Oligosaccharide structure of human C4.
Open Access
- 1 March 1985
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Immunology
- Vol. 134 (3) , 1790-1798
- https://doi.org/10.4049/jimmunol.134.3.1790
Abstract
The oligosaccharide structure of human C4 was studied by using C4 purified from plasma and C4 secreted by human hepatoma-derived cell line, HepG2. The alpha- and beta-chains of human C4 are glycosylated, whereas the gamma-chain is devoid of carbohydrate. The alpha-chain has three complex fucosylated oligosaccharides of the biantennary type, one each on the alpha 2, alpha 3, and alpha 4 fragments. The beta-chain has a single high mannose oligosaccharide primarily of the Man9GlcNAc2 type. The approximately 2000 Mr difference between the alpha-chains of the two C4 gene products (C4A and C4B) was localized to the alpha 2 fragment and is not due to carbohydrate. Sulfation of the C4 alpha-chain was localized to the alpha 4 fragment of the alpha-chain. Hence, the Mr difference between the two gene products is likely to reside in amino acid differences. The oligosaccharide structure of three incompletely processed C4 molecules was also analyzed. These molecules have the oligosaccharide composition of the appropriate individual subunits. Therefore, intracellular proteolytic processing to the multi-chain form of C4 is not required for proper oligosaccharide processing.This publication has 8 references indexed in Scilit:
- Variation in the glycosylation of the murine sex-limited protein: comparison with the fourth component of murine complement.The Journal of Immunology, 1983
- Amino acid sequence homologies and glycosylation differences between the fourth component of murine complement and sex-limited protein.Proceedings of the National Academy of Sciences, 1982
- Complement biosynthesis by the human hepatoma-derived cell line HepG2.Journal of Clinical Investigation, 1982
- Separation of neutral oligosaccharides by high-performance liquid chromatographyAnalytical Biochemistry, 1981
- Synthesis of the mouse complement component C 4 (Ss‐protein) by peritoneal macrophages: kinetics of secretion and glycosylation of the subunitsEuropean Journal of Immunology, 1980
- A structural basis for four distinct elution profiles on concanavalin A – Sepharose affinity chromatography of glycopeptidesCanadian Journal of Biochemistry, 1979
- Structural and functional differences between the H-2 controlled Ss and Slp proteins.The Journal of Experimental Medicine, 1978
- Cell-free synthesis of the fourth component of guinea pig complement (C4): identification of a precursor of serum C4 (pro-C4).Proceedings of the National Academy of Sciences, 1977