The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation
Open accessAbstract
Mucin-type O-linked glycoproteins are involved in a variety of biological interactions in higher eukaryotes. The biosynthesis of these glycoproteins is initiated by a family of polypeptide N -acetyl-α-galactosaminyltransferases (ppGalNAcTs) that modify proteins in the secretory pathway. The lack of a defined consensus sequence for the ppGalNAcTs makes the prediction of mucin-type O-linked glycosylation difficult based on primary sequence alone. Herein we present a method for labeling mucin-type O-linked glycoproteins with a unique chemical tag, the azide, which permits their selective covalent modification from complex cell lysates. From a panel of synthetic derivatives, we identified an azido GalNAc analog ( N -azidoacetylgalactosamine, GalNAz) that is metabolized by numerous cell types and installed on mucin-type O-linked glycoproteins by the ppGalNAcTs. The azide serves as a bioorthogonal chemical handle for selective modification with biochemical or biophysical probes using the Staudinger ligation. The approach was validated by labeling a recombinant glycoprotein that is known to possess O-linked glycans with GalNAz. In addition, GalNAz efficiently labeled mucin-type O-linked glycoproteins expressed at endogenous levels. The ability to label mucin-type O-linked glycoproteins with chemical tags should facilitate their identification by proteomic strategies.
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Self-citationConcepts and Principles of O-Linked Glycosylation
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Cited by
Bioorthogonal Chemistry: Fishing for Selectivity in a Sea of Functionality
Sletten, E. M., & Bertozzi, C. R. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200900942 · Cited by 3,165
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Click Chemistry in Proteomic Investigations
Parker, C. G., & Pratt, M. R. (2020) · Cell · doi:10.1016/j.cell.2020.01.025 · Cited by 380
Advances in mass spectrometry driven O-glycoproteomics
Levery, S. B., Steentoft, C., Halim, A., Narimatsu, Y., Clausen, H., & Vakhrushev, S. Y. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.09.026 · Cited by 111
Metadata
- Authors
- Hang, H. C., Yu, C., Kato, D. L., & Bertozzi, C. R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2003-12
- Volume
- 100
- Issue
- 25
- Pages
- 14846-14851
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2118002029
- Cited by
- 580
- References
- 43
- FWCI
- 3.11
- Type
- journal article
- Language
- en
- Open access
- green
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- Hang, H. C., Yu, C., Kato, D. L., & Bertozzi, C. R. (2003). A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.2335201100
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