Phosphorylation at Ser 727 Increases STAT3 Interaction with PKC<i>ε</i> Regulating Neuron–Glia Crosstalk via IL-6-Mediated Hyperalgesia In Vivo and In Vitro

<div>Interaction between PKC<i>ε</i> and STAT3<sup>Ser727</sup> in nociceptive regulation during inflammatory pain. PKC<i>ε</i> and STAT3 engaged with IL-6-mediated neuronal and glial cell crosstalk during inflammatory nociceptive transmission. Under inflammatory conditions, upregulated PKC<i>ε</i> and STAT3<sup>Ser727</sup> phosphorylation interacted in the spinal cord and subsequently increased IL-6 promoter activity that manifested as IL-6 cytokine-mediated inflammatory pain. T-5224, Mino, and LAA inhibited the PKC<i>ε</i>/STAT3/IL-6 signaling pathway and the activation of neurons, astrocytes, and glial cells during inflammatory pain development. IL-6: interleukin-6; LAA: L-2-aminoadipic acid; Mino: minocycline; PKC<i>ε</i>: protein kinase C epsilon; STAT3: signal transducer and activator of transcription 3.</div>

Mediators of Inflammation

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Figure 8

Figure 8: Phosphorylation at Ser 727 Increases STAT3 Interaction with PKC<i>ε</i> Regulating Neuron–Glia Crosstalk via IL-6-Mediated Hyperalgesia In Vivo and In Vitro 

Figure 8 | Phosphorylation at Ser 727 Increases STAT3 Interaction with PKCε Regulating Neuron–Glia Crosstalk via IL-6-Mediated Hyperalgesia In Vivo and In Vitro 