Structure of the N‐linked oligosaccharides of the human transferrin receptor
Open Access
- 1 April 1992
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 205 (1) , 257-267
- https://doi.org/10.1111/j.1432-1033.1992.tb16776.x
Abstract
Human transferrin receptor was isolated from placenta and from the hepatocarcinoma cell line Hep G2. Asparagine-linked oligosaccharides were released by treatment of tryptic glycopeptides with endo-β-N-acetylglucosaminidase H or peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase F. Oligosaccharide alditols were fractionated by anion-exchange high-performance liquid chromatography and by high-pH anion-exchange chromatography. Glycans from placental transferrin receptor were further characterized, after desialylation, by methylation analysis and, in part, by liquid secondary-ion mass spectrometry. Sialylation of placental transferrin receptor was examined by lectin affinity blotting with Sambucus nigra agglutinin and Maackia amurensis agglutinin. In order to trace possible inter-individual differences in N-glycosylation of the receptor, two preparations of placental transferrin receptor purified from two donors were compared. The results demonstrate that human transferrin receptor from placenta predominantly carries diantennary and triantennary N-acetyllactosaminic glycans as well as hybrid-type species, the galactose residues of which being almost completely substituted with (α2–3)-linked sialic acid residues. Distinct differences were noted in the glycosylation pattern of the receptor from different individuals. Transferrin receptor from donor A carried predominantly diantennary and triantennary complex-type glycans, in part fucosylated at the innermost N-acetylglucosamine residue, in addition to small amounts of bisected and of incomplete diantennary species. Placental transferrin receptor from donor B predominantly carried triantennary N-acetyllactosaminic glycans without fucose and hybrid-type oligosaccharides with four or five mannose residues. Distinct from placental transferrin receptor, the receptor from Hep G2 cells contained larger amounts of oligomannosidic glycans with six to nine mannose residues and tetrasialylated complex-type oligosaccharides apart from mono-, di- and trisialylated species.Keywords
This publication has 67 references indexed in Scilit:
- Presence of fucosylated triantennary, tetraantennary and pentaantennary glycans in transferrin synthesized by the human hepatocarcinoma cell line Hep G2European Journal of Biochemistry, 1989
- Carbohydrate structure of glycoprotein 65 encoded by the polycythemia‐inducing strain of Friend spleen focus‐forming virusEuropean Journal of Biochemistry, 1989
- Recycling glycoproteins do not return to the cis-Golgi.The Journal of cell biology, 1988
- Structural and conformational analysis of sialyloligosaccharides using carbon-13 nuclear magnetic resonance spectroscopyBiochemistry, 1984
- Coordination between enzyme specificity and intracellular compartmentation in the control of protein‐bound oligosaccharide biosynthesisBiology of the Cell, 1984
- Carbohydrates of the tumor cell surfaceBiochimica et Biophysica Acta (BBA) - Reviews on Cancer, 1984
- Separation procedure and sugar composition of oligosaccharides in the surface glycoprotein of friend murine leukemia virusBiochimica et Biophysica Acta (BBA) - General Subjects, 1982
- Different asparagine-linked sugar chains on the two polypeptide chains of human chorionic gonadotropinBiochemical and Biophysical Research Communications, 1980
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970