Glycopeptide N-acetylgalactosaminyltransferase specificities for O-glycosylated sites on MUC5AC mucin motif peptides
Open accessAbstract
The recombinant proteins of the two novel UDP-N-acetylgalactosamine (GalNAc) glycopeptide:N-acetylgalactosaminyltransferases (designated gpGaNTase-T7 and gpGaNTase-T9) were assayed with O-glycosylated products obtained from the prior action of the ubiquitous transferases (GaNTase-T1 and GaNTase-T2) towards MUC5AC mucin motif peptides (GTTPSPVPTTSTTSAP and peptides with single amino acid substitutions, GTTPSAVPTTSTTSVP and GTTPSPVPTTSITSVP, that are a reflection of mucin molecule polymorphism). gpGaNTase-T9 is known to be expressed differentially and more abundantly than gpGaNTase-T7 in some tissues; the results of in vitro glycosylation also indicates a difference in acceptor substrate specificities between the gpGaNTase isoforms. With the use of capillary electrophoresis, MS and Edman degradation, our study suggests that, in the O-glycosylation of mucin-type proteins, approach and recognition signalling by gpGaNTase-T7 and gpGaNTase-T9 depend largely on the peptide's primary structure (for example the presence of multiple clusters of hydroxy amino acids and the number of GalNAc residues attached to the peptide backbone). O-glycosylation in terms of sites of attachment seems to be less random than previously described and, if sequential reactions are ordered throughout the Golgi stack, the complete O-glycosylation of the mucin molecules seems to be finely tuned to respond to specific damage to, or attack on, epithelia.
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Previous in vitro studies with GalNAc-T2 have identified Thr9 in the MUC5AC peptide as a preferred glycosylation site.
“Previous in vitro studies with GalNAc-T2 have identified Thr7 in the synthetic EA2 peptide sequence [14, 15] and Thr9 in the MUC5AC peptide as preferred glycosylation sites [31].”
From High level in vivo mucin-type glycosylation in Escherichia coli (2018) · cites this paper as [31]
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High level in vivo mucin-type glycosylation in Escherichia coli
Mueller, P., Gauttam, R., Raab, N., Handrick, R., Wahl, C., Leptihn, S., Zorn, M., Kussmaul, M., Scheffold, M., Eikmanns, B., et al. (2018) · Microbial Cell Factories · doi:10.1186/s12934-018-1013-9 · Cited by 22 · see citing works
- Authors
- TETAERT, D., TEN HAGEN, K. G., RICHET, C., BOERSMA, A., GAGNON, J., & DEGAND, P.
- Affiliations
- Unité INSERM No. 377, Biologie et Physiopathologie de Cellules Mucipares, Place de Verdun, 59045 Lille Cédex, France
- Center for Oral Biology, Aab Institute for Biomedical Sciences, University of Rochester, 601 Elmwood Avenue, Box 611, Rochester, NY 14642, U.S.A.
- Inserm (FR)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- RICHET, Colette
- BOERSMA, Arnold
- DEGAND, Pierre
- ORCID
- GAGNON, Jean
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2001-06-25
- Volume
- 357
- Issue
- 1
- Pages
- 313-320
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1221957
- OpenAlex
- W2023618350
- Cited by
- 31
- References
- 28
- Citations by year
- 2026: 1 · 2024: 1 · 2022: 1 · 2018: 1 · 2017: 1 · 2015: 1 · 2012: 1
- FWCI
- 1.40
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Keywords
- N-acetylgalactosaminyltransferase, O-glycosylation, MUC5AC mucin, acceptor substrate specificity, Golgi glycosylation
- MeSH terms
- Amino Acid Sequence, Animals, Chlorocebus aethiops, Glycosylation, Isoenzymes, Kinetics, Molecular Sequence Data, Mucins, Peptide Fragments, Peptides, Recombinant Proteins, Substrate Specificity, Transfection, N-Acetylgalactosaminyltransferases, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, COS Cells, Mucin 5AC
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