RRC ID |
57671
|
Author |
Kojima N, Yoshida Y, Kurosawa N, Lee YC, Tsuji S.
|
Title |
Enzymatic activity of a developmentally regulated member of the sialyltransferase family (STX): evidence for alpha 2,8-sialyltransferase activity toward N-linked oligosaccharides.
|
Journal |
FEBS Lett
|
Abstract |
We have detected sialyltransferase activity of recombinant mouse STX, which was cloned from rat brain as a new member of the sialyltransferase family, but sialyltransferase activity of which had not been detected previously [Livingston and Paulson, J. Biol. Chem. (1993) 268, 11504-11507]. The activity of mouse STX was specific toward sialylated glycoproteins. N-Glycanase treatment and linkage-specific sialidase treatment of glycoproteins revealed that STX transfers sialic acids through alpha 2,8-linkages to only N-linked oligosaccharides of glycoproteins. However, polymerase activity for polysialic acid synthesis was not detected for this sialyltransferase. Since this alpha 2,8-sialyltransferase gene is highly restricted in fetal and newborn brain, it may be involved in the polysialylation of glycoproteins, especially of N-CAM.
|
Volume |
360(1)
|
Pages |
1-4
|
Published |
1995-2-20
|
DOI |
10.1016/0014-5793(95)00059-i
|
PII |
0014-5793(95)00059-I
|
PMID |
7875291
|
MeSH |
Animals
Base Sequence
Cloning, Molecular
DNA, Complementary
Gene Expression Regulation, Enzymologic*
Mice
Molecular Sequence Data
Oligosaccharides / metabolism*
Sialyltransferases / genetics
Sialyltransferases / metabolism*
|
IF |
3.057
|
Times Cited |
104
|
Resource |
DNA material |
mST8SiaII (RDB02078) |