PMID- 10187838
OWN - NLM
STAT- MEDLINE
DCOM- 19990503
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 15
DP  - 1999 Apr 9
TI  - Molecular cloning and characterization of a human uronyl 2-sulfotransferase that 
      sulfates iduronyl and glucuronyl residues in dermatan/chondroitin sulfate.
PG  - 10474-80
AB  - A partial-length human cDNA with a predicted amino acid sequence homologous to a 
      previously described heparan sulfate iduronyl 2-sulfotransferase (Kobayashi, M., 
      Habuchi, H., Yoneda, M., Habuchi, O., and Kimata, K. (1997) J. Biol. Chem. 272,
      13980-13985) was obtained by searching the expressed sequence-tagged data bank.
      Northern blot analysis was performed using this homologous cDNA as a probe, which
      demonstrated ubiquitous expression of messages of 5.1 and 2.0 kilobases in a
      number of human tissues and in several human cancer cell lines. Since the human
      lymphoma Raji cell line had the highest level of expression, it was used to
      isolate a full-length cDNA clone. The full-length cDNA was found to contain an
      open reading frame that predicted a type II transmembrane protein composed of 406
      amino acid residues. The cDNA in a baculovirus expression vector was expressed in
      Sf9 insect cells, and cell extracts were then incubated together with
      3'-phosphoadenosine 5'-phospho[35S]sulfate and potential glycosaminoglycan
      acceptors. This demonstrated substantial sulfotransferase activity with dermatan 
      sulfate, a small degree of activity with chondroitin sulfate, but no
      sulfotransferase activity with desulfated N-resulfated heparin. Analysis of
      [35S]sulfate-labeled disaccharide products of chondroitin ABC, chondroitin AC,
      and chondroitin B lyase treatment demonstrated that the enzyme only transferred
      sulfate to the 2-position of uronyl residues, which were preponderantly iduronyl 
      residues in dermatan sulfate, but some lesser transfer to glucuronyl residues of 
      chondroitin sulfate.
FAU - Kobayashi, M
AU  - Kobayashi M
AD  - Department of Biology, Massachusetts Institute of Technology, Cambridge,
      Massachusetts 02139, USA.
FAU - Sugumaran, G
AU  - Sugumaran G
FAU - Liu, J
AU  - Liu J
FAU - Shworak, N W
AU  - Shworak NW
FAU - Silbert, J E
AU  - Silbert JE
FAU - Rosenberg, R D
AU  - Rosenberg RD
LA  - eng
SI  - GENBANK/AB020316
GR  - AR-41649/AR/NIAMS NIH HHS/United States
GR  - HL-66385/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA, Complementary)
RN  - 0 (Glucuronates)
RN  - 24967-94-0 (Dermatan Sulfate)
RN  - 3402-98-0 (Iduronic Acid)
RN  - 8A5D83Q4RW (Glucuronic Acid)
RN  - 9007-28-7 (Chondroitin Sulfates)
RN  - EC 2.8.2.- (Sulfotransferases)
RN  - EC 2.8.2.- (UST protein, human)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Baculoviridae
MH  - Base Sequence
MH  - Chondroitin Sulfates/*metabolism
MH  - Chromatography, High Pressure Liquid
MH  - Cloning, Molecular
MH  - DNA, Complementary/chemistry
MH  - Dermatan Sulfate/*metabolism
MH  - Expressed Sequence Tags
MH  - Glucuronates/*metabolism
MH  - Glucuronic Acid
MH  - Humans
MH  - Iduronic Acid/*metabolism
MH  - Molecular Sequence Data
MH  - Spodoptera
MH  - Sulfotransferases/*genetics/*metabolism
MH  - Tumor Cells, Cultured
EDAT- 1999/04/03 00:00
MHDA- 1999/04/03 00:01
CRDT- 1999/04/03 00:00
PHST- 1999/04/03 00:00 [pubmed]
PHST- 1999/04/03 00:01 [medline]
PHST- 1999/04/03 00:00 [entrez]
AID - 10.1074/jbc.274.15.10474 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Apr 9;274(15):10474-80. doi: 10.1074/jbc.274.15.10474.