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Down‐Regulation of c‐<i>neu</i> Receptors by Nerve Growth Factor in PC12 Cells
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1995
Year
Synaptic TransmissionImmunologyNeurotransmissionPeripheral NerveCellular NeurobiologySynaptic SignalingCellular PhysiologySocial SciencesPc12 CellsSignaling PathwayReceptor Tyrosine KinaseNeuroimmunologyCell SignalingMolecular NeuroscienceMolecular PhysiologyP185c-neu ReceptorsTyrosine ResiduesG Protein-coupled ReceptorReceptor (Biochemistry)Nervous SystemPharmacologyCell BiologySignal TransductionNerve Growth FactorNeuropeptide ReceptorNeuroscienceMolecular NeurobiologyMedicine
A small number of p185c-neu receptors have been found on PC12 cells. These receptors show some basal phosphorylation in quiescent cells. When the cells are treated with nerve growth factor (NGF) for a short time, some increase in phosphorylation is seen, mainly on serine and threonine residues, and this is accompanied by a slight shift in the apparent molecular weight. Epidermal growth factor (EGF) also increases the phosphorylation of p185c-neu, in this case on tyrosine residues. Neither heregulin-beta 1 nor gp30 stimulates the tyrosine phosphorylation of p185c-neu, and neither has a proliferative effect on the cells. Treatment of the cells with NGF for 5 days produces a 70-80% reduction in the number of p185c-neu receptors. This down-regulation does not occur when PC12nnr5 cells, which lack the high-affinity NGF receptor, p140trk, are treated with NGF. The level of p185c-neu mRNA is not altered by NGF treatment, suggesting that the down-regulation is due to either a translational or a posttranslational alteration.