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1 Renal Unit, Massachusetts General Hospital East, Charlestown 02129; 2 Department of Medicine, Harvard Medical School, and 3 Experimental Medicine, Brigham and Women's Hospital, Boston 02115; and 4 Renal Section, Boston Medical Center, Boston, Massachusetts 02118
Previous studies
have indicated a role of the actin cytoskeleton in the regulation of
the cystic fibrosis transmembrane conductance regulator (CFTR) ion
channel. However, the exact molecular nature of this regulation is
still largely unknown. In this report human epithelial CFTR was
expressed in human melanoma cells genetically devoid of the filamin
homologue actin-cross-linking protein ABP-280 [ABP(
)]. cAMP stimulation of ABP() cells or
cells genetically rescued with ABP-280 cDNA [ABP(+)] was
without effect on whole cell Cl
currents. In
ABP() cells expressing CFTR, cAMP was also without effect on
Cl conductance. In contrast, cAMP induced a 10-fold
increase in the diphenylamine-2-carboxylate (DPC)-sensitive whole cell
Cl currents of ABP(+)/CFTR(+) cells. Further, in
cells expressing both CFTR and a truncated form of ABP-280 unable to
cross-link actin filaments, cAMP was also without effect on CFTR
activation. Dialysis of ABP-280 or filamin through the patch pipette,
however, resulted in a DPC-inhibitable increase in the whole cell
currents of ABP()/CFTR(+) cells. At the single-channel level,
protein kinase A plus ATP activated single Cl
channels only in excised patches from ABP(+)/CFTR(+) cells.
Furthermore, filamin alone also induced Cl channel
activity in excised patches of ABP()/CFTR(+) cells. The present
data indicate that an organized actin cytoskeleton is required for
cAMP-dependent activation of CFTR.
ABP-280; cystic fibrosis transmembrane conductance regulator; actin cytoskeleton; adenosine 3',5'-cyclic monophosphate
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