28 research outputs found

    Myosin X is Recruited to Focal Adhesion and Induces Filopodia Initiation

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    Ī±1A-Adrenergic Receptor Induces Activation of Extracellular Signal-Regulated Kinase 1/2 through Endocytic Pathway

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    G protein-coupled receptors (GPCRs) activate mitogen-activated protein kinases through a number of distinct pathways in cells. Increasing evidence has suggested that endosomal signaling has an important role in receptor signal transduction. Here we investigated the involvement of endocytosis in Ī±1A-adrenergic receptor (Ī±1A-AR)-induced activation of extracellular signal-regulated kinase 1/2 (ERK1/2). Agonist-mediated endocytic traffic of Ī±1A-AR was assessed by real-time imaging of living, stably transfected human embryonic kidney 293A cells (HEK-293A). Ī±1A-AR was internalized dynamically in cells with agonist stimulation, and actin filaments regulated the initial trafficking of Ī±1A-AR. Ī±1A-AR-induced activation of ERK1/2 but not p38 MAPK was sensitive to disruption of endocytosis, as demonstrated by 4Ā°C chilling, dynamin mutation and treatment with cytochalasin D (actin depolymerizing agent). Activation of protein kinase C (PKC) and C-Raf by Ī±1A-AR was not affected by 4Ā°C chilling or cytochalasin D treatment. U73122 (a phospholipase C [PLC] inhibitor) and Ro 31ā€“8220 (a PKC inhibitor) inhibited Ī±1B-AR- but not Ī±1A-AR-induced ERK1/2 activation. These data suggest that the endocytic pathway is involved in Ī±1A-AR-induced ERK1/2 activation, which is independent of Gq/PLC/PKC signaling

    Blood Lead Levels of Children and Its Trend in China

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