epidermal-growth-factor has been researched along with 2-aminoethoxydiphenyl-borate* in 2 studies
2 other study(ies) available for epidermal-growth-factor and 2-aminoethoxydiphenyl-borate
| Article | Year |
|---|---|
The human transient receptor potential vanilloid 3 channel is sensitized via the ERK pathway.
The transient receptor potential vanilloid 3 (TRPV3) channel is a Ca Topics: Boron Compounds; Cell Line, Transformed; Cymenes; Epidermal Growth Factor; ErbB Receptors; Green Fluorescent Proteins; HEK293 Cells; Humans; Keratinocytes; MAP Kinase Signaling System; Membrane Transport Modulators; Mitogen-Activated Protein Kinase 3; Monoterpenes; Mutagenesis, Site-Directed; Mutation; Patch-Clamp Techniques; Phosphorylation; Protein Interaction Domains and Motifs; Protein Processing, Post-Translational; Recombinant Proteins; Threonine; TRPV Cation Channels; Up-Regulation | 2017 |
Activation of H2O2-induced VSOR Cl- currents in HTC cells require phospholipase Cgamma1 phosphorylation and Ca2+ mobilisation.
Volume-sensitive outwardly rectifying (VSOR) Cl(-) channels participate in several physiological processes such as regulatory volume decrease, cell cycle regulation, proliferation and apoptosis. Recent evidence points to a significant role of hydrogen peroxide (H(2)O(2)) in VSOR Cl(-) channel activation. The aim of this study was to determine the signalling pathways responsible for H(2)O(2)-induced VSOR Cl(-) channel activation. In rat hepatoma (HTC) cells, H(2)O(2) elicited a transient increase in tyrosine phosphorylation of phospholipase Cgamma1 (PLCgamma1) that was blocked by PP2, a Src-family protein kinases inhibitor. Also, H(2)O(2) triggered an increase in cytosolic [Ca(2+)] that paralleled the time course of PLCgamma1 phosphorylation. The H(2)O(2)-induced [Ca(2+)](i) rise was prevented by the generic phospholipase C (PLC) inhibitor U73122 and the inositol 1,4,5-trisphosphate-receptor (IP(3)R) blocker 2-APB. In line with these results, manoeuvres that prevented PLCgamma1 activation and/or [Ca(2+)](i) rise, abolished H(2)O(2)-induced VSOR Cl(-) currents. Furthermore, in cells that overexpress a phosphorylation-defective dominant mutant of PLCgamma1, H(2)O(2) did not induce activation of VSOR Cl(-) currents. All these H(2)O(2)-induced effects were independent of extracellular Ca(2+). Our findings suggest that activation of PLCgamma1 and subsequent Ca(2+)(i) mobilisation mediate H(2)O(2)-induced VSOR Cl(-) currents, indicating that H(2)O(2) operates via redox-sensitive signalling pathways akin to those activated by osmotic challenges. Topics: Animals; Boron Compounds; Calcium Signaling; Cell Line, Tumor; Chloride Channels; Enzyme Activation; Epidermal Growth Factor; Estrenes; Genes, Dominant; Hydrogen Peroxide; Ion Channel Gating; Liver Neoplasms, Experimental; Mutant Proteins; Phospholipase C gamma; Phosphorylation; Pyrimidines; Pyrrolidinones; Rats; src-Family Kinases | 2007 |