cAMP-independent activation of CFTR Cl channels by the tyrosine kinase inhibitor genistein.

@article{Illek1995cAMPindependentAO,
  title={cAMP-independent activation of CFTR Cl channels by the tyrosine kinase inhibitor genistein.},
  author={Beate Illek and Horst Fischer and Gabriela F. dos Santos and Jonathan H. Widdicombe and Terry E. Machen and William W. Reenstra},
  journal={The American journal of physiology},
  year={1995},
  volume={268 4 Pt 1},
  pages={C886-93}
}
Genistein, a protein tyrosine kinase inhibitor, activates the cystic fibrosis transmembrane conductance regulator (CFTR) in transfected NIH-3T3 fibroblasts that express the CFTR (3T3-CFTR). CFTR activity was assayed by 125I efflux and by patch clamping in the cell-attached mode. Both forskolin and genistein stimulated 125I efflux and activated a 9-10 pS anion channel in 3T3-CFTR cells but failed to activate 125I efflux in mock-transfected NIH-3T3 cells. Genistein, unlike forskolin and 3… CONTINUE READING

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