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http://purl.uniprot.org/citations/15863355http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15863355http://www.w3.org/2000/01/rdf-schema#comment"

Background

alpha(1)-Acid glycoprotein (AGP), an acute phase reactant, is extensively glycosylated at five Asn-linked glycosylation sites. In a number of pathophysiological states, including inflammation, rheumatoid arthritis, and cancer, alterations of Asn-linked glycans (N-glycans) have been reported. We investigated alteration of N-glycans at each of glycosylation sites of AGP in the sera of patients with acute and chronic inflammation.

Methods

AGP purified from sera was digested with Glu-C and the liberated glycopeptides were isolated by reverse phase HPLC. N-glycans released with peptide N-glycosidase F and followed by neuraminidase treatment were analyzed by matrix-assisted laser desorption ionization-time of flight mass spectrometry.

Results

Site-specific differences in branching structures were observed among N-glycosylation sites 1, 3, 4 and 5. Within the sera of patients with acute inflammation, increases in bi-antennary and decreases in tri- and tetra-antennary structures were observed, as well as increases in alpha1,3-fucosylation, at most glycosylation sites. In the sera of patients with chronic inflammation, increased rates of tri-antennary alpha1,3-fucosylation at sites 3 and 4 and tetra-antennary alpha1,3-fucosylation at sites 3, 4 and 5 were detected. Although there were no significant differences between acute and chronic sera in site directed branching structures, significant differences of alpha1,3-fucosylation were detected in tri-antennary at sites 2, 4 and 5 and in tetra-antennary at sites 3 and 4.

Conclusion

Little variation in the N-glycan composition of the glycosylation sites of AGP was observed among healthy individuals, while the sera of patients with acute inflammation demonstrated increased numbers of bi-antennary and alpha1,3-fucosylated N-glycan structures at each glycosylation site."xsd:string
http://purl.uniprot.org/citations/15863355http://purl.org/dc/terms/identifier"doi:10.1016/j.bbagen.2005.03.012"xsd:string
http://purl.uniprot.org/citations/15863355http://purl.uniprot.org/core/author"Matsumoto K."xsd:string
http://purl.uniprot.org/citations/15863355http://purl.uniprot.org/core/author"Azuma Y."xsd:string
http://purl.uniprot.org/citations/15863355http://purl.uniprot.org/core/author"Aoki Y."xsd:string
http://purl.uniprot.org/citations/15863355http://purl.uniprot.org/core/author"Higai K."xsd:string
http://purl.uniprot.org/citations/15863355http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15863355http://purl.uniprot.org/core/name"Biochim Biophys Acta"xsd:string
http://purl.uniprot.org/citations/15863355http://purl.uniprot.org/core/pages"128-135"xsd:string
http://purl.uniprot.org/citations/15863355http://purl.uniprot.org/core/title"Glycosylation of site-specific glycans of alpha1-acid glycoprotein and alterations in acute and chronic inflammation."xsd:string
http://purl.uniprot.org/citations/15863355http://purl.uniprot.org/core/volume"1725"xsd:string
http://purl.uniprot.org/citations/15863355http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15863355
http://purl.uniprot.org/citations/15863355http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15863355
http://purl.uniprot.org/uniprot/#_B4E1B5-mappedCitation-15863355http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15863355
http://purl.uniprot.org/uniprot/#_P19652-mappedCitation-15863355http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15863355
http://purl.uniprot.org/uniprot/B4E1B5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15863355
http://purl.uniprot.org/uniprot/P19652http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15863355