JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kono, M.
Right arrow Articles by Tsuji, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kono, M.
Right arrow Articles by Tsuji, S.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Volume 271, Number 46, Issue of November 15, 1996 pp. 29366-29371
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Molecular Cloning and Expression of a Fifth Type of alpha 2,8-Sialyltransferase (ST8Sia V)
ITS SUBSTRATE SPECIFICITY IS SIMILAR TO THAT OF SAT-V/III, WHICH SYNTHESIZE GD1c, GT1a, GQ1b AND GT3

(Received for publication, June 20, 1996, and in revised form, August 19, 1996)

Mari Kono , Yukiko Yoshida , Naoya Kojima and Shuichi Tsuji

From Molecular Glycobiology, Frontier Research Program, The Institute of Physical and Chemical Research (RIKEN), Wako, Saitama 351-01, Japan

The cDNAs encoding a new alpha 2,8-sialyltransferase (ST8Sia V) were cloned from a mouse brain cDNA library by means of a polymerase chain reaction-based method using the nucleotide sequence information on mouse ST8Sia I (GD3 synthase) and mouse ST8Sia III (Siaalpha 2,3Galbeta 1,4GlcNAcalpha 2,8-sialyltransferase), both of which exhibit activity toward glycolipids. The predicted amino acid sequence of ST8Sia V shows 36.1% and 15.0% identity to those of mouse ST8Sia I and III, respectively. The recombinant protein A-fused ST8Sia V expressed in COS-7 cells exhibited an alpha 2,8-sialyltransferase activity toward GM1b, GD1a, GT1b, and GD3, and synthesized GD1c, GT1a, GQ1b, and GT3, respectively. The apparent Km values for GM1b, GD1a, GT1b and GD3 were 1.1, 0.082, 0.070, and 0.28 mM, respectively. However, ST8Sia V did not exhibit activity toward GM3. Thus, the substrate specificity of ST8Sia V is different from those of ST8Sia I and III, both of which exhibit activity toward GM3. Transfection of the ST8Sia V gene into COS-7 cells, which express GD1a as a major glycolipid, led to the expression of determinants for monoclonal antibody 4F10, which recognizes GT1a and GQ1b, suggesting that ST8Sia V exhibits activity toward gangliosides GD1a and/or GT1b in vivo. The expression of the ST8Sia V gene was tissue- and developmental stage-specific, and was clearly different from those of other alpha 2,8-sialyltransferase genes. The ST8Sia V gene was strongly expressed in the brain and weakly in other tissues such as the liver. In addition, its expression was greater in the adult than fetal brain. These results strongly indicate that ST8Sia V is a candidate for SAT-V, the alpha 2,8-sialyltransferase involved in GD1c, GT1a, GQ1b, and GT3 synthesis.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
GlycobiologyHome page
A. Ishii, T. Ikeda, S. Hitoshi, I. Fujimoto, T. Torii, K. Sakuma, S.-i. Nakakita, S. Hase, and K. Ikenaka
Developmental changes in the expression of glycogenes and the content of N-glycans in the mouse cerebral cortex
Glycobiology, March 1, 2007; 17(3): 261 - 276.
[Abstract] [Full Text] [PDF]


Home page
GlycobiologyHome page
E. M. Comelli, S. R. Head, T. Gilmartin, T. Whisenant, S. M. Haslam, S. J. North, N.-K. Wong, T. Kudo, H. Narimatsu, J. D. Esko, et al.
A focused microarray approach to functional glycomics: transcriptional regulation of the glycome
Glycobiology, February 1, 2006; 16(2): 117 - 131.
[Abstract] [Full Text] [PDF]


Home page
GlycobiologyHome page
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]


Home page
J. Lipid Res.Home page
R. K. Yu, E. Bieberich, T. Xia, and G. Zeng
Regulation of ganglioside biosynthesis in the nervous system
J. Lipid Res., May 1, 2004; 45(5): 783 - 793.
[Abstract] [Full Text] [PDF]


Home page
J BiochemHome page
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]


Home page
J. Biol. Chem.Home page
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 page
J. Biol. Chem.Home page
C. Sato, T. Matsuda, and K. Kitajima
Neuronal Differentiation-dependent Expression of the Disialic Acid Epitope on CD166 and Its Involvement in Neurite Formation in Neuro2A Cells
J. Biol. Chem., November 15, 2002; 277(47): 45299 - 45305.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Takashima, H.-k. Ishida, T. Inazu, T. Ando, H. Ishida, M. Kiso, S. Tsuji, and M. Tsujimoto
Molecular Cloning and Expression of a Sixth Type of alpha 2,8-Sialyltransferase (ST8Sia VI) That Sialylates O-Glycans
J. Biol. Chem., June 28, 2002; 277(27): 24030 - 24038.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Y.-C. Lee, M. Kaufmann, S. Kitazume-Kawaguchi, M. Kono, S. Takashima, N. Kurosawa, H. Liu, H. Pircher, and S. Tsuji
Molecular Cloning and Functional Expression of Two Members of Mouse NeuAc{alpha}2,3Gal{beta}1,3GalNAc GalNAc{alpha}2,6-Sialyltransferase Family, ST6GalNAc III and IV
J. Biol. Chem., April 23, 1999; 274(17): 11958 - 11967.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. K. Datta, A. Sinha, and J. C. Paulson
Mutation of the Sialyltransferase S-sialylmotif Alters the Kinetics of the Donor and Acceptor Substrates
J. Biol. Chem., April 17, 1998; 273(16): 9608 - 9614.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
N. Shiraishi, A. Natsume, A. Togayachi, T. Endo, T. Akashima, Y. Yamada, N. Imai, S. Nakagawa, S. Koizumi, S. Sekine, et al.
Identification and Characterization of Three Novel beta 1,3-N-Acetylglucosaminyltransferases Structurally Related to the beta 1,3-Galactosyltransferase Family
J. Biol. Chem., January 26, 2001; 276(5): 3498 - 3507.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. Angata, T.-Y. Yen, A. El-Battari, B. A. Macher, and M. Fukuda
Unique Disulfide Bond Structures Found in ST8Sia IV Polysialyltransferase Are Required for Its Activity
J. Biol. Chem., April 27, 2001; 276(18): 15369 - 15377.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. Angata, M. Suzuki, J. McAuliffe, Y. Ding, O. Hindsgaul, and M. Fukuda
Differential Biosynthesis of Polysialic Acid on Neural Cell Adhesion Molecule (NCAM) and Oligosaccharide Acceptors by Three Distinct alpha 2,8-Sialyltransferases, ST8Sia IV (PST), ST8Sia II (STX), and ST8Sia III
J. Biol. Chem., June 9, 2000; 275(24): 18594 - 18601.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.