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Proteomic Analysis Reveals Drug Accessible Cell Surface N-Glycoproteins of Primary and Established Glioblastoma Cell Lines
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2012 (English)In: Journal of Proteome Research, ISSN 1535-3893, E-ISSN 1535-3907, Vol. 11, no 10, 4885-4893 p.Article in journal (Refereed) Published
Abstract [en]

Glioblastoma is the most common primary Glioblastoma Cell Surface Capturing brain tumor in adults with low average survival time after diagnosis. In order to improve glioblastoma treatment, new drug-accessible targets need to be identified. Cell surface glycoproteins are prime drug targets due to their accessibility at the surface of cancer cells. To overcome the limited availability of suitable antibodies for cell surface protein detection, we performed a comprehensive mass spectrometric investigation of the glioblastoma surfaceome. Our combined cell surface capturing analysis of primary ex vivo glioblastoma cell lines in combination with established glioblastoma cell lines revealed 633 N-glycoproteins, which vastly extends the known data of surfaceome drug targets at subcellular resolution. We provide direct evidence of common glioblastoma cell surface glycoproteins and an approximate estimate of their abundances, information that could not be derived from genomic and/or transcriptomic glioblastoma studies. Apart from our pharmaceutically valuable repertoire of already and potentially drug-accessible cell surface glycoproteins, we built a mass-spectrometry-based toolbox enabling directed, sensitive, and repetitive glycoprotein measurements for clinical follow-up studies. The included Skyline Glioblastoma SRM assay library provides an elevated starting point for parallel testing of the abundance level of the detected glioblastoma surfaceome members in future drug perturbation experiments.

Place, publisher, year, edition, pages
2012. Vol. 11, no 10, 4885-4893 p.
Keyword [en]
glioblastoma, N-glycoproteins, cell surface accessible drug targets, cell surface capturing, N-glycoproteome SRM library
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:kth:diva-104700DOI: 10.1021/pr300360aISI: 000309441000011ScopusID: 2-s2.0-84867449353OAI: diva2:567080
EU, European Research Council, ERC-2008-AdG 233226Science for Life Laboratory - a national resource center for high-throughput molecular bioscience

QC 20121112

Available from: 2012-11-12 Created: 2012-11-09 Last updated: 2012-11-12Bibliographically approved

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Lundberg, EmmaUhlén, Mathias
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Proteomics (closed 20130101)Science for Life Laboratory, SciLifeLab
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