PMID- 10362653
OWN - NLM
STAT- MEDLINE
DCOM- 19990729
LR  - 20181218
IS  - 0002-9513 (Print)
IS  - 0002-9513 (Linking)
VI  - 276
IP  - 6
DP  - 1999 Jun
TI  - MRP3, a new ATP-binding cassette protein localized to the canalicular domain of
      the hepatocyte.
PG  - G1493-500
LID - 10.1152/ajpgi.1999.276.6.G1493 [doi]
AB  - 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.
FAU - Ortiz, D F
AU  - Ortiz DF
AD  - Department of Physiology, Tufts University School of Medicine, Boston,
      Massachusetts 02111, USA. dortiz@opal.tufts.edu
FAU - Li, S
AU  - Li S
FAU - Iyer, R
AU  - Iyer R
FAU - Zhang, X
AU  - Zhang X
FAU - Novikoff, P
AU  - Novikoff P
FAU - Arias, I M
AU  - Arias IM
LA  - eng
GR  - DK-35652/DK/NIDDK NIH HHS/United States
GR  - DK-51005/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Am J Physiol
JT  - The American journal of physiology
JID - 0370511
RN  - 0 (ATP-Binding Cassette Transporters)
RN  - 0 (Multidrug Resistance-Associated Proteins)
RN  - 0 (RNA, Messenger)
RN  - 1YV0492L5Z (multidrug resistance-associated protein 3)
SB  - IM
MH  - ATP-Binding Cassette Transporters/genetics/isolation & purification/*metabolism
MH  - Amino Acid Sequence/genetics
MH  - Animals
MH  - Cholestasis/metabolism
MH  - Hyperbilirubinemia/genetics/metabolism
MH  - Intracellular Membranes/metabolism
MH  - Liver/cytology/*metabolism
MH  - Male
MH  - Molecular Sequence Data
MH  - *Multidrug Resistance-Associated Proteins
MH  - Mutation/physiology
MH  - RNA, Messenger/metabolism
MH  - Rats
MH  - Rats, Mutant Strains
MH  - Rats, Sprague-Dawley
MH  - Tissue Distribution/physiology
EDAT- 1999/06/11 00:00
MHDA- 1999/06/11 00:01
CRDT- 1999/06/11 00:00
PHST- 1999/06/11 00:00 [pubmed]
PHST- 1999/06/11 00:01 [medline]
PHST- 1999/06/11 00:00 [entrez]
AID - 10.1152/ajpgi.1999.276.6.G1493 [doi]
PST - ppublish
SO  - Am J Physiol. 1999 Jun;276(6):G1493-500. doi: 10.1152/ajpgi.1999.276.6.G1493.