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1 Department of Physiology, Tufts University School of Medicine, Boston, Massachusetts 02111; and 2 Department of Pathology, Albert Einstein College of Medicine, Bronx, New York 10461
Bile secretion in liver is
driven in large part by ATP-binding cassette (ABC)-type proteins that
reside in the canalicular membrane and effect ATP-dependent transport
of bile acids, phospholipids, and non-bile acid organic anions.
Canalicular ABC-type proteins can be classified into two subfamilies
based on membrane topology and sequence identity: MDR1, MDR3, and SPGP
resemble the multidrug resistance (MDR)
P-glycoprotein, whereas MRP2 is similar in structure and
sequence to the multidrug resistance protein MRP1 and transports similar substrates. We now report the isolation of the rMRP3 gene from
rat liver, which codes for a protein 1522 amino acids in length that
exhibits extensive sequence similarity with MRP1 and MRP2. Northern
blot analyses indicate that rMRP3 is expressed in lung and intestine of
Sprague-Dawley rats as well as in liver of Eisai hyperbilirubinemic
rats and TR
mutant rats, which are deficient in MRP2
expression. rMRP3 expression is also transiently induced in liver
shortly after birth and during obstructive cholestasis.
Antibodies raised against MRP3 recognize a polypeptide of
190-200 kDa, which is reduced in size to 155-165 kDa after treatment
with endoglycosidases. Immunoblot analysis and immunoconfocal
microscopy indicate that rMRP3 is present in the canalicular membrane,
suggesting that it may play a role in bile formation.
MRP; bile duct ligation; TR rat; apical
hepatocyte domain; glycoprotein
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