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  • P-ISSN 2233-4203
  • E-ISSN 2093-8950

Quantitative Phosphoproteomics of the Human Neural Stem Cell Differentiation into Oligodendrocyte by Mass Spectrometry

Mass Spectrometry Letters / Mass Spectrometry Letters, (P)2233-4203; (E)2093-8950
2012, v.3 no.4, pp.93-100
https://doi.org/10.5478/MSL.2012.3.4.93
Kun Cho (Korea Basic Science Institute)
Jin Young Kim (Korea Basic Science Institute)
Eunmin Kim (Korea Basic Science Institute)
Gun Wook Park (Korea Basic Science Institute)
Tae Wook Kang (Korea Basic Science Institute)
Jung Hae Yoon (Research Institute at Nationwide Childre)
Seung U. Kim (University of British Columbia)
Kyunghee Byun (Gachon University)
Bonghee Lee (Gachon University)
Jong Shin Yoo (Korea Basic Science Institute, Republic of Korea)
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Abstract

Cellular processes such as proliferation, differentiation, and adaptation to environmental changes are regulated byprotein phosphorylation. In order to enhance the understanding of molecular dynamics for biological process in detail, it is necessaryto develop sensitive and comprehensive analytical methods for the determination of protein phosphorylation. Neural stemcells hold great promise for neural repair following an injury or disease. In this study, we made differentiated oligodendrocytesfrom human neural stem cells using over-expression of olig2 gene. We confirmed using quantitative phosphoproteome analysisapproach that combines stable isotope labeling by amino acids in cell culture (SILAC) and TiO2 micro-column for phosphopeptideenrichment with MS2 and MS3 mass spectrometry. We detected 275 phosphopeptides which were modulated at least 2-foldbetween human neural stem cells and oligodendrocytes. Among them, 23 phosphoproteins were up-regulated in oligodendrocytesand 79 phosphoproteins were up-regulated in F3 cells.

keywords
Phosphoproteomics, TiO2, SILAC, LTQ-FT MS, Neural Stem Cell (NSC), Oligodendrocyte


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투고일Submission Date
2012-12-07
수정일Revised Date
2012-12-24
게재확정일Accepted Date
2012-12-24
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