PMID- 10644753
OWN - NLM
STAT- MEDLINE
DCOM- 20000229
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 4
DP  - 2000 Jan 28
TI  - The occurrence of three isoforms of heparan sulfate 6-O-sulfotransferase having
      different specificities for hexuronic acid adjacent to the targeted
      N-sulfoglucosamine.
PG  - 2859-68
AB  - We previously cloned heparan sulfate 6-O-sulfotransferase (HS6ST) (Habuchi, H.,
      Kobayashi, M., and Kimata, K. (1998) J. Biol. Chem. 273, 9208-9213). In this
      study, we report the cloning and characterization of three mouse isoforms of
      HS6ST, a mouse homologue to the original human HS6ST (HS6ST-1) and two novel
      HS6STs (HS6ST-2 and HS6ST-3). The cDNAs have been obtained from mouse brain cDNA 
      library by cross-hybridization with human HS6ST cDNA. The three cDNAs contained
      single open reading frames that predicted type II transmembrane proteins composed
      of 401, 506, and 470 amino acid residues, respectively. Amino acid sequence of
      HS6ST-1 was 51 and 57% identical to those of HS6ST-2 and HS6ST-3, respectively.
      HS6ST-2 and HS6ST-3 had the 50% identity. Overexpression of each isoform in COS-7
      cells resulted in about 10-fold increase of HS6ST activity. The three isoforms
      purified with anti-FLAG antibody affinity column transferred sulfate to heparan
      sulfate and heparin but not to other glycosaminoglycans. Each isoform showed
      different specificity toward the isomeric hexuronic acid adjacent to the targeted
      N-sulfoglucosamine; HS6ST-1 appeared to prefer the iduronosyl N-sulfoglucosamine 
      while HS6ST-2 had a different preference, depending upon the substrate
      concentrations, and HS6ST-3 acted on either substrate. Northern analysis showed
      that the expression of each message in various tissues was characteristic to the 
      respective isoform. HS6ST-1 was expressed strongly in liver, and HS6ST-2 was
      expressed mainly in brain and spleen. In contrast, HS6ST-3 was expressed rather
      ubiquitously. These results suggest that the expression of these isoforms may be 
      regulated in tissue-specific manners and that each isoform may be involved in the
      synthesis of heparan sulfates with tissue-specific structures and functions.
FAU - Habuchi, H
AU  - Habuchi H
AD  - Institute for Molecular Science of Medicine, Aichi Medical University, Nagakute, 
      Aichi 480-1195, Japan.
FAU - Tanaka, M
AU  - Tanaka M
FAU - Habuchi, O
AU  - Habuchi O
FAU - Yoshida, K
AU  - Yoshida K
FAU - Suzuki, H
AU  - Suzuki H
FAU - Ban, K
AU  - Ban K
FAU - Kimata, K
AU  - Kimata K
LA  - eng
SI  - GENBANK/AB024565
SI  - GENBANK/AB024566
SI  - GENBANK/AB024567
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA, Complementary)
RN  - 0 (Hexuronic Acids)
RN  - 0 (Isoenzymes)
RN  - 9050-30-0 (Heparitin Sulfate)
RN  - EC 2.8.2.- (HS6ST2 protein, human)
RN  - EC 2.8.2.- (Hs6st1 protein, mouse)
RN  - EC 2.8.2.- (Hs6st2 protein, mouse)
RN  - EC 2.8.2.- (Hs6st3 protein, mouse)
RN  - EC 2.8.2.- (Sulfotransferases)
RN  - EC 2.8.2.- (heparan sulfate 6-O-sulfotransferase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - COS Cells
MH  - Cloning, Molecular
MH  - DNA, Complementary
MH  - Heparitin Sulfate/*metabolism
MH  - Hexuronic Acids/chemistry/*metabolism
MH  - Humans
MH  - Isoenzymes/genetics/*metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Sequence Homology, Amino Acid
MH  - Substrate Specificity
MH  - Sulfotransferases/genetics/*metabolism
EDAT- 2000/01/25 09:00
MHDA- 2000/03/04 09:00
CRDT- 2000/01/25 09:00
PHST- 2000/01/25 09:00 [pubmed]
PHST- 2000/03/04 09:00 [medline]
PHST- 2000/01/25 09:00 [entrez]
AID - 10.1074/jbc.275.4.2859 [doi]
PST - ppublish
SO  - J Biol Chem. 2000 Jan 28;275(4):2859-68. doi: 10.1074/jbc.275.4.2859.