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Hydrogen sulfide (H 2 S) has been recognized as a signalling molecule which affects the activity of ion channels and transporters in epithelial cells. The cystic fibrosis transmembrane conductance regulator (CFTR) is an epithelial anion channel and a key regulator of electrolyte and fluid homeostasis. In this study, we investigated the regulation of CFTR by H 2 S. Human CFTR was heterologously expressed in  Xenopus  oocytes and its activity was electrophysiologically measured by microelectrode recordings. The H 2 S-forming sulphur salt Na 2 S as well as the slow-releasing H 2 S-liberating compound GYY4137 increased transmembrane currents of CFTR-expressing oocytes. Na 2 S had no effect on native, non-injected oocytes. The effect of Na 2 S was blocked by the CFTR inhibitor CFTR_inh172, the adenylyl cyclase inhibitor MDL 12330A, and the protein kinase A antagonist cAMPS-Rp. Na 2 S potentiated CFTR stimulation by forskolin, but not that by IBMX. Na 2 S enhanced CFTR stimulation by membrane-permeable 8Br-cAMP under inhibition of adenylyl cyclase-mediated cAMP production by MDL 12330A. These data indicate that H 2 S activates CFTR in  Xenopus  oocytes by inhibiting phosphodiesterase activity and subsequent stimulation of CFTR by cAMP-dependent protein kinase A. In epithelia, an increased CFTR activity may correspond to a pro-secretory response to H 2 S which may be endogenously produced by the epithelium or H 2 S-generating microflora.

Hydrogen sulfide stimulates CFTR in Xenopus oocytes by activation of the cAMP/PKA signalling axis