Novel induction of α-lactalbumin-mediated lacdiNAc-R expression in vivo

被引：4

作者：

Do, SI ^{[1
]}

Lee, KY ^{[1
]}

Kim, HN ^{[1
]}

机构：

[1] KRIBB, Glycobiol Div, Anim Cell & Med Glycobiol Lab, Taejon 305600, South Korea

来源：

BIOCHEMICAL JOURNAL | 2000年 / 348卷 / pt 1期

关键词：

nucleotide sugar switching; Lec8; cells; beta 1,4-galactosyltransferase; beta 1,4-N-acetylgalactosaminyltransferase;

D O I：

10.1042/0264-6021:3480229

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：

alpha-lactalbumin (alpha-LA) is a regulatory protein by which the mammalian beta 1,4-galactosyltransferase (beta 1,4-galT) is induced to utilize glucose as an acceptor instead of N-acetylglucosamine (GlcNAc) during lactose synthesis in mammary gland. a-LA can also modulate beta 1,4-galT to utilize UDP-N-acetylgalactosamine (UDP-GalNAc) as a donor towards GlcNAc acceptor substrate with high efficiency in vitro [Do, Do and Cummings (1995) J. Biol. Chem. 270, 18447-18451]. In the present study we transfected cDNA encoding bovine alpha-LA into Lec8 cells and examined whether nucleotide sugar switching of UDP-galactose (UDP- Cal) into UDP-GalNAc occurred in vivo and whether the neo-glycosylation of GalNAc beta 1,4GlcNAc-R structure was synthesized in cc-LA-stable transfectants. Our studies demonstrate that the stable expression of oc-LA in Lec8 cells induces the formation of GalNAc beta 1,4GlcNAc-R in vivo through nucleotide sugar switching of beta 1,4-galT.

引用

页码：229 / 234

页数：6

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