PMID- 11333265
OWN - NLM
STAT- MEDLINE
DCOM- 20010816
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 276
IP  - 28
DP  - 2001 Jul 13
TI  - Molecular cloning and characterization of a novel human galactose 
      3-O-sulfotransferase that transfers sulfate to gal beta 1-->3galNAc residue in 
      O-glycans.
PG  - 25697-704
AB  - We have identified a novel galactose 3-O-sulfotransferase, termed Gal3ST-4, by 
      analysis of an expression sequence tag using the amino acid sequence of human 
      cerebroside 3'-sulfotransferase (Gal3ST-1). The isolated cDNA contains a single 
      open reading frame coding for a protein of 486 amino acids with a type II 
      transmembrane topology. The amino acid sequence of Gal3ST-4 revealed 33%, 39%, 
      and 30% identity to human Gal3ST-1, Gal beta 1-->3/4GlcNAc:-->3'-sulfotransferase 
      (Gal3ST-2) and Gal beta 1-->4GlcNAc:-->3'-sulfotransferase (Gal3ST-3), 
      respectively. The Gal3ST-4 gene comprised at least four exons and was located on 
      human chromosome 7q22. Expression of Gal3ST-4 in COS-7 cells produced a 
      sulfotransferase activity that catalyzes the transfer of [(35)S]sulfate to the 
      C-3' position of Gal beta 1-->3GalNAc alpha 1-O-Bn. Gal3ST-4 recognizes Gal beta 
      1-->3GalNAc and Gal beta 1-->3(GlcNAc beta 1-->6)GalNAc as good substrates, but 
      not Gal beta 1-->3GalNAc(OH) or Gal beta 1-->3/4GlcNAc. Asialofetuin is also a 
      good substrate, and the sulfation was found exclusively in O-linked glycans that 
      consist of the Gal beta 1-->3GalNAc moiety, suggesting that the enzyme is 
      specific for O-linked glycans. Northern blot analysis revealed that 2.5-kilobase 
      mRNA for the enzyme is expressed extensively in various tissues. These results 
      suggest that Gal3ST-4 is the fourth member of a Gal:-->3-sulfotransferase family 
      and that the four members, Gal3ST-1, Gal3ST-2, Gal3ST-3, and Gal3ST-4, are 
      responsible for sulfation of different acceptor substrates.
FAU - Seko, A
AU  - Seko A
AD  - Department of Biochemistry, Sasaki Institute, 2-2, Kanda-Surugadai, 2-3, 
      Chiyoda-ku, Tokyo 101-0062, Japan.
FAU - Hara-Kuge, S
AU  - Hara-Kuge S
FAU - Yamashita, K
AU  - Yamashita K
LA  - eng
SI  - GENBANK/AF316113
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20010501
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Polysaccharides)
RN  - 0 (Sulfates)
RN  - EC 2.8.2.- (Sulfotransferases)
RN  - EC 2.8.2.- (galactose 3-O-sulfotransferase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Cloning, Molecular
MH  - Humans
MH  - Molecular Sequence Data
MH  - Polysaccharides/metabolism
MH  - Sequence Alignment
MH  - Substrate Specificity
MH  - Sulfates/metabolism
MH  - Sulfotransferases/*genetics/metabolism
EDAT- 2001/05/03 10:00
MHDA- 2001/08/17 10:01
CRDT- 2001/05/03 10:00
PHST- 2001/05/03 10:00 [pubmed]
PHST- 2001/08/17 10:01 [medline]
PHST- 2001/05/03 10:00 [entrez]
AID - S0021-9258(19)30112-7 [pii]
AID - 10.1074/jbc.M101558200 [doi]
PST - ppublish
SO  - J Biol Chem. 2001 Jul 13;276(28):25697-704. doi: 10.1074/jbc.M101558200. Epub 
      2001 May 1.