Activates Mitogen-Activated Protein Kinase/Erk Pathway Signaling and Cell Proliferation in Non–Small Cell Lung Cancer Cells in an Epidermal Growth Factor Receptor–Independent Manner

Krysan¹,

Reckamp

Dalwadi³

et al. 2005

Cancer Research

214

163

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“…Furthermore, some different GPCRs, in addition to FPR shown in this study, are also capable of transactivating EGFR, including the receptors for lysophosphatidic acid (LPA; refs. [24][25][26], thrombin (27)(28)(29), endothelin-1 (30-34), carbachol (35)(36)(37), angiotensin (38)(39)(40), bombesin (41,42), and the chemokine SDF1 (CXCL12; ref. 43).…”

Section: Discussionmentioning

confidence: 99%

Transactivation of the Epidermal Growth Factor Receptor by Formylpeptide Receptor Exacerbates the Malignant Behavior of Human Glioblastoma Cells

Huang

Bian

et al. 2007

Cancer Research

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The G protein-coupled formylpeptide receptor (FPR), which mediates leukocyte migration in response to bacterial and host-derived chemotactic peptides, promotes the chemotaxis, survival, and tumorigenesis of highly malignant human glioblastoma cells. Because glioblastoma cells may also express other receptors for growth signals, such as the epidermal growth factor (EGF) receptor (EGFR), we investigated the role of EGFR in the signaling cascade of FPR and how two receptors cross-talk to exacerbate tumor growth. We found that N-formyl-methionyl-leucyl-phenylalanine, an FPR agonist peptide, rapidly induced EGFR phosphorylation at tyrosine residue (Tyr) 992, but not residues 846, 1068, or 1173, in glioblastoma cells, whereas all these residues were phosphorylated after only EGF treatment. The FPR agonist-induced EGFR phosphorylation in tumor cells was dependent on the presence of FPR as well as GAi proteins, and was controlled by Src tyrosine kinase. The transactivation of EGFR contributes to the biological function of FPR in glioblastoma cells because inhibition of EGFR phosphorylation significantly reduced FPR agonist-induced tumor cell chemotaxis and proliferation. Furthermore, depletion of both FPR and EGFR by short interference RNA abolished the tumorigenesis of the glioblastoma cells. Our study indicates that the glioblastoma-promoting activity of FPR is mediated in part by transactivation of EGFR and the cross-talk between two receptors exacerbates the malignant phenotype of tumor cells. Thus, targeting both receptors may yield antiglioblastoma agents superior to those targeting one of them. [Cancer Res 2007;67(12):5906-13]

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“…TFPI2 plays a role in the regulation of plasmin-mediated matrix remodeling (Neaud et al 2004). It is interesting to note that full-length TFPI2 as well as RELN are very-lowdensity lipoprotein receptor (VLDLR) ligands, with an antiproliferative activity (Hembrough et al 2001).…”

Section: Gene Analysismentioning

confidence: 99%

Changes in granulosa cells' gene expression associated with increased oocyte competence in bovine

Nivet¹,

Vigneault²,

Blondin³

et al. 2013

Reproduction

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One of the challenges in mammalian reproduction is to understand the basic physiology of oocyte quality. It is believed that the follicle status is linked to developmental competence of the enclosed oocyte. To explore the link between follicles and competence in cows, previous research at our laboratory has developed an ovarian stimulation protocol that increases and then decreases oocyte quality according to the timing of oocyte recovery post-FSH withdrawal (coasting). Using this protocol, we have obtained the granulosa cells associated with oocytes of different qualities at selected times of coasting. Transcriptome analysis was done with Embryogene microarray slides and validation was performed by real-time PCR. Results show that the major changes in gene expression occurred from 20 to 44 h of coasting, when oocyte quality increases. Secondly, among upregulated genes (20-44 h), 25% were extracellular molecules, highlighting potential granulosa signaling cascades. Principal component analysis identified two patterns: one resembling the competence profile and another associated with follicle growth and atresia. Additionally, three major functional changes were identified: i) the end of follicle growth (BMPR1B, IGF2, and RELN), involving interactions with the extracellular matrix (TFPI2); angiogenesis (NRP1), including early hypoxia, and potentially oxidative stress (GFPT2, TF, and VNN1) and ii) apoptosis (KCNJ8) followed by iii) inflammation (ANKRD1). This unique window of analysis indicates a progressive hypoxia during coasting mixed with an increase in apoptosis and inflammation. Potential signaling pathways leading to competence have been identified and will require downstream testing. This preliminary analysis supports the potential role of the follicular differentiation in oocyte quality both during competence increase and decrease phases.Reproduction (2013) 145 555-565

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Thrombin Up-regulates Tissue Factor Pathway Inhibitor-2 Synthesis through a Cyclooxygenase-2-dependent, Epidermal Growth Factor Receptor-independent Mechanism

Cited by 37 publications

References 41 publications

Prostaglandin E2 Activates Mitogen-Activated Protein Kinase/Erk Pathway Signaling and Cell Proliferation in Non–Small Cell Lung Cancer Cells in an Epidermal Growth Factor Receptor–Independent Manner

Prostaglandin E2 Activates Mitogen-Activated Protein Kinase/Erk Pathway Signaling and Cell Proliferation in Non–Small Cell Lung Cancer Cells in an Epidermal Growth Factor Receptor–Independent Manner

Transactivation of the Epidermal Growth Factor Receptor by Formylpeptide Receptor Exacerbates the Malignant Behavior of Human Glioblastoma Cells

Changes in granulosa cells' gene expression associated with increased oocyte competence in bovine

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