Glycosylation in Human Thyroglobulin: Location of the N-Linked Oligosaccharide Units and Comparison with Bovine Thyroglobulin
Abstract
The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence contains 20 putative N-linked glycosylation sites. We have characterized the glycopeptides contained in a tryptic digest of hTG in order to determine which sites are actually linked to carbohydrate. In addition, the distribution of oligosaccharide type(s) at these confirmed sites of N-linked glycosylation has been examined. Glycopeptides were purified using gel permeation chromatography followed by several steps of HPLC. The purified tryptic glycopeptides were characterized by gas phase sequencing and carbohydrate analysis and located within the amino acid sequence of thyroglobulin. Each of the recovered glycopeptides contained a consensus sequence for N-linked glycosylation. Of the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein. Eight of these confirmed glycosylation sites (at positions 57, 465, 510, 729, 797, 1696, 1754, and 2230) appear to be linked to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine. Five sites (at positions 1200, 1329, 1993, 2275, and 2562) contain high mannose type units and two sites (at positions 179 and 1345) are linked to oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose and may be either hybrid or complex structures. In addition, position 928 was found to be…
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Twelve previously predicted N-linked GlcNac were resolved in the maps, and four that had not been identified were found at N110, N484, N1869 and N2122.
“We resolved 12 previously predicted N-linked GlcNac in our maps, and four that had not been identified, at N110, N484, N1869 and N212220 (Extended Data Table 3).”
From The structure of human thyroglobulin (2020) · cites this paper as [20]
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Hoofnagle, A. N., Becker, J. O., Wener, M. H., & Heinecke, J. W. (2008) · Clinical Chemistry · doi:10.1373/clinchem.2008.109652 · Cited by 314 · see citing works
The structure of human thyroglobulin
Coscia, F., Taler-Verčič, A., Chang, V. T., Sinn, L., O’Reilly, F. J., Izoré, T., Renko, M., Berger, I., Rappsilber, J., Turk, D., et al. (2020) · Nature · doi:10.1038/s41586-020-1995-4 · Cited by 147 · see citing works
Carvalho, V. M. (2012) · Journal of Chromatography B · doi:10.1016/j.jchromb.2011.08.027 · Cited by 90 · see citing works
- Authors
- Yang, S.-X., Pollock, H. G., & Rawitch, A. B.
- Affiliations
- University of Kansas Medical Center (US)
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 1996-03
- Volume
- 327
- Issue
- 1
- Pages
- 61-70
- ISSN
- 0003-9861 (ISSN-L)
- OpenAlex
- W2130329013
- Cited by
- 68
- References
- 0
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 3 · 2023: 2 · 2022: 4 · 2021: 4 · 2020: 3 · 2019: 6 · 2018: 1 · 2017: 2 · 2016: 2 · 2015: 3 · 2014: 2 · 2013: 2 · 2012: 1
- FWCI
- 0.71
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Archives of Biochemistry and Biophysics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK018896, NIDDK18896)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Disorders and Treatments
- Keywords
- human thyroglobulin, N-glycosylation, glycosylation sites, oligosaccharide structure, complex-type oligosaccharides, high-mannose oligosaccharides, fucose, galactose, glycopeptides, trypsin digestion, beta-turn, bovine thyroglobulin
- MeSH terms
- Amino Acid Sequence, Animals, Carbohydrates, Cattle, Chromatography, Gel, Chromatography, High Pressure Liquid, Chromatography, Ion Exchange, Glycopeptides, Glycosylation, Humans, Molecular Sequence Data, Oligosaccharides, Peptide Fragments, Peptide Mapping, Thyroglobulin, Thyroid Gland, Trypsin, Sequence Homology, Amino Acid, Protein Structure, Secondary
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