ST6GalNAc II重新定义的底物特异性：第二个候选唾液酸化Tn合酶
Redefined substrate specificity of ST6GalNAc II: a second candidate sialyl-Tn synthase.
作者信息
Kono M, Tsuda T, Ogata S, Takashima S, Liu H, Hamamoto T, Itzkowitz S H, Nishimura S, Tsuji S
机构信息
Molecular Glycobiology, Frontier Research Program, Institute of Physical and Chemical Research (RIKEN), Wako, Saitama, Japan.
出版信息
Biochem Biophys Res Commun. 2000 May 27;272(1):94-7. doi: 10.1006/bbrc.2000.2745.
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., NeuAc alpha2-6GalNAc-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.
利用绵羊颌下粘蛋白、[Ala-Thr（GalNAc）-Ala]n聚合物（n = 7 - 11），对作用于O-连接寡糖合成的ST6GalNAc I和II的受体底物特异性进行了重新研究。有人提出，基于ST6GalNAc I而非ST6GalNAc II对去唾液酸半乳糖胎球蛋白表现出活性这一结果，只有ST6GalNAc I能够合成唾液酸化-Tn抗原的碳水化合物结构，即NeuAcα2-6GalNAc-O-Thr/Ser[黑泽等人，《生物化学杂志》269，19048 - 19053（1994）]。在本研究中，我们提供证据表明，ST6GalNAc I和II对仅具有GalNAc-O-Thr/Ser结构的去唾液酸-OSM（绵羊颌下粘蛋白）和[Ala-Thr（GalNAc）-Ala]n聚合物（n = 7 - 11）均表现出活性。这些结果有力地表明，不仅ST6GalNAc I，而且ST6GalNAc II都是唾液酸化-Tn合成酶的候选者。
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