PMID- 10535998
OWN - NLM
STAT- MEDLINE
DCOM- 19991210
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 22
DP  - 1999 Oct 26
TI  - Molecular cloning and functional analysis of SUT-1, a sulfate transporter from
      human high endothelial venules.
PG  - 12772-7
AB  - High endothelial venules (HEV) are specialized postcapillary venules found in
      lymphoid organs and chronically inflamed tissues that support high levels of
      lymphocyte extravasation from the blood. One of the major characteristics of HEV 
      endothelial cells (HEVEC) is their capacity to incorporate large amounts of
      sulfate into sialomucin-type counter-receptors for the lymphocyte homing receptor
      L-selectin. Here, we show that HEVEC express two functional classes of sulfate
      transporters defined by their differential sensitivity to the anion-exchanger
      inhibitor 4,4'-diisothiocyanostilbene-2, 2'-disulfonic acid (DIDS), and we report
      the molecular characterization of a DIDS-resistant sulfate transporter from human
      HEVEC, designated SUT-1. SUT-1 belongs to the family of Na(+)-coupled anion
      transporters and exhibits 40-50% amino acid identity with the rat renal
      Na(+)/sulfate cotransporter, NaSi-1, as well as with the human and rat
      Na(+)/dicarboxylate cotransporters, NaDC-1/SDCT1 and NaDC-3/SDCT2. Functional
      expression studies in cRNA-injected Xenopus laevis oocytes showed that SUT-1
      mediates high levels of Na(+)-dependent sulfate transport, which is resistant to 
      DIDS inhibition. The SUT-1 gene mapped to human chromosome 7q33. Northern
      blotting analysis revealed that SUT-1 exhibits a highly restricted tissue
      distribution, with abundant expression in placenta. Reverse transcription-PCR
      analysis indicated that SUT-1 and the diastrophic dysplasia sulfate transporter
      (DTD), one of the two known human DIDS-sensitive sulfate transporters, are
      coexpressed in HEVEC. SUT-1 and DTD could correspond, respectively, to the
      DIDS-resistant and DIDS-sensitive components of sulfate uptake in HEVEC.
      Together, these results demonstrate that SUT-1 is a distinct human Na(+)-coupled 
      sulfate transporter, likely to play a major role in sulfate incorporation in HEV.
FAU - Girard, J P
AU  - Girard JP
AD  - Laboratoire de Biologie Vasculaire, Institut de Pharmacologie et de Biologie
      Structurale du Centre National de la Recherche Scientifique, 205 route de
      Narbonne, 31077 Toulouse, France. girard@ipbs.fr
FAU - Baekkevold, E S
AU  - Baekkevold ES
FAU - Feliu, J
AU  - Feliu J
FAU - Brandtzaeg, P
AU  - Brandtzaeg P
FAU - Amalric, F
AU  - Amalric F
LA  - eng
SI  - GENBANK/AF169301
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Anion Transport Proteins)
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (SLC13A4 protein, human)
RN  - 0 (Sulfate Transporters)
RN  - 0 (Sulfates)
RN  - 0 (Symporters)
RN  - 9NEZ333N27 (Sodium)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - *Anion Transport Proteins
MH  - Carrier Proteins/*genetics/metabolism
MH  - Cells, Cultured
MH  - Chromosome Mapping
MH  - Chromosomes, Human, Pair 7
MH  - Cloning, Molecular
MH  - DNA, Complementary
MH  - Endothelium, Vascular/cytology/*metabolism
MH  - Humans
MH  - Molecular Sequence Data
MH  - Rats
MH  - Sequence Homology, Amino Acid
MH  - Sodium/metabolism
MH  - Sulfate Transporters
MH  - Sulfates/*metabolism
MH  - *Symporters
MH  - Venules/cytology/*metabolism
PMC - PMC23093
EDAT- 1999/10/27 00:00
MHDA- 1999/10/27 00:01
CRDT- 1999/10/27 00:00
PHST- 1999/10/27 00:00 [pubmed]
PHST- 1999/10/27 00:01 [medline]
PHST- 1999/10/27 00:00 [entrez]
AID - 10.1073/pnas.96.22.12772 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12772-7. doi:
      10.1073/pnas.96.22.12772.