Different O-glycosylation of respiratory mucin glycopeptides from a patient with cystic fibrosis
| 详细信息 | 推荐本文 | |
- 作者：Kristina A Thomsson ; Ingemar Carlstedt ; Niclas G Karlsson ; Hasse Karlsson and Gunnar C Hansson
- 关键词：mucin ; cystic fibrosis ; oligosaccharides ; MALDI ; GC ; MS ; CF ; cystic fibrosis ; GalNAcol ; N ; acetylgalactosaminitol ; Hex ; hexose ; HexNAc ; N ; acetylhexosamine ; HexNAcol ; GC ; gas chromatography ; MALDI ; matrix ; assisted laser ; FAB ; fast atom bombardmen
- 刊名：Glycoconjugate Journal
- 出版时间：1998
- 出版年：1998
- 期刊代码：11_02820080
- 类别：env
- 卷：15
- 期：8
- 页码：823-833
- 数据来源：sp
摘要
The O-linked oligosaccharides from three fractions of highly glycosylated mucin glycopeptides obtained from sputum of a patient with cystic fibrosis were characterized and compared regarding size, composition, sequence and when possible linkage positions. Neutral and sialic acid-containing glycans were permethylated and analyzed by high-temperature GC-MS and MALDI-MS, showing more than 60 different oligosaccharides with a size of up to 15 monosaccharide units. Some of the observed oligosaccharides are novel for respiratory secretions, one being a trifucosylated heptasaccharide with the proposed structure: Fuc-Gal-4(Fuc-3)GlcNAc-(Fuc-)Gal-3GalNAcol. The glycosylation of two of the glycopeptide fractions was similar with regard to the neutral and sialylated oligosaccharides despite their different origins from the sol or gel phase. Analysis of the sulfated oligosaccharides by FAB-MS/MS indicated that the gel fraction contained C-6 linked sulfate groups while the two sol fractions also contained C-3 linked sulfate. The results suggest the presence of different glycosylated mucin domains, probably originating from different mucin glycoforms and/or apoproteins in the airway of cystic fibrosis patients.