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/OH exchange
activity in Caco-2 cells by phorbol esters is mediated by PKC
Section of Digestive and Liver Diseases, Department of Medicine, University of Illinois at Chicago and West Side Department of Veterans Affairs Medical Center, Chicago, Illinois 60612
The present studies were
undertaken to examine the possible regulation of apical membrane
Cl
/OH exchanger in Caco-2 cells by protein
kinase C (PKC). The effect of the phorbol ester phorbol 12-myristate
13-acetate (PMA), an in vitro PKC agonist, on OH
gradient-driven 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS)-sensitive 36Cl uptake in Caco-2 cells was assessed.
The results demonstrated that PMA decreased apical
Cl/OH exchanger activity via
phosphatidylinositol 3-kinase (PI3-kinase)-mediated activation of
PKC
. The data consistent with these conclusions are as follows:
1) short-term treatment of cells for 1-2 h with PMA
(100 nM) significantly decreased Cl/OH
exchange activity compared with control (4
-PMA); 2)
pretreatment of cells with specific PKC inhibitors chelerythrine
chloride, calphostin C, and GF-109203X completely blocked the
inhibition of Cl/OH exchange activity by
PMA; 3) specific inhibitors for PKC (Ro-318220) but not
PKC (Go-6976) significantly blocked the PMA-mediated inhibition;
4) specific PI3-kinase inhibitors wortmannin and LY-294002 significantly attenuated the inhibitory effect of PMA; and
5) PI3-kinase activators IRS-1 peptide and
phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3] mimicked the effects of PMA.
These findings provide the first evidence for PKC-mediated
inhibition of Cl/OH exchange activity in
Caco-2 cells and indicate the involvement of the PI3-kinase-mediated
pathways in the regulation of Cl absorption in intestinal
epithelial cells.
phosphatidylinositol 3-kinase; protein kinase C epsilon; human intestine; chloride absorption; phorbol 12-myristate 13-acetate
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