Authors: Asha Nair Manuela Simonetti Elsa Fabbretti Andrea Nistri
Publish Date: 2009/12/04
Volume: 30, Issue: 4, Pages: 505-509
Abstract
Cdk5 is an endogenous kinase activated by the neuronalspecific protein p35 and implicated in multiple neuronal functions including modulation of certain pain responses We investigated whether Cdk5 could regulate ATPgated P2X3 receptors that are members of the family of membrane proteins expressed by sensory neurons to transduce nociception in baseline and chronic pain To study the potential P2X3 receptor modulation by Cdk5 we cotransfected rat P2X3 receptors and Cdk5 into HEK cells and observed increased P2X3 receptor serine phosphorylation together with downregulation of receptor currents only when these genes were transfected together with the gene of the Cdk5 activator p35 The changes in receptor responses were limited to depressed current amplitude as desensitization and recovery were not altered Transfection of p35 with P2X3 similarly downregulated receptor responses suggesting that this phenomenon could be observed even with constitutive Cdk5 The present data indicate a novel target to express the action of Cdk5 on membrane proteins involved in pain perception
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