Source:http://linkedlifedata.com/resource/pubmed/id/17205978
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
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| pubmed:dateCreated |
2007-4-9
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| pubmed:abstractText |
A gel-based method for a mass spectrometric site-specific glycoanalysis was developed using a recombinant glycoprotein expressed in two different cell lines. Hydrophilic interaction liquid chromatography at nanoscale level was used to enrich for glycopeptides prior to MS. The glycoprofiling was performed using matrix-assisted laser desorption/ionization MS and MS/MS. The method proved to be fast and sensitive and furthermore yielded a comprehensive site-specific glycan analysis, allowing a differentiation of the glycoprofiles of the two sources of recombinant protein, both comprising N-glycans of a highly heterogeneous nature. To test the potential of the method, tissue inhibitor of metalloproteinases-1 (TIMP-1), a secreted low abundance N-glycosylated protein and a cancer marker, was purified in an individual-specific manner from plasma of five healthy individuals using IgG depletion and immunoaffinity chromatography. The corresponding TIMP-1 glycoprofiles were determined to be highly similar, comprising mainly bi- and triantennary complex oligosaccharides. Additionally it was shown that platelet-derived TIMP-1 displayed a similar glycoprofile. This is the first study to investigate the glycosylation of naturally occurring human TIMP-1, and the high similarity of the glycoprofiles showed that individual-specific glycosylation variations of TIMP-1 are minimal. In addition, the results showed that TIMP-1 derived from platelets and plasma is similarly glycosylated. This comprehensive and rapid glycoprofiling of a low abundance glycoprotein performed in an individual-specific manner allows for future studies of glycosylated biomarkers for person-specific detection of altered glycosylation and may thus allow early detection and monitoring of diseases.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
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| pubmed:issn |
1535-9476
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
6
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
638-47
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| pubmed:meshHeading |
pubmed-meshheading:17205978-Amino Acid Sequence,
pubmed-meshheading:17205978-Animals,
pubmed-meshheading:17205978-Blood Platelets,
pubmed-meshheading:17205978-CHO Cells,
pubmed-meshheading:17205978-Cell Line,
pubmed-meshheading:17205978-Chromatography, Affinity,
pubmed-meshheading:17205978-Cricetinae,
pubmed-meshheading:17205978-Cricetulus,
pubmed-meshheading:17205978-Glycosylation,
pubmed-meshheading:17205978-Humans,
pubmed-meshheading:17205978-Peptide Fragments,
pubmed-meshheading:17205978-Plasma,
pubmed-meshheading:17205978-Protein Array Analysis,
pubmed-meshheading:17205978-Proteomics,
pubmed-meshheading:17205978-Recombinant Proteins,
pubmed-meshheading:17205978-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:17205978-Tandem Mass Spectrometry,
pubmed-meshheading:17205978-Tissue Inhibitor of Metalloproteinase-1
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| pubmed:year |
2007
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| pubmed:articleTitle |
Rapid and individual-specific glycoprofiling of the low abundance N-glycosylated protein tissue inhibitor of metalloproteinases-1.
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| pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark.
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| pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|