Developmental expression and characterization of the alpha2,8-polysialyltransferase activity in embryonic chick brain.

@article{Sevigny1998DevelopmentalEA,
  title={Developmental expression and characterization of the alpha2,8-polysialyltransferase activity in embryonic chick brain.},
  author={M B Sevigny and Jin Ye and Shinobu Kitazume-Kawaguchi and Frederic A. Troy},
  journal={Glycobiology},
  year={1998},
  volume={8 9},
  pages={857-67}
}
The alpha2,8-polysialyltransferases (polySTs) from embryonic chick brain catalyze the alpha2,8-specific polysialylation of endogenous neural cell adhesion molecules (N-CAMs). This posttranslation glycosylation decreases N-CAM-dependent cell adhesion and migration. The enzymatic properties of the membrane-bound form of the polyST activity was investigated in vitro. Our results show that the polyST activity was developmentally expressed with maximum specific activity appearing about 12 days after… CONTINUE READING

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DTT and chemical modification studies using the thiol - directed alkylating reagents , N - ethylmaleimide ( NEM ) and iodoacetamide ( IAA ) , were used to show that at least one cysteinyl residue in the polyST was of critical importance for polysialylation , but of lesser importance for monosialylation , catalyzed by the alpha2,3- , alpha2,6- , and alpha2,8-monosialyltransferases ( monoSTs ) .
DTT and chemical modification studies using the thiol - directed alkylating reagents , N - ethylmaleimide ( NEM ) and iodoacetamide ( IAA ) , were used to show that at least one cysteinyl residue in the polyST was of critical importance for polysialylation , but of lesser importance for monosialylation , catalyzed by the alpha2,3- , alpha2,6- , and alpha2,8-monosialyltransferases ( monoSTs ) .
First , the polySTs contain heparin - like , positively charged amino acid clusters upstream of both sialylmotif L and S. Second , the polySTs contain a uniquely extended basic amino acid region ( pI 11 .
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