Sialylation of glycoprotein oligosaccharides with N-acetyl-, N-glycolyl-, and N-O-diacetylneuraminic acids - PubMed (original) (raw)

. 1985 Jul 25;260(15):8838-49.

PMID: 4019457

Free article

Sialylation of glycoprotein oligosaccharides with N-acetyl-, N-glycolyl-, and N-O-diacetylneuraminic acids

H H Higa et al. J Biol Chem. 1985.

Free article

Abstract

Four common sialic acids (Sia), NeuAc, N-glycolyl-neuraminic acid (NeuGc), 4-O-acetyl-N-acetylneuraminic acid (4-O-Ac-NeuAc), and 9-O-Ac-NeuAc were examined for activation to their corresponding CMP-sialic acid conjugates and subsequently for their transfer to glycoprotein oligosaccharides by purified mammalian sialyltransferases. CMP-sialic acid synthetases from calf brain and from bovine and equine submaxillary glands were found to convert NeuAc, NeuGc, and 9-O-Ac-NeuAc to their corresponding CMP-sailic acids. In contrast, no conversion of 4-O-Ac-NeuAc to CMP-4-O-Ac-NeuAc was observed for any of the three synthetases examined. A new procedure for the preparation of CMP-9-O-Ac-NeuAc, CMP-NeuGc, and CMP-NeuAc in high yield and purity was developed, using the calf brain CMP-sialic acid synthetase. Each of these derivatives was tested as donor substrates for six mammalian sialyltransferases purified from porcine, rat, and bovine tissues, including a bovine GalNAc alpha 2,6 sialyltransferase whose purification is described in this report. The sialyltransferases examined represent those which form the Sia alpha 2,6Gal beta 1,4-GlcNAc-, Sia alpha 2,3Gal beta 1,3(4)GlcNAc-, Sia alpha 2,3Gal beta 1,3-GalNAc- and Sia alpha 2,6GalNAc- sequences found on N-linked and O-linked oligosaccharides of glycoproteins. CMP-NeuAc and CMP-NeuGc were equally good donor substrates for all six sialyltransferases. However, transfer of 9-O-Ac-NeuAc from CMP-9-O-Ac-NeuAc varied from only 10% to nearly 70% that of the transfer of NeuAc from CMP-NeuAc. Results are viewed to define the relative roles of direct transfer of these sialic acids and modification of glycosidically bound NeuAc in glycoproteins.

PubMed Disclaimer

Cited by

Tumor cell surface beta 1-4-linked galactose binds to lectin(s) on microvascular endothelial cells and contributes to organ colonization.
Cornil I, Kerbel RS, Dennis JW. Cornil I, et al. J Cell Biol. 1990 Aug;111(2):773-81. doi: 10.1083/jcb.111.2.773. J Cell Biol. 1990. PMID: 2116422 Free PMC article.
Relationship between mitogenic activity of influenza viruses and the receptor-binding specificity of their hemagglutinin molecules.
Anders EM, Scalzo AA, Rogers GN, White DO. Anders EM, et al. J Virol. 1986 Nov;60(2):476-82. doi: 10.1128/JVI.60.2.476-482.1986. J Virol. 1986. PMID: 3490581 Free PMC article.
Metabolism of vertebrate amino sugars with N-glycolyl groups: elucidating the intracellular fate of the non-human sialic acid N-glycolylneuraminic acid.
Bergfeld AK, Pearce OM, Diaz SL, Pham T, Varki A. Bergfeld AK, et al. J Biol Chem. 2012 Aug 17;287(34):28865-81. doi: 10.1074/jbc.M112.363549. Epub 2012 Jun 12. J Biol Chem. 2012. PMID: 22692205 Free PMC article.
Enzymatic synthesis of nucleotide sugars.
Bülter T, Elling L. Bülter T, et al. Glycoconj J. 1999 Feb;16(2):147-59. doi: 10.1023/a:1026444726698. Glycoconj J. 1999. PMID: 10612414 Review.
The N-glycolyl form of mouse sialyl Lewis X is recognized by selectins but not by HECA-452 and FH6 antibodies that were raised against human cells.
Mitoma J, Miyazaki T, Sutton-Smith M, Suzuki M, Saito H, Yeh JC, Kawano T, Hindsgaul O, Seeberger PH, Panico M, Haslam SM, Morris HR, Cummings RD, Dell A, Fukuda M. Mitoma J, et al. Glycoconj J. 2009 Jul;26(5):511-23. doi: 10.1007/s10719-008-9207-8. Epub 2008 Dec 17. Glycoconj J. 2009. PMID: 19089612 Free PMC article.

Sialylation of glycoprotein oligosaccharides with N-acetyl-, N-glycolyl-, and N-O-diacetylneuraminic acids - PubMed (original) (raw)