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Title 

Cloning and expression of cDNA for a human Siaα2,3Galβ1,4GlcNA:α2,8-Sialyltransferase (hST8Sia III)

Authors 

Y C LeeY J KimKi-Young LeeKyung Sook KimB U KimH N KimC H KimSu Il Do

Publisher 

Elsevier

Issue Date 

1998

Citation 

Archives of Biochemistry and Biophysics, vol. 360, no. 1, pp. 41-46

Keywords 

sialic acidSiaα2,3Galβ1,4GlcNac:α2,8-sialyltransferase (hST8Sia III)fetuin glycoprotein acceptor

Abstract 

The cDNA encoding human Sia-α2,3-Gal-β1,4-Glc-NAc-R:α2,8- sialytransferase, hST8Sia III, was isolated by screening of a human brain cDNA library with polymerase chain reaction-amplified DNA probe generated from the sequence of mouse ST8Sia III (mST8Sia III) and by 5' rapid amplification of cDNA ends of mRNA isolated from human brain tissues. Comparative analysis of the predicted protein-coding region between our cloned hST8Sia III and mST8Sia III showed 92 and 96% identities in the nucleotide and the amino acid sequence, respectively. The soluble hST8Sia III protein expressed in COS-7 showed an extremely high catalytic activity of transferring sialic acid through α2,8-linkage to intact fetuin glycoprotein, whereas the transferring activity was completely undetectable toward either α2,6-sialylated glycoprotein or desialylated glycoprotein acceptors. Northern analysis of hST8Sia III showed that the transcript corresponding to 11 kb was expressed in both human fetal and adult brain, while the expression of the 5.5-kb transcript was restricted to fetal liver, indicating that the expression of hST8Sia III is developmentally and tissue-specifically regulated.

ISSN 

0096-9621

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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