- P-ISSN 2233-4203
- E-ISSN 2093-8950
- P-ISSN2233-4203
- E-ISSN2093-8950
- ESCI, SCOPUS, KCI
Article Detail
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Nitrated Proteome in Human Embryonic Stem Cells
Mass Spectrometry Letters / Mass Spectrometry Letters, (P)2233-4203; (E)2093-8950
2016, v.7 no.4, pp.85-90
https://doi.org/10.5478/MSL.2016.7.4.85
(Kyung Hee University)
(Institute for Basic Science)
(Kyung Hee University)
(Institute for Basic Science)
(Kyung Hee University)
Kang,
J. W., Hwang,
D., &
Kim,
K.
P.
(2016). Nitrated Proteome in Human Embryonic Stem Cells. Mass Spectrometry Letters, 7(4), 85-90, https://doi.org/10.5478/MSL.2016.7.4.85
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Abstract
Post-translational modifications (PTMs) of proteins regulate self-renewal and differentiation in embryonic stem cells (ESCs). Nitration of tyrosine residues of proteins in ESCs modulates their downstream pathways, which can affect self-renewal and differentiation. However, protein tyrosine nitration (PTN) in ESCs has been rarely studied. We reviewed 23 nitrated sites in stem cell proteins. Functional enrichment analysis showed that these nitrated proteins are involved in signal transduction, cell adhesion and migration, and cell proliferation in ESCs. Comparison between the nitrated and known phosphorylated sites revealed that 7 nitrated sites had overlapping phosphorylated sites, indicating functional links of PTNs to their associated signaling pathways in ESCs. Therefore, nitrated proteome provides a basis for understanding potential roles of PTN in self-renewal and differentiation of ESCs.
- keywords
- Tyrosine nitration, Nitrotyrosine enrichment, LC-MS/MS, Proteomics, Embryonic stem cells
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- Submission Date
- 2016-12-05
- Revised Date
- 2016-12-22
- Accepted Date
- 2016-12-22
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