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

被引：20

作者：

Hennebicq S. ^{[1
]}

Tetaert D. ^{[1
]}

Soudan B. ^{[1
,2
]}

Boersma A. ^{[1
,2
]}

Briand G. ^{[3
]}

Richet C. ^{[1
]}

Gagnon J. ^{[4
]}

Degand P. ^{[1
]}

机构：

[1] Unité INSERM N 377, Bâtiment G. BISERTE, 59045 Lille Cédex, Place de Verdun

[2] Lab. de Biochimie et Endocrinologie, USN A, 59045 Lille Cédex

[3] Serv. Commun Spectrometrie de Masse, Université de Lille II, Faculté de Médecine, 59045 Lille Cédex, Place de Verdun

[4] Institut de Biologie Structurale, CEA/CNRS, 38027 Grenoble Cédex

来源：

Glycoconjugate Journal | 1998年 / 15卷 / 3期

关键词：

Capillary electrophoresis; Edman degradation; Gastric mucosa; MUC5AC; Mucin; O-Glycosylation; UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase;

D O I：

10.1023/A:1006949129456

中图分类号：

学科分类号：

摘要：

The present work was carried out to study the role of the peptide moiety in the addition of O-linked N-acetylgalactosamine to human apomucin using human crude microsomal homogenates from gastric mucosa (as enzyme source) and a series of peptide accepters 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.

引用

页码：275 / 282

页数：7

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