Analysis of biochemical features of ST8 α-N-acetyl-neuraminide α2,8-sialyltransferase (St8sia) 5 isoforms

被引:3
作者
Araki, Erino [1 ,2 ]
Hane, Masaya [1 ,2 ,3 ]
Hatanaka, Rina [1 ,2 ]
Kimura, Ryota [1 ,2 ]
Tsuda, Kana [1 ,2 ]
Konishi, Miku [4 ]
Komura, Naoko [4 ]
Ando, Hiromune [4 ]
Kitajima, Ken [1 ,2 ,3 ]
Sato, Chihiro [1 ,2 ,3 ]
机构
[1] Nagoya Univ, Grad Sch Bioagr Sci, Chikusa Ku, Nagoya, Aichi 4648601, Japan
[2] Nagoya Univ, Biosci & Biotechnol Ctr, Chikusa Ku, Nagoya, Aichi 4648601, Japan
[3] Nagoya Univ, Inst Glycocore Res iGCORE, GlycobioMed Res Ctr iGMED, Chikusa Ku, Nagoya, Aichi 4648601, Japan
[4] Gifu Univ, Inst Glycocore Res iGCORE, 1-1 Yanagido, Gifu 5011193, Japan
关键词
Sialic acid; Sialyltransferase; Melanoma; Ganglioside; isoform; MOLECULAR-CLONING; EXPRESSION; SYNTHASE; GLYCOPROTEINS; RETENTION; ANTIGENS; ACIDS;
D O I
10.1007/s10719-021-10034-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Gangliosides are important components of the membrane and are involved in many biological activities. St8sia5 is an alpha 2,8-sialyltransferase involved in ganglioside synthesis, and has three isoforms. In this study, we analyzed the features of three isoforms, St8sia5-S, -M, and -L that had not been analyzed, and found that only St8sia5-L was localized in the Golgi, while the majority of St8sia5-M and -S were localized in the ER. The localization of Golgi of St8sia5 depended on the stem region. In addition, the incorporation of exogenous GD3 was upregulated only in St8sia5-L expressing cells. Taken together, the localization of St8sia5 is important for the activity of the enzyme.
引用
收藏
页码:291 / 302
页数:12
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