Product Reference
Glycine receptor internalization by protein kinases activation.
| |
|
| Author |
Miguel Ángel Velázquez-Flores,Rocío Salceda,Miguel Ãngel Velázquez-Flores,RocÃo Salceda |
| Citation Information |
Synapse (New York, N.Y.), 65: (2011) |
| Keywords |
Animals,Cyclic AMP-Dependent Protein Kinases,Endocytosis,Enzyme Activation,Female,Male,Phosphorylation,Protein Binding,Protein Kinase C,Radioligand Assay,Rats,Rats, Long-Evans,Receptors, Glycine,Retina |
| Related Products |
05-1000 |
| Pub Med ID |
21656573 |
| |
|
Abstract
Although glycine-induced currents in the central nervous system have been proven to be modulated by protein kinases A (PKA) and C (PKC), the mechanism is not well understood. In order to better comprehend the mechanism involved in this phenomenon, we tested the PKA and PKC activation effect on the specific [(3) H]glycine and [(3) H]strychnine binding to postsynaptic glycine receptor (GlyR) in intact rat retina. The specific binding constituted about 20% of the total radioligand binding. Kinetic analysis of the specific binding exhibited a sigmoidal behavior with three glycine and two strychnine binding sites and affinities of 212 nM for [(3) H]glycine and 50 nM for [(3) H]strychnine. Specific radioligand binding was decreased (60-85%) by PKA and PKC activation, an effect that was blocked by specific kinases inhibitors, as well as by cytochalasin D. GlyR expressed in the plasma membrane decreased about 50% in response to kinases activation, which was consistent with an increase of the receptor in the microsomal fraction when PKA was activated. Moreover, immunoprecipitation studies indicated that these kinases lead to a time-dependent receptor phosphorylation. Our results suggest that in retina, GlyR is cross-regulated by G protein-coupled receptors, activating PKA and PKC.
