» Articles » PMID: 10211704

Increased Elongation of N-acetyllactosamine Repeats in Doubly Glycosylated Lysozyme with a Particular Spacing of the Glycosylation Sites

Overview
Journal Glycoconj J
Publisher Springer
Date 1999 Apr 22
PMID 10211704
Citations 1
Authors
Affiliations
Soon will be listed here.
Abstract

Lysozyme is an example of an extensively studied secretory enzyme. Glycosylated mutant human lysozyme has been used as a model in studies on the biosynthesis of N-acetyllactosamine repeats in N-linked oligosaccharides. We examined the biosynthesis of the repeats in two doubly glycosylated mutants and describe here a rapid purification and separation of singly and doubly glycosylated molecules. In one of the mutants, the elongation of the repeats is enhanced if the molecules are doubly glycosylated, but not if the carbohydrate is attached to either site individually. This enhancement is not seen in the other doubly glycosylated mutant. Since lysozyme is not structurally related to glycoproteins bearing carbohydrate with N-acetyllactosamine repeats, we propose that in multivalent substrates the synthesis of the repeats can be promoted by a proper spacing of the elongated carbohydrate antennae in addition to any role of the protein backbone.

Citing Articles

Glycosylation-site-selective synthesis of N-acetyl-lactosamine repeats in bis-glycosylated human lysozyme.

Melcher R, Hillebrand A, Bahr U, Schroder B, Karas M, Hasilik A Biochem J. 2000; 348 Pt 3:507-15.

PMID: 10839980 PMC: 1221091.

References
1.
Cho S, Yeh J, Cho M, Cummings R . Transcriptional regulation of alpha1,3-galactosyltransferase in embryonal carcinoma cells by retinoic acid. Masking of Lewis X antigens by alpha-galactosylation. J Biol Chem. 1996; 271(6):3238-46. DOI: 10.1074/jbc.271.6.3238. View

2.
Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

3.
Wang W, Lee N, Aoki D, Fukuda M, Fukuda M . The poly-N-acetyllactosamines attached to lysosomal membrane glycoproteins are increased by the prolonged association with the Golgi complex. J Biol Chem. 1991; 266(34):23185-90. View

4.
Fukuda M, Hakomori S . Structures of branched blood group A-active glycosphingolipids in human erythrocytes and polymorphism of A- and H-glycolipids in A1 and A2 subgroups. J Biol Chem. 1982; 257(1):446-55. View

5.
Tai G, Nieduszynski I, Fullwood N, Huckerby T . Human corneal keratan sulfates. J Biol Chem. 1997; 272(45):28227-31. DOI: 10.1074/jbc.272.45.28227. View