Document Detail


Molecular cloning and expression of human ST6GalNAc III: restricted tissue distribution and substrate specificity.
MedLine Citation:
PMID:  16169874     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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 alpha2,3-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.
Authors:
Akiko Tsuchida; Manabu Ogiso; Yoko Nakamura; Makoto Kiso; Keiko Furukawa; Koichi Furukawa
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of biochemistry     Volume:  138     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  2005 Sep 
Date Detail:
Created Date:  2005-09-19     Completed Date:  2005-12-02     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  237-43     Citation Subset:  IM    
Affiliation:
Department of Biochemistry II, Nagoya University School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-0065, Japan.
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MeSH Terms
Descriptor/Qualifier:
Alternative Splicing
Amino Acid Sequence
Animals
Base Sequence
Cell Line
Cloning, Molecular
Exons
Glycoside Hydrolases / metabolism
Humans
Mice
Molecular Sequence Data
Protein Isoforms / genetics,  metabolism*
Protein Structure, Tertiary
Rats
Sequence Alignment
Sialyltransferases / genetics,  metabolism*
Substrate Specificity
Tissue Distribution
alpha-Fetoproteins / chemistry,  metabolism
Chemical
Reg. No./Substance:
0/Protein Isoforms; 0/alpha-Fetoproteins; EC 2.4.99.-/Neu5Ac N-acetylgalactosamine 2,6-sialyltransferase; EC 2.4.99.-/Sialyltransferases; EC 3.2.1.-/Glycoside Hydrolases; EC 3.2.1.-/glycanase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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