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alters cAMP-dependent
stimulation of CFTR in Calu-3 cells
Cystic Fibrosis Center and Departments of Pediatrics and Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio 44106
Protein kinase C
(PKC) regulates cystic fibrosis transmembrane conductance regulator
(CFTR) channel activity but the PKC signaling mechanism is not yet
known. The goal of these studies was to identify PKC isotype(s)
required for control of CFTR function. CFTR activity was measured as
36Cl efflux in a Chinese hamster
ovary cell line stably expressing wild-type CFTR (CHO-wtCFTR) and in a
Calu-3 cell line. Chelerythrine, a PKC inhibitor, delayed increased
CFTR activity induced with phorbol 12-myristate 13-acetate or with the
cAMP-generating agents (
)-epinephrine or forskolin plus
8-(4-chlorophenylthio)adenosine 3',5'- cyclic
monophosphate. Immunoblot analysis of Calu-3 cells revealed that
PKC-
, -
II, -
, -
, and
-
were expressed in confluent cell cultures. Pretreatment of cell
monolayers with Lipofectin plus antisense oligonucleotide to PKC-
for 48 h prevented stimulation of CFTR with ()-epinephrine,
reduced PKC- activity in unstimulated cells by 52.1%, and decreased
PKC- mass by 76.1% but did not affect hormone-activated protein
kinase A activity. Sense oligonucleotide to PKC- and antisense
oligonucleotide to PKC- and - did not alter
()-epinephrine-stimulated CFTR activity. These results demonstrate the selective regulation of CFTR function by constitutively active PKC-.
Chinese hamster ovary cell line; chelerythrine; chloride efflux; epinephrine; protein kinase A; protein kinase C; cystic fibrosis transmembrane conductance regulator
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