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(Received for publication, December 24, 1996, and in revised form, March 6, 1997)
From the Although secretin is known to stimulate ductal
bile secretion by directly interacting with cholangiocytes, the precise
cellular mechanisms accounting for this choleretic effect are unknown. We have previously shown that secretin stimulates exocytosis in cholangiocytes and that these cells transport water mainly via the
water channel aquaporin-1 (AQP1). In this study, we tested the
hypothesis that secretin promotes osmotic water movement in cholangiocytes by inducing the exocytic insertion of AQP1 into plasma
membranes. Exposure of highly purified isolated rat cholangiocytes to
secretin caused significant, dose-dependent increases in
osmotic membrane water permeability (Pf)
(e.g. increased by 60% with 10
Volume 272, Number 20,
Issue of May 16, 1997
pp. 12984-12988
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
EVIDENCE FOR A SECRETIN-INDUCED VESICULAR TRANSLOCATION OF
AQUAPORIN-1
,
,
Center for Basic Research in Digestive
Diseases, Departments of Internal Medicine, Biochemistry, and Molecular
Biology, Mayo Clinic and Foundation, Mayo Medical School, Rochester,
Minnesota 55905 and the § Departments of Biological
Chemistry and Medicine, The Johns Hopkins University School of
Medicine, Baltimore, Maryland 21205
7
M secretin), which was reversibly inhibited by the water
channel blocker HgCl2. Immunoblotting analysis of
cholangiocyte membrane fractions showed that secretin caused up to a
3-fold increase in the amount of AQP1 in plasma membranes and a
proportional decrease in the amount of the water channel in microsomes,
suggesting a secretin-induced redistribution of AQP1 from intracellular
to plasma membranes. Both the secretin-induced increase in
cholangiocyte Pf and AQP1 redistribution were
blocked by two perturbations that inhibit secretin-stimulated
exocytosis in cholangiocytes, i.e. treatment with
colchicine and exposure at low temperatures (20 and 4 °C). Our
results demonstrate that secretin increases AQP1-mediated
Pf in cholangiocytes. Moreover, our studies implicate the microtubule-dependent vesicular translocation
of AQP1 water channels to the plasma membrane, a mechanism that appears to be essential for secretin-induced ductal bile secretion and suggests
that AQP1 can be regulated by membrane trafficking.
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