Redefined Substrate Specificity of ST6GalNAc II: A Second Candidate Sialyl-Tn Synthase
| Autor: | Shou Takashima, Shin-Ichiro Nishimura, Mari Kono, Shunichiro Ogata, Hong Liu, Shuichi Tsuji, Tetsuro Tsuda, Toshiro Hamamoto, Steven H. Itzkowitz |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Sialyltransferase
Stereochemistry Molecular Sequence Data Biophysics Oligosaccharides In Vitro Techniques Biochemistry Substrate Specificity ST6GalNAc II Mice Animals Antigens Tumor-Associated Carbohydrate Molecular Biology Sialyl tn Sheep ATP synthase biology Chemistry Ovine Submaxillary Mucin Cell Biology Carbohydrate Acceptor Recombinant Proteins Sialyltransferases carbohydrates (lipids) Carbohydrate Sequence COS Cells biology.protein Substrate specificity |
| Zdroj: | Biochemical and Biophysical Research Communications. 272:94-97 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.2000.2745 |
| Popis: | The acceptor substrate specificities of ST6GalNAc I and II, which act on the synthesis of O-linked oligosaccharides, were reexamined using ovine submaxillary mucin, [Ala-Thr(GalNAc)-Ala] n polymer ( n = 7–11). It has been suggested that only ST6GalNAc I can synthesize carbohydrate structures of sialyl-Tn-antigen; i.e., NeuAcα2-6GalNAc- O -Thr/Ser [Kurosawa et al., J. Biol. Chem. 269, 19048–19053 (1994)] based on the result that ST6GalNAc I, not ST6GalNAc II, exhibited activity toward asialoagalacto-fetuin. In this study, we present evidence that both ST6GalNAc I and II exhibit activity toward asialo-OSM (ovine submaxillary mucin) and [Ala-Thr(GalNAc)-Ala] n polymer ( n = 7–11) which have only the GalNAc- O -Thr/Ser-structures. These results strongly indicate that not only ST6GalNAc I but also II are candidates for sialyl-Tn synthases. |
| Databáze: | OpenAIRE |
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