| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
|
|
|
|||||||
|
|||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Papers In Press, published online ahead of print April 29, 2002
Laboratory of Cellular Biochemistry, RIKEN, Wako, Saitama 351-0198
Corresponding Author: staka{at}postman.riken.go.jp
A novel member of the mouse
J. Biol. Chem, 10.1074/jbc.M112367200
Submitted on December 26, 2001
Revised on April 26, 2002
Accepted on April 29, 2002
Molecular cloning and expression of a sixth type of
2,8-sialyltransferase (ST8Sia VI) that sialylates O-glycans
2,8-sialyltransferase (ST8Sia) family, designated ST8Sia VI, was identified by BLAST analysis of expressed sequence tags. The sequence of ST8Sia VI encoded a protein of 398 amino acids and it showed 42.0% and 38.3% amino acid sequence identity with mouse 2,8-sialyltransferases ST8Sia I (GD3 synthase) and ST8Sia V (GD1c, GT1a, GQ1b, and GT3 synthase), respectively. The recombinant soluble form of ST8Sia VI expressed in COS-7 cells exhibited 2,8-sialyltransferase activity toward both glycolipids and glycoproteins that have the NeuAc2,3(6)Gal sequence at the nonreducing end of their carbohydrate groups. This enzyme formed NeuAc2,8NeuAc-structures but not oligo or polysialic acid structures. Analysis of the fetuin sialylated by ST8Sia VI indicated that ST8Sia VI prefers O-glycans to N-glycans as acceptor substrates. Substrate specificities and kinetic properties also showed that ST8Sia VI prefers O-glycans to glycolipids as acceptor substrates. ST8Sia VI also exhibited activity toward oligosaccharides such as 3’- and 6’-sialyllactose, and the structure of the minimal acceptor substrate for ST8Sia VI is determined as the NeuAc2,3(6)Gal sequence. The expression of the ST8Sia VI gene was ubiquitous, and the highest expression was observed in kidney with three major transcripts of 8.2, 3.8, and 2.7 kb. This is the first report of a mammalian 2,8-sialyltransferase that sialylates O-glycans preferentially.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  Y. Takakura, H. Tsukamoto, and T. Yamamoto Molecular Cloning, Expression and Properties of an {alpha}/{beta}-Galactoside {alpha}2,3-Sialyltransferase from Vibrio sp. JT-FAJ-16 J. Biochem., September 1, 2007; 142(3): 403 - 412. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Asahina, C. Sato, M. Matsuno, T. Matsuda, K. Colley, and K. Kitajima Involvement of the {alpha}2,8-Polysialyltransferases II/STX and IV/PST in the Biosynthesis of Polysialic Acid Chains on the O-Linked Glycoproteins in Rainbow Trout Ovary J. Biochem., November 1, 2006; 140(5): 687 - 701. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. Avril, S. J. North, S. M. Haslam, H. J. Willison, and P. R. Crocker Probing the cis interactions of the inhibitory receptor Siglec-7 with {alpha}2,8-disialylated ligands on natural killer cells and other leukocytes using glycan-specific antibodies and by analysis of {alpha}2,8-sialyltransferase gene expression J. Leukoc. Biol., October 1, 2006; 80(4): 787 - 796. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Z. Yasukawa, C. Sato, K. Sano, H. Ogawa, and K. Kitajima Identification of disialic acid-containing glycoproteins in mouse serum: a novel modification of immunoglobulin light chains, vitronectin, and plasminogen Glycobiology, July 1, 2006; 16(7): 651 - 665. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Z. Yasukawa, C. Sato, and K. Kitajima Inflammation-dependent changes in {alpha}2,3-, {alpha}2,6-, and {alpha}2,8-sialic acid glycotopes on serum glycoproteins in mice Glycobiology, September 1, 2005; 15(9): 827 - 837. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Harduin-Lepers, R. Mollicone, P. Delannoy, and R. Oriol The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach Glycobiology, August 1, 2005; 15(8): 805 - 817. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. Koles, K. D. Irvine, and V. M. Panin Functional Characterization of Drosophila Sialyltransferase J. Biol. Chem., February 6, 2004; 279(6): 4346 - 4357. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Takashima, S. Tsuji, and M. Tsujimoto Comparison of the Enzymatic Properties of Mouse {beta}-Galactoside {alpha}2,6-Sialyltransferases, ST6Gal I and II J. Biochem., August 1, 2003; 134(2): 287 - 296. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Takashima, S. Tsuji, and M. Tsujimoto Characterization of the Second Type of Human beta -Galactoside alpha 2,6-Sialyltransferase (ST6Gal II), Which Sialylates Galbeta 1,4GlcNAc Structures on Oligosaccharides Preferentially. GENOMIC ANALYSIS OF HUMAN SIALYLTRANSFERASE GENES J. Biol. Chem., November 22, 2002; 277(48): 45719 - 45728. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
