PMID- 10484490
OWN - NLM
STAT- MEDLINE
DCOM- 19991018
LR  - 20181010
IS  - 0002-9513 (Print)
IS  - 0002-9513 (Linking)
VI  - 277
IP  - 3
DP  - 1999 Sep
TI  - Cloning of mouse prostaglandin transporter PGT cDNA: species-specific substrate
      affinities.
PG  - R734-41
LID - 10.1152/ajpregu.1999.277.3.R734 [doi]
AB  - We recently identified and/or cloned the PG transporter PGT in the rat (rPGT)
      (Kanai, N., R. Lu, J. A. Satriano, Y. Bao, A. W. Wolkoff, and V. L. Schuster,
      Science 268: 866-869, 1995) and the human (hPGT) (Lu, R., and V. L. Schuster, J. 
      Clin. Invest. 98: 1142-1149, 1996). Here we have cloned and expressed the mouse
      PGT (mPGT) cDNA. The tissue distribution of mPGT mRNA expression is significantly
      more restricted than that of rPGT and hPGT mRNA. Although the deduced amino acid 
      sequence of mPGT is similar to the rat (91% identity) and human (82% identity)
      homologues, it has three regions of dissimilarity: amino acids 128-163 and
      283-298, and valine 610 and isoleucine 611 (predicted to lie within putative
      transmembrane span 12). Affinities of hPGT, rPGT, and mPGT for several PG
      substrates differed, with hPGT having the highest [low Michaelis constant (K(m))]
      and mPGT the lowest affinity. A chimeric protein, linking the N-terminal domain
      of mPGT with the C-terminal domain of hPGT, had affinity for PGE2
      indistinguishable from that of hPGT, indicating that the C-terminal domain
      dictates K(m). We mutagenized mouse valine 610 and isoleucine 611 to their
      corresponding human residues (methionine and glycine, respectively); however,
      these changes did not convert the inhibition constant of mPGT to that of hPGT.
      The mouse gene was localized to chromosome 9 in a region syntenic with the region
      of human chromosome 3 containing the hPGT gene. These studies highlight the
      species-dependence of tissue expression and function of PGT and lay the
      groundwork for the use of the mouse as a model system for the study of PGT
      function.
FAU - Pucci, M L
AU  - Pucci ML
AD  - Department of Medicine, Albert Einstein College of Medicine, Bronx, New York
      10461, USA.
FAU - Bao, Y
AU  - Bao Y
FAU - Chan, B
AU  - Chan B
FAU - Itoh, S
AU  - Itoh S
FAU - Lu, R
AU  - Lu R
FAU - Copeland, N G
AU  - Copeland NG
FAU - Gilbert, D J
AU  - Gilbert DJ
FAU - Jenkins, N A
AU  - Jenkins NA
FAU - Schuster, V L
AU  - Schuster VL
LA  - eng
GR  - R01 DK049688/DK/NIDDK NIH HHS/United States
GR  - DK-49688/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 (Antiporters)
RN  - 0 (DNA, Complementary)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Organic Anion Transporters)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (SLCO2A1 protein, human)
RN  - 0 (Slco2a1 protein, mouse)
RN  - 0 (Slco2a1 protein, rat)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antiporters/*genetics/metabolism
MH  - Chromosome Mapping
MH  - Cloning, Molecular
MH  - DNA, Complementary/*genetics/isolation & purification
MH  - DNA-Binding Proteins/*genetics/metabolism
MH  - Humans
MH  - Mice
MH  - Molecular Sequence Data
MH  - Organ Specificity
MH  - Organic Anion Transporters
MH  - Rats
MH  - Recombinant Fusion Proteins/genetics/metabolism
MH  - Sequence Alignment
MH  - Species Specificity
EDAT- 1999/09/14 00:00
MHDA- 1999/09/14 00:01
CRDT- 1999/09/14 00:00
PHST- 1999/09/14 00:00 [pubmed]
PHST- 1999/09/14 00:01 [medline]
PHST- 1999/09/14 00:00 [entrez]
AID - 10.1152/ajpregu.1999.277.3.R734 [doi]
PST - ppublish
SO  - Am J Physiol. 1999 Sep;277(3):R734-41. doi: 10.1152/ajpregu.1999.277.3.R734.