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PMID: 9579804 Published · ppublish English Journal Article

Influence of the amino acid sequence on the MUC5AC motif peptide O-glycosylation by human gastric UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase(s).

Glycoconjugate journal ·Vol. 15 ·No. 3 ·1998-03-00 ·Pages 275-82

Hennebicq S, Tetaert D, Soudan B, Boersma A, Briand G, Richet C, Gagnon J, Degand P

Abstract

The present work was carried out to study the role of the peptide moiety in the addition of O-linked N-acetylgalactosamineto human apomucin using human crude microsomal homogenates from gastric mucosa (as enzyme source) and a series of peptide acceptors representative of tandem repeat domains deduced from the MUC5AC mucin gene (expressed in the gastric mucosa). Being rich in threonine and serine placed in clusters, these peptides provided several potential sites for O-glycosylation. The glycosylated products were analysed by a combination of electrospray mass spectrometry and capillary electrophoresis in order to isolate the glycopeptides and to determine their sequence by Edman degradation. The O-glycosylation of our MUC5AC motif peptides gave information on the specificity and activity of the gastric microsomal UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase(s). The proline residues and the induced-conformations are of great importance for the recognition of MUC5AC peptides but they are not the only factors for the choice of the O-glycosylation sites. Moreover, for the di-glycosylated peptides, the flanking regions of the proline residues strongly influence the site of the second O-glycosylation.

MeSH Terms
Amino Acid Sequence Binding Sites Gastric Mucosa/enzymology Glycosylation Humans In Vitro Techniques Microsomes/enzymology Molecular Sequence Data Mucin 5AC Mucins/chemistry,metabolism N-Acetylgalactosaminyltransferases/metabolism Oligopeptides/chemistry,metabolism Protein Conformation Substrate Specificity
Chemicals
MUC5AC protein, human Mucin 5AC Mucins Oligopeptides N-Acetylgalactosaminyltransferases polypeptide N-acetylgalactosaminyltransferase
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Hennebicq S
Unité INSERM N 377, Lille, France.
Tetaert D
Soudan B
Boersma A
Briand G
Richet C
Gagnon J
Degand P
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Article Info
Journal
Glycoconjugate journal
Abbr.
Glycoconj J
ISSN
0282-0080
DOI
10.1023/a:1006949129456
Published
1998-03-00
Pages
275-82
Language
English
Region
United States
NLM ID
8603310
Subset
IM
External Links
PubMed source DOI: 10.1023/a:1006949129456 View journal details
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