2012 Fiscal Year Final Research Report
The molecular basis of interactions between cancer cells and neurons in glioma invasion
Project/Area Number |
22700375
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Single-year Grants |
Research Field |
Nerve anatomy/Neuropathology
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Research Institution | The University of Tokyo |
Principal Investigator |
SHUO Takuya 東京大学, 医科学研究所, 特任研究員 (90399006)
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Project Period (FY) |
2010 – 2012
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Keywords | 脳腫瘍 / 神経膠腫細胞 / 神経細胞 / メタロプロテアーゼ / プロテオグリカン / 糖鎖 / 質量分析 / MALDI(マトリックス支援レーザー脱離イオン化法) |
Research Abstract |
To understand the molecular basis of interactions between glioma and neurons, we investigated the role of MT-MMP/neuroglycan C axis. In this study, we found that a recombinant MT-MMP catalytic domain could actually cleave full-length neuroglycan C in two fragments. In addition, we developed a new MALDI-mass spectrometric technique to analyze glycopeptides in a highly sensitive manner, and then we used the method to evaluate glycosylation status of MT-MMP.
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[Journal Article] MZF21 protein, a regulator of the disassembly of focal adhesions and cancer metastasis contains a novel noncanonical pleckstrin homology domain2013
Author(s)
Nagano M, Hoshino D, Koshiba S, Shuo T, Koshikawa N, Tomizawa T, Hayashi F, Tochio N, Harada T, Akizawa T, Watanabe S, Handa N, Shirouzu M, Kigawa T, Yokoyama S, Seiki
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Journal Title
J Biol Chem
Volume: 286巻
Pages: 1598-31609
DOI
Peer Reviewed
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[Presentation] Glycan characterization of MT1-MMP2011
Author(s)
Takuya Shuo
Organizer
an invasion-promoting metalloproteinase, by MALDI-digital ion trap mass spectrometrySeventh General Meeting of the International Proteolysis Society
Place of Presentation
Hilton San Diego Resort and Spa(San Diego/USA)
Year and Date
2011-10-19
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