PMID- 10644574
OWN - NLM
STAT- MEDLINE
DCOM- 20000616
LR  - 20171213
IS  - 0193-1857 (Print)
IS  - 0193-1857 (Linking)
VI  - 278
IP  - 1
DP  - 2000 Jan
TI  - A novel human organic anion transporting polypeptide localized to the basolateral
      hepatocyte membrane.
PG  - G156-64
AB  - We cloned and expressed a new organic anion transporting polypeptide (OATP),
      termed human OATP2, (OATP-C, LST-1; symbol SLC21A6), involved in the uptake of
      various lipophilic anions into human liver. The cDNA encoding OATP2 comprised
      2073 base pairs, corresponding to a protein of 691 amino acids, which were 44%
      identical to the known human OATP. An antibody directed against the carboxy
      terminus localized OATP2 to the basolateral membrane of human hepatocytes.
      Northern blot analysis indicated a strong expression of OATP2 only in human
      liver. Transport mediated by recombinant OATP2 and its localization were studied 
      in stably transfected Madin-Darby canine kidney strain II (MDCKII) and HEK293
      cells. Confocal microscopy localized recombinant OATP2 protein to the lateral
      membrane of MDCKII cells. Substrates included 17beta-glucuronosyl estradiol,
      monoglucuronosyl bilirubin, dehydroepiandrosterone sulfate, and cholyltaurine.
      17beta-Glucuronosyl estradiol was a preferred substrate, with a Michaelis-Menten 
      constant value of 8.2 microM; its uptake was Na(+) independent and was inhibited 
      by sulfobromophthalein, with a inhibition constant value of 44 nM. Our results
      indicate that OATP2 is important for the uptake of organic anions, including
      bilirubin conjugates and sulfobromophthalein, in human liver.
FAU - Konig, J
AU  - Konig J
AD  - Division of Tumor Biochemistry, Deutsches Krebsforschungszentrum, D-69120
      Heidelberg, Germany. j.koenig@dkfz-heidelberg.de
FAU - Cui, Y
AU  - Cui Y
FAU - Nies, A T
AU  - Nies AT
FAU - Keppler, D
AU  - Keppler D
LA  - eng
SI  - GENBANK/H62893
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Am J Physiol Gastrointest Liver Physiol
JT  - American journal of physiology. Gastrointestinal and liver physiology
JID - 100901227
RN  - 0 (17-glucuronosylestradiol)
RN  - 0 (Anion Transport Proteins)
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (Glucuronates)
RN  - 0 (Recombinant Proteins)
RN  - 4TI98Z838E (Estradiol)
SB  - IM
MH  - Amino Acid Sequence/genetics
MH  - Animals
MH  - Anion Transport Proteins
MH  - Blotting, Northern
MH  - Carrier Proteins/genetics/*metabolism/physiology
MH  - Cell Line
MH  - Cloning, Molecular
MH  - DNA, Complementary/genetics
MH  - Dogs
MH  - Estradiol/analogs & derivatives/pharmacokinetics
MH  - Fluorescent Antibody Technique
MH  - Glucuronates/pharmacokinetics
MH  - Humans
MH  - Intracellular Membranes/*metabolism
MH  - Liver/cytology/*metabolism
MH  - Molecular Sequence Data
MH  - Recombinant Proteins/metabolism
MH  - Tissue Distribution
EDAT- 2000/01/25 09:00
MHDA- 2000/06/24 11:00
CRDT- 2000/01/25 09:00
PHST- 2000/01/25 09:00 [pubmed]
PHST- 2000/06/24 11:00 [medline]
PHST- 2000/01/25 09:00 [entrez]
AID - 10.1152/ajpgi.2000.278.1.G156 [doi]
PST - ppublish
SO  - Am J Physiol Gastrointest Liver Physiol. 2000 Jan;278(1):G156-64. doi:
      10.1152/ajpgi.2000.278.1.G156.