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and PKC
on basolateral membrane
dynamics in intestinal epithelia
1 Department of Surgery, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267; and 2 Department of Medicine, McMaster University, Hamilton, Ontario, Canada L8S 4L8
PKC is a critical effector of plasma
membrane dynamics, yet the mechanism and isoform-specific role of PKC
are poorly understood. We recently showed that the phorbol ester PMA
(100 nM) induces prompt activation of the novel isoform PKC
followed
by late activation of the conventional isoform PKC
in T84 intestinal
epithelia. PMA also elicited biphasic effects on endocytosis,
characterized by an initial stimulatory phase followed by an inhibitory
phase. Activation of PKC was shown to be responsible for stimulation of basolateral endocytosis, but the role of PKC was not defined. Here, we used detailed time-course analysis as well as selective activators and inhibitors of PKC isoforms to infer the action of PKC
on basolateral endocytosis. Inhibition of PKC by the selective
conventional PKC inhibitor Gö-6976 (5 µM) completely blocked
the late inhibitory phase and markedly prolonged the stimulatory phase
of endocytosis measured by FITC-dextran uptake. The PKC-selective agonist carbachol (100 µM) induced prolonged stimulation of
endocytosis devoid of an inhibitory phase. Actin disassembly caused by
PMA was completely blocked by Gö-6850 but not by Gö-6976,
implicating PKC as the key isoform responsible for actin disruption.
The Ca2+ agonist thapsigargin (5 µM) induced early
activation of PKC when added simultaneously with PMA. This early
activation of PKC blocked the ability of PMA to remodel basolateral
F-actin and abolished the stimulatory phase of basolateral endocytosis.
Activation of PKC stabilizes F-actin and thereby opposes the effect
of PKC on membrane remodeling in T84 cells.
protein kinase C isoforms; cytoskeleton; intestinal mucosa; calcium
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