neuromedin-b and lysophosphatidic-acid

neuromedin-b has been researched along with lysophosphatidic-acid* in 1 studies

Other Studies

1 other study(ies) available for neuromedin-b and lysophosphatidic-acid

Article	Year
G-protein coupled receptor agonists mediate Neu1 sialidase and matrix metalloproteinase-9 cross-talk to induce transactivation of TOLL-like receptors and cellular signaling. Cellular signalling, 2012, Volume: 24, Issue:11 The mechanism(s) behind GPCR transactivation of TLR receptors independent of TLR ligands is unknown. Here, GPCR agonists bombesin, bradykinin, lysophosphatidic acid (LPA), cholesterol, angiotensin-1 and -2, but not thrombin induce Neu1 activity in live macrophage cell lines and primary bone marrow macrophage cells from wild-type (WT) mice but not from Neu1-deficient mice. Using immunocytochemistry and NFκB-dependent secretory alkaline phosphatase (SEAP) analyses, bombesin induced NFκB activation in BMC-2 and RAW-blue macrophage cells, which was inhibited by MyD88 homodimerization inhibitor, Tamiflu, galardin, piperazine and anti-MMP-9 antibody. Bombesin receptor, neuromedin B (NMBR), forms a complex with TLR4 and MMP9. Silencing MMP9 mRNA using siRNA transfection of RAW-blue macrophage cells markedly reduced Neu1 activity associated with bombesin-, bradykinin- and LPA-treated cells to the untreated controls. These findings uncover a molecular organizational GPCR signaling platform to potentiate Neu1 and MMP-9 cross-talk on the cell surface that is essential for the transactivation of TLR receptors and subsequent cellular signaling. Topics: Animals; Antiviral Agents; Bombesin; Bradykinin; Cells, Cultured; Lysophospholipids; Matrix Metalloproteinase 9; Mice; Myeloid Differentiation Factor 88; Neuraminidase; Neurokinin B; NF-kappa B; Oseltamivir; Protein Binding; Receptors, Bombesin; Receptors, G-Protein-Coupled; RNA Interference; RNA, Small Interfering; Signal Transduction; Toll-Like Receptors; Transcriptional Activation; Vasodilator Agents	2012

Article

Year

G-protein coupled receptor agonists mediate Neu1 sialidase and matrix metalloproteinase-9 cross-talk to induce transactivation of TOLL-like receptors and cellular signaling.

Cellular signalling, 2012, Volume: 24, Issue:11

The mechanism(s) behind GPCR transactivation of TLR receptors independent of TLR ligands is unknown. Here, GPCR agonists bombesin, bradykinin, lysophosphatidic acid (LPA), cholesterol, angiotensin-1 and -2, but not thrombin induce Neu1 activity in live macrophage cell lines and primary bone marrow macrophage cells from wild-type (WT) mice but not from Neu1-deficient mice. Using immunocytochemistry and NFκB-dependent secretory alkaline phosphatase (SEAP) analyses, bombesin induced NFκB activation in BMC-2 and RAW-blue macrophage cells, which was inhibited by MyD88 homodimerization inhibitor, Tamiflu, galardin, piperazine and anti-MMP-9 antibody. Bombesin receptor, neuromedin B (NMBR), forms a complex with TLR4 and MMP9. Silencing MMP9 mRNA using siRNA transfection of RAW-blue macrophage cells markedly reduced Neu1 activity associated with bombesin-, bradykinin- and LPA-treated cells to the untreated controls. These findings uncover a molecular organizational GPCR signaling platform to potentiate Neu1 and MMP-9 cross-talk on the cell surface that is essential for the transactivation of TLR receptors and subsequent cellular signaling.

Topics: Animals; Antiviral Agents; Bombesin; Bradykinin; Cells, Cultured; Lysophospholipids; Matrix Metalloproteinase 9; Mice; Myeloid Differentiation Factor 88; Neuraminidase; Neurokinin B; NF-kappa B; Oseltamivir; Protein Binding; Receptors, Bombesin; Receptors, G-Protein-Coupled; RNA Interference; RNA, Small Interfering; Signal Transduction; Toll-Like Receptors; Transcriptional Activation; Vasodilator Agents

2012