Abstract
The N-linked glycans on transferrin and alpha(1)-antitrypsin from patients with congenital disorders of glycosylation type I have increased fucosylation and branching relative to normal controls. The elevated levels of monofucosylated biantennary glycans are probably due to increased alpha-(1-->6) fucosylation. The presence of bi- and trifucosylated triantennary and tetra-antennary glycans indicated that peripheral alpha-(1-->3), as well as core alpha-(1-->6), fucosylation is increased. Altered processing was observed on both the fully and underglycosylated glycoforms.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amidohydrolases
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Carbohydrate Metabolism, Inborn Errors / classification
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Carbohydrate Metabolism, Inborn Errors / metabolism*
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Carbohydrate Sequence
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Case-Control Studies
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Electrophoresis, Gel, Two-Dimensional
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Fucose / chemistry
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Fucose / metabolism
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Glycosylation
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Humans
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Molecular Sequence Data
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Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
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Polysaccharides / chemistry
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Polysaccharides / metabolism*
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Protein Processing, Post-Translational
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Transferrin / chemistry
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Transferrin / metabolism
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alpha 1-Antitrypsin / chemistry
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alpha 1-Antitrypsin / metabolism
Substances
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Polysaccharides
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Transferrin
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alpha 1-Antitrypsin
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Fucose
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Amidohydrolases
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Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase