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      5-HT(1A) receptors transactivate the platelet-derived growth factor receptor type beta in neuronal cells.

      Cellular Signalling
      Animals, Calcium, metabolism, Calcium Signaling, Cells, Cultured, Humans, Mice, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinase 3, Neurons, cytology, Pertussis Toxin, pharmacology, Phosphorylation, drug effects, Proto-Oncogene Proteins c-sis, Receptor, Platelet-Derived Growth Factor beta, genetics, Receptor, Serotonin, 5-HT1A, Serotonin, Transcriptional Activation, Type C Phospholipases, src-Family Kinases

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          Abstract

          In the absence of ligand, certain growth factor receptors can be activated via G-protein coupled receptor (GPCR) activation in a process termed transactivation. Serotonin (5-HT) receptors can transactivate platelet-derived growth factor (PDGF) β receptors in smooth muscle cells, but it is not known if similar pathways occur in neuronal cells. Here we show that 5-HT can transiently increase the phosphorylation of PDGFβ receptors through 5-HT(1A) receptors in a time- and dose-dependent manner in SH-SY5Y neuroblastoma cells. 5-HT also transactivates PDGFβ receptors in primary cortical neurons. This transactivation pathway is pertussis-toxin sensitive and Src tyrosine kinase-dependent. This pathway is also dependent on phospholipase C activity and intracellular calcium signaling. Several studies involving PDGFβ receptor transactivation by GPCRs have also demonstrated a PDGFβ receptor-dependent increase in the phosphorylation of ERK1/2. Yet in SH-SY5Y cells, 5-HT treatment causes a PDGFβ receptor-independent increase in ERK1/2 phosphorylation. This crosstalk between 5-HT and PDGFβ receptors identifies a potentially important signaling link between the serotonergic system and growth factor signaling in neurons. Copyright © 2012 Elsevier Inc. All rights reserved.

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