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J. Biol. Chem., Vol. 276, Issue 10, 7218-7224, March 9, 2001
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From the Tufts University School of Medicine, Department of
Physiology, Boston, Massachusetts 02111
ABC transporter trafficking in rat
liver induced by cAMP or taurocholate and
[35S]methionine metabolic labeling followed by
subcellular fractionation were used to identify and characterize
intrahepatic pools of ABC transporters. ABC transporter trafficking
induced by cAMP or taurocholate is a physiologic response to a temporal
demand for increased bile secretion. Administration of cAMP or
taurocholate to rats increased amounts of SPGP, MDR1, and MDR2 in the
bile canalicular membrane by 3-fold; these effects abated after 6 h and were insensitive to prior treatment of rats with cycloheximide.
Half-lives of ABC transporters were 5 days, which suggests cycling of
ABC transporters between canalicular membrane and intrahepatic sites
before degradation. In vivo [35S]methionine
labeling of rats followed by immunoprecipitation of (sister of
P-glycoprotein) (SPGP) from subcellular liver fractions revealed a
steady state distribution after 20 h of SPGP between canalicular
membrane and a combined endosomal fraction. After mobilization of
transporters from intrahepatic sites with cAMP or taurocholate, a
significant increase in the amount of ABC transporters in canalicular
membrane vesicles was observed, whereas the decrease in the combined
endosomal fraction remained below detection limits in Western blots.
This observation is in accordance with relatively large intracellular
ABC transporter pools compared with the amount present in the bile
canalicular membrane. Furthermore, trafficking of newly synthesized
SPGP through intrahepatic sites was accelerated by additional
administration of cAMP but not by taurocholate, indicating two distinct
intrahepatic pools. Our data indicate that ABC transporters cycle
between the bile canaliculus and at least two large intrahepatic ABC
transporter pools, one of which is mobilized to the canalicular
membrane by cAMP and the other, by taurocholate. In parallel to
regulation of other membrane transporters, we propose that the
"cAMP-pool" in hepatocytes corresponds to a recycling
endosome, whereas recruitment from the "taurocholate-pool" involves
a hepatocyte-specific mechanism.
Transporters on Demand
INTRAHEPATIC POOLS OF CANALICULAR ATP BINDING CASSETTE
TRANSPORTERS IN RAT LIVER*
,
*
This work was supported by Deutsche Forschungsgemeinschaft
Research Grant Ki 640 (to H. K.) and by National Institutes of Health
Grants DK35652 (NIDDK) and 30DK34928 (Digestive Disease Center, NIDDK)
(to I. M. A.).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Max-Planck-Institut für molekulare
Physiologie, Otto-Hahn-Str. 11, 44227 Dortmund, Germany.
§
To whom correspondence should be addressed: Tufts University School
of Medicine, Dept. of Physiology, 136 Harrison Ave., Boston, MA 02111. Tel.: 617-636-6739; Fax: 617-636-0445; E-mail: irwin. arias{at}tufts.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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