| pubmed-article:17205978 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17205978 | lifeskim:mentions | umls-concept:C0040300 | lld:lifeskim |
| pubmed-article:17205978 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:17205978 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:17205978 | lifeskim:mentions | umls-concept:C0205251 | lld:lifeskim |
| pubmed-article:17205978 | lifeskim:mentions | umls-concept:C0439831 | lld:lifeskim |
| pubmed-article:17205978 | lifeskim:mentions | umls-concept:C2346714 | lld:lifeskim |
| pubmed-article:17205978 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:17205978 | pubmed:dateCreated | 2007-4-9 | lld:pubmed |
| pubmed-article:17205978 | 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. | lld:pubmed |
| pubmed-article:17205978 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17205978 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17205978 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17205978 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17205978 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17205978 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17205978 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17205978 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:17205978 | pubmed:issn | 1535-9476 | lld:pubmed |
| pubmed-article:17205978 | pubmed:author | pubmed-author:BrünnerNilsN | lld:pubmed |
| pubmed-article:17205978 | pubmed:author | pubmed-author:NielsenHans... | lld:pubmed |
| pubmed-article:17205978 | pubmed:author | pubmed-author:HøjrupPeterP | lld:pubmed |
| pubmed-article:17205978 | pubmed:author | pubmed-author:ThøgersenIda... | lld:pubmed |
| pubmed-article:17205978 | pubmed:author | pubmed-author:EnghildJan... | lld:pubmed |
| pubmed-article:17205978 | pubmed:author | pubmed-author:LademannUlrik... | lld:pubmed |
| pubmed-article:17205978 | pubmed:author | pubmed-author:Thaysen-Ander... | lld:pubmed |
| pubmed-article:17205978 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17205978 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:17205978 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17205978 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17205978 | pubmed:pagination | 638-47 | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:meshHeading | pubmed-meshheading:17205978... | lld:pubmed |
| pubmed-article:17205978 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17205978 | pubmed:articleTitle | Rapid and individual-specific glycoprofiling of the low abundance N-glycosylated protein tissue inhibitor of metalloproteinases-1. | lld:pubmed |
| pubmed-article:17205978 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark. | lld:pubmed |
| pubmed-article:17205978 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17205978 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:17205978 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17205978 | lld:pubmed |
