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B3GAT2  -  beta-1,3-glucuronyltransferase 2

Homo sapiens

Synonyms: Beta-1,3-glucuronyltransferase 2, GLCATS, Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2, GlcAT-D, GlcAT-S, ...
 
 
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Disease relevance of B3GAT2

  • To clarify the enzymatic properties of the respective glucuronyltransferases, we established an expression system for producing large amounts of soluble forms of flag-tagged human GlcAT-P and GlcAT-S in Escherichia coli [1].
 

High impact information on B3GAT2

  • Our data unequivocally establish that inflammatory cytokines, particularly TNF-alpha, stimulate the glucuronosyltransferse, GlcAT-P, and GlcAT-S, gene expression in brain endothelial cells and promote T-cell adhesion via SGPG-L-selectin recognition, a preliminary step for onset of neuroinflammation [2].
  • Both GlcAT-P and GlcAT-S transferred glucuronic acid (GlcA) not only to a glycoprotein acceptor, asialoorosomucoid (ASOR), but also to a glycolipid acceptor, paragloboside [3].
  • The deduced amino acid sequence of mouse GlcAT-S consists of 324 amino acids and has a type II membrane topology [4].
  • Moreover, the mouse GlcAT-S gene is composed of four exons spanning over more than 25 kilobase pairs [4].
  • Southern blot analysis and chromosomal mapping indicated that the mouse GlcAT-S gene is a single copy gene and it was mapped to the A4-B region of mouse chromosome 1 [4].
 

Biological context of B3GAT2

  • Cloning, characterization, and chromosome mapping of the human GlcAT-S gene [5].
  • GlcAT-S is composed of four exons and encodes a 324-amino-acid protein, which shows 89% homology with the rat glcat-s protein and is involved in the biosynthesis of the HNK-1 carbohydrate epitope on glycoproteins [5].
  • Comparative analyses of the enzymatic activities of GlcAT-S and GlcAT-P showed that there are notable differences in the acceptor substrate specificities of these enzymes [6].
 

Associations of B3GAT2 with chemical compounds

  • Phe245, one of the most important GlcAT-P residues for the recognition of acceptors, is a tryptophan in GlcAT-S [6].
  • In addition, Val320, which is located on the C-terminal long loop of the neighboring molecule in the dimer and critical in the recognition of the acceptor sugar molecule by the GlcAT-P dimer, is an alanine in GlcAT-S [6].
 

Analytical, diagnostic and therapeutic context of B3GAT2

  • These differences play key roles in establishing the distinct specificity for the acceptor substrate by GlcAT-S, which is further supported by site-directed mutagenesis of GlcAT-S and a computer-aided model building of GlcAT-S/substrate complexes [6].
  • Northern blot analysis revealed that the mouse GlcAT-S transcript is specifically expressed in the nervous system [4].

References

  1. Purification and characterization of two recombinant human glucuronyltransferases involved in the biosynthesis of HNK-1 carbohydrate in Escherichia coli. Kakuda, S., Oka, S., Kawasaki, T. Protein Expr. Purif. (2004) [Pubmed]
  2. Tumor necrosis factor-alpha up-regulates glucuronosyltransferase gene expression in human brain endothelial cells and promotes T-cell adhesion. Dasgupta, S., Yanagisawa, M., Krishnamurthy, K., Liour, S.S., Yu, R.K. J. Neurosci. Res. (2007) [Pubmed]
  3. Different acceptor specificities of two glucuronyltransferases involved in the biosynthesis of HNK-1 carbohydrate. Kakuda, S., Sato, Y., Tonoyama, Y., Oka, S., Kawasaki, T. Glycobiology (2005) [Pubmed]
  4. cDNA cloning, genomic structure and chromosomal mapping of the mouse glucuronyltransferase-S involved in the biosynthesis of the HNK-1 carbohydrate epitope. Imiya, K., Ishizaki, T., Seiki, T., Saito, F., Inazawa, J., Oka, S., Kawasaki, T. Gene (2002) [Pubmed]
  5. Cloning, characterization, and chromosome mapping of the human GlcAT-S gene. Marcos, I., Galán, J.J., Borrego, S., Antiñolo, G. J. Hum. Genet. (2002) [Pubmed]
  6. Crystal structure of GlcAT-S, a human glucuronyltransferase, involved in the biosynthesis of the HNK-1 carbohydrate epitope. Shiba, T., Kakuda, S., Ishiguro, M., Morita, I., Oka, S., Kawasaki, T., Wakatsuki, S., Kato, R. Proteins (2006) [Pubmed]
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