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transport
proteins by PKC in Calu-3 cells
The Cystic Fibrosis Center, Departments of Pediatrics and Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio 44106-4948
Cl
transport proteins expressed
in a Calu-3 airway epithelial cell line were differentiated by function
and regulation by protein kinase C (PKC) isotypes. mRNA expression of
Cl transporters was semiquantitated by RT-PCR after
transfection with a sense or antisense oligonucleotide to the PKC
isotypes that modulate the activity of the cystic fibrosis
transmembrane conductance regulator [CFTR (PKC-
)] or of the
Na/K/2Cl (NKCC1) cotransporter (PKC-
). Expression of NKCC1 and CFTR
mRNAs and proteins was independent of antisense oligonucleotide
treatment. Transport function was measured in cell monolayers grown on
a plastic surface or on filter inserts. With both culture
methods, the antisense oligonucleotide to PKC- decreased the
amount of PKC- and reduced cAMP-dependent activation of CFTR but not
1-adrenergic activation of NKCC1. The antisense
oligonucleotide to PKC- did not affect CFTR function but did block
1-adrenergic activation of NKCC1 and reduce PKC-
mass. These results provide the first evidence for mRNA and protein
expression of NKCC1 in Calu-3 cells and establish the differential
regulation of CFTR and NKCC1 function by specific PKC isotypes at a
site distal to mRNA expression and translation in airway epithelial cells.
sodium-potassium-2chloride cotransport; antisense oligonucleotide; permeabilized monolayer; reverse transcriptase-polymerase chain
reaction; actin; -adrenergic activation; methoxamine; phorbol ester; cystic fibrosis transmembrane conductance regulator; protein kinase C
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