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Different O-glycosylation of respiratory mucin glycopeptides from a patient with cystic fibrosis.

Journal article
Authors Kristina A Thomsson
I Carlstedt
Niclas G. Karlsson
Hasse Karlsson
Gunnar C. Hansson
Published in Glycoconjugate journal
Volume 15
Issue 8
Pages 823-33
ISSN 0282-0080
Publication year 1998
Published at Institute of Medical Biochemistry
Pages 823-33
Language en
Keywords Adolescent, Carbohydrate Sequence, Chromatography, High Pressure Liquid, Cystic Fibrosis, Female, Gas Chromatography-Mass Spectrometry, Glycopeptides, chemistry, Glycosylation, Humans, Molecular Sequence Data, Mucins, chemistry, Oligosaccharides, chemistry, Sequence Analysis, Spectrometry, Mass, Fast Atom Bombardment, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Sputum, chemistry, Sulfuric Acid Esters
Subject categories Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)


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.

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