• Port-a-Patch

    Smallest patch clamp setup in the world
  • Port-a-Patch

    Easy to learn - ideal for teaching
  • Port-a-Patch

    Records from cells, organelles and bilayers
  • Port-a-Patch

    First planar patch clamp device on the market
  • Port-a-Patch

    Ideal for internal solution exchange applications

2012 - Interleukin-1R3 mediates interleukin-1–induced potassium current increase through fast activation of Akt kinase

icon pap   Port-a-Patch publication in Proceedings of the National Academy of Sciences of the Unites States of America (2012)

Authors: 
Qian J., Zhu L., Li Q., Belevych N., Chen Q., Zhao F., Herness S., Quan N.

 

Journal: 
Proc Natl Acad Sci U S A. (2012) 109(30):12189-94


Abstract: 

Inflammatory cytokine interleukin-1 (IL-1) performs multiple functions in the central nervous system. The type 1 IL-1 receptor (IL-1R1) and the IL-1 receptor accessory protein (IL-1RAcP) form a functional IL-1 receptor complex that is thought to mediate most, if not all, IL-1–induced effects. Several recent studies, however, suggest the existence of a heretofore-unidentified receptor for IL-1. In this study, we report that the IL-1R1 gene contains an internal promoter that drives the transcription of a shortened IL-1R1 mRNA. This mRNA is the template for a unique IL-1R protein that is identical to IL-1R1 at the C terminus, but with a shorter extracellular domain at the N terminus. We have termed this molecule IL-1R3. The mRNA and protein for IL-1R3 are expressed in normal and two strains of commercially available IL-1R1 knockout mice. Western blot analysis shows IL-1R3 is preferentially expressed in neural tissues. Furthermore, IL-1β binds specifically to IL-1R3 when it is complexed with the newly discovered alternative IL-1 receptor accessory protein, IL-1RAcPb. Stimulation of neurons expressing both IL-1R3 and IL-1RAcPb with IL-1β causes fast activation of the Akt kinase, which leads to an increase in voltage-gated potassium current. These results demonstrate that IL-1R3/IL-1RAcPb complex mediates a unique subset of IL-1 activity that accounts for many previously unexplained IL-1 effects in the central nervous system.


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