Molecular cloning and expression of GalNAc alpha 2,6-sialyltransferase.
作者： N. Kurosawa , T. Hamamoto , Y.C. Lee , T. Nakaoka , N. Kojima
DOI: 10.1016/S0021-9258(17)42272-1
关键词:
摘要: cDNA clones encoding GalNAc alpha 2,6-sialyltransferase (EC 2.4.99.3) have been isolated from chick embryo libraries using sequence information obtained the conserved amino acid of previously cloned enzymes. The included an open reading frame coding for 566 acids, and deduced showed 12% identity with that Gal beta 1,4GlcNAc embryo. primary structure this enzyme suggested a putative domain structure, like in other glycosyltransferases, consisting short NH2-terminal cytoplasmic domain, signal-membrane anchor proteolytically sensitive stem region, large COOH-terminal active domain. was confirmed by construction recombinant sialyltransferase which part (232 residues) replaced immunoglobulin signal sequence. expression COS-7 cells resulted secretion catalytically soluble form into medium. expressed exhibited activity toward only asialomucin (asialo)fetuin, no significant being detected glycoprotein glycolipid substrates tested. 14C-Sialylated glycols re-sialylated were identical to NeuAc 2,6-GalNAc-ol GlcNAc 1,3(NeuAc 2,6) GalNAc-ol. Synthetic GalNAc-SerNAc also served as acceptor 2,6-sialylation. These results clearly is 2,6-sialyltransferase.
sci-hub.st 参考文章(58)
A. Arce, H. J. Maccioni, R. Caputto, The biosynthesis of gangliosides. The incorporation of galactose, N-acetylgalactosamine and N-acetylneuraminic acid into endogenous acceptors of subcellular particles from rat brain in vitro Biochemical Journal. ,vol. 121, pp. 483- 493 ,(1971) , 10.1042/BJ1210483
SUSAN J. KIMBER, Changes in cell-surface glycoconjugates during embryonic development demonstrated using lectins and other probes. Biochemical Society Transactions. ,vol. 17, pp. 23- 27 ,(1989) , 10.1042/BST0170023
M L Bergh, G J Hooghwinkel, D H van den Eijnden, Biosynthesis of the O-glycosidically linked oligosaccharide chains of fetuin. Indications for an alpha-N-acetylgalactosaminide alpha 2 leads to 6 sialyltransferase with a narrow acceptor specificity in fetal calf liver. Journal of Biological Chemistry. ,vol. 258, pp. 7430- 7436 ,(1983) , 10.1016/S0021-9258(18)32197-5
J C Paulson, K J Colley, Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation. Journal of Biological Chemistry. ,vol. 264, pp. 17615- 17618 ,(1989) , 10.1016/S0021-9258(19)84610-0
H Den, B Kaufman, E J McGuire, S Roseman, The sialic acids. XVIII. Subcellular distribution of seven glycosyltransferases in embryonic chicken brain. Journal of Biological Chemistry. ,vol. 250, pp. 739- 746 ,(1975) , 10.1016/S0021-9258(19)41958-3
J Weinstein, U de Souza-e-Silva, J C Paulson, Purification of a Gal beta 1 to 4GlcNAc alpha 2 to 6 sialyltransferase and a Gal beta 1 to 3(4)GlcNAc alpha 2 to 3 sialyltransferase to homogeneity from rat liver. Journal of Biological Chemistry. ,vol. 257, pp. 13835- 13844 ,(1982) , 10.1016/S0021-9258(18)33524-5
A Rosenberg, A Sauer, E.P. Noble, H.J. Gross, R Chang, R Brossmer, Developmental patterns of ganglioside sialosylation coincident with neuritogenesis in cultured embryonic chick brain neurons Journal of Biological Chemistry. ,vol. 267, pp. 10607- 10612 ,(1992) , 10.1016/S0021-9258(19)50060-6
D M Carlson, C Blackwell, Structures and Immunochemical Properties of Oligosaccharides Isolated from Pig Submaxillary Mucins Journal of Biological Chemistry. ,vol. 243, pp. 616- 626 ,(1968) , 10.1016/S0021-9258(18)93649-5
J Weinstein, E U Lee, K McEntee, P H Lai, J C Paulson, Primary structure of beta-galactoside alpha 2,6-sialyltransferase. Conversion of membrane-bound enzyme to soluble forms by cleavage of the NH2-terminal signal anchor. Journal of Biological Chemistry. ,vol. 262, pp. 17735- 17743 ,(1987) , 10.1016/S0021-9258(18)45441-5
Halina Den, Bernard Kaufman, Saul Roseman, Properties of some glycosyltransferases in embryonic chicken brain. Journal of Biological Chemistry. ,vol. 245, pp. 6607- 6615 ,(1970) , 10.1016/S0021-9258(18)62577-3