CFTR - "Effect of internal F- on activation of Cystic Fibrosis Transmembrane Conductance (CFTR) regulator by forskolin"

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The aim of this study was to investigate the effect of internal F- on the activation of the cystic fibrosis transmembrane conductance regulator (CFTR) by forskolin in the whole cell patch clamp configuration. Experiments were conducted with Nanion’s fully automated patch clamp device, the Patchliner. The CFTR is a phosphorylation regulated Cl- channel. In order for the channel to be active it needs to be phosphorylated. Subsequent binding of ATP to intracellular nucleotide binding sites controls the opening and closing of the channel (Zhou et al., 2006). Our standard internal solutions contain F-. Regulation of many ion channels does not seem to be affected by the presence of F- in the intracellular solution, however, that is not true for every ion channel. F-, for example, has been shown to activate adenylate cyclase (Eckstein et al., 1979, Insel and Ostrom, 2003). Forskolin – a commonly used CFTR activator – is known to activate CFTR through activation of adenylate cyclase. This leads to phosphorylation (and hence activation) of CFTR by protein kinase A (PKA). It would be interesting to see if F- can be used as a substitute for forskolin in its role as a CFTR activator. In this report we summarize some preliminary measurements of CFTR currents in the whole cell patch clamp configuration with the Patchliner to obtain insight into the effects of F- on CFTR currents.

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