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Caffeine activates ryanodine receptor channels in an excised nuclear patch

Caffeine activates ryanodine receptor channels in an excised nuclear patch

Katja Witschas

Visiting Postdoctoral Research Assistant

I am interested in understanding the function of intracellular ion channels in their native membrane environment. These channels such as the ryanodine receptor (RyR) control the process of Ca2+-release from intracellular stores and are crucial to the normal functioning of heart, brain, muscle and many other organs. There are other ion channels present in the ER/SR of most cells such as trimeric intracellular cation channels (TRIC-A and TRIC-B) or chloride channels whose physiological role has not been fully identified. Studying these ion channels in a native membrane will increase our understanding of the channel’s gating mechanism and will finally lead to the development of more effective therapeutic options.


Towards this end, I am using the patch-clamp technique to study intracellular ion channels from the nuclear membrane of cardiomyocytes. The outer nuclear membrane is continuous with the ER, providing a more physiological environment compared to the reconstitution of ion channel proteins into artificial lipid bilayers. Furthermore, I use a mammalian cell line overexpressing these channels in the cell nucleus to elucidate the effect of a highly crowded membrane on ion channel function.

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