Skip Navigation

Journal of Biochemistry 2005 138(3):237-243; doi:10.1093/jb/mvi124
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
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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Tsuchida, A.
Right arrow Articles by Furukawa, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tsuchida, A.
Right arrow Articles by Furukawa, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2005 The Japanese Biochemical Society

Regular Paper

Molecular Cloning and Expression of Human ST6GalNAc III: Restricted Tissue Distribution and Substrate Specificity

Akiko Tsuchida1, Manabu Ogiso1, Yoko Nakamura1, Makoto Kiso2, Keiko Furukawa1 and Koichi Furukawa1,*

1 Department of Biochemistry II, Nagoya University School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-0065; and 2 Department of Applied Bioorganic Chemistry, Faculty of Agriculture, Gifu University, Gifu, 501-1193

* To whom correspondence should be addressed. Tel: +81-52-744-2070; Fax: +81-52-744-2069; E-mail: koichi{at}med.nagoya-u.ac.jp

We isolated human ST6GalNAc III cDNA clones. The typical cDNA clones predicted a type II membrane protein of 305 amino acids with a short cytoplasmic transmembrane domain of sixteen amino acids and a catalytic domain of 280 amino acids. A short form clone predicted a protein of 240 amino acids lacking 65 amino acids including the transmembrane portion. The alternative usage of the second exon seemed to generate these two transcripts. Both had two common regions found among sialyltransferases cloned so far, i.e. sialyl motif L and sialyl motif S. Alignments of human, mouse and rat orthologs indicated that high homologies, i.e. 85–95% identity among these species at amino acid levels. We analyzed the expression pattern and substrate specificity of the product, demonstrating a very restricted expression pattern and a high substrate specificity. Northern blotting revealed that hST6GalNAc III is expressed in kidney and brain as a single band at 3.2 kb. In enzyme assay of the long form, the transfer of sialic acid onto {alpha}2,3-sialylated acceptor substrates, i.e. GM1b and sialyl lactotetraosylceramide, was observed. hST6GalNAc III also showed sialyltransferase activity toward O-glycans (but not N-glycans) in fetuin.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J BiochemHome page
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]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.