Mass Spectrometry Letters

Korean Society for Mass Spectrometry (한국질량분석학회)
권호 표지
DOI QR코드

DOI QR Code

An Application of Electrostatic Repulsion Hydrophilic Interaction Chromatography in Phospho- and Glycoproteome Profiling of Epicardial Adipose Tissue in Obesity Mouse

  • Tran, Trang Huyen (Lee Gil Ya Cancer and Diabetes Institute, Gachon University) ;
  • Hwang, In-Jae (Institute of Molecular Biology and Genetics School of Biological Sciences, Seoul National University) ;
  • Park, Jong-Moon (Lee Gil Ya Cancer and Diabetes Institute, Gachon University) ;
  • Kim, Jae-Bum (Institute of Molecular Biology and Genetics School of Biological Sciences, Seoul National University) ;
  • Lee, Hoo-Keun (Lee Gil Ya Cancer and Diabetes Institute, Gachon University)
  • Received : 2012.05.07
  • Accepted : 2012.05.20
  • Published : 2012.06.28
Download PDF
⟨ Previous Next ⟩

Abstract

Phosphorylation and glycosylation are two of the most important and widespread post-translational modifications (PTMs) in an organism. Proteomics analysis of the PTMs has been challenged by low stoichiometry of the modified proteins and suppression effects by high abundance proteins, typically no-functional house-keeping proteins. In this study, a novel method was applied for not only isolating PTM peptides from intact peptides but also concurrently characterizing of glyco- and phosphoproteome using electrostatic repulsion hydrophilic interaction chromatography (ERLIC) packed with silica coated by crosslinked polyethyleneimine. For 2 mg tryptic digest of mouse proteome of epicardial adipose tissue with fat diet, 802 N-glycosylated peptides of 316 glycoproteins and 159 phosphorylated peptides of 75 phosphoproteins were identified using HPLC chip/quadrupole time-of-flight (Q-OF) tandem mass spectrometer.

Keywords

References

  1. Cohen, P. Trends Biochem. Sci. 2000, 25, 596. https://doi.org/10.1016/S0968-0004(00)01712-6
  2. Apweiler, R; Hermjakob, H.; Sharon, N. Biochim. Biophys. Acta 1999, 1473, 4. https://doi.org/10.1016/S0304-4165(99)00165-8
  3. Dennis, J. W.; Granovsk, M.; Warren, C. E. Bio Essays 1999, 21, 412.
  4. Durand, G.; Seta, N. Clin. Chem. 2000, 46, 795.
  5. Cohen, P. Eur. J. Biochem. 2001, 268, 5001. https://doi.org/10.1046/j.0014-2956.2001.02473.x
  6. Hood, L. Mech. Ageing Dev. 2003, 124, 9. https://doi.org/10.1016/S0047-6374(02)00164-1
  7. Aebersold, R.; Cravatt, B. F. Trends Biotechnol. 2002, 20, 1. https://doi.org/10.1016/S0167-7799(01)01871-6
  8. Ballif, B. A.; Villen, J.; Beausoleil, S. A.; Schwartz, D.; Gygi, S. P. Mol. Cell Proteomics 2004, 3, 1093. https://doi.org/10.1074/mcp.M400085-MCP200
  9. Lewandrowski, U.; Zahedi, R. P.; Moebius, J.; Walter, U.; Sickmann, A. Mol. Cell Proteomics 2007, 6, 1933. https://doi.org/10.1074/mcp.M600390-MCP200
  10. Gan, C. S.; Guo, T.; Zhang, H.; Lim, S. K.; Sze, S. K. J. Proteome Res. 2008, 7, 4869. https://doi.org/10.1021/pr800473j
  11. Alpert, A. J. Anal Chem. 2008, 80, 62. https://doi.org/10.1021/ac070997p
  12. Lewandrowski, U. L. K.; Zahedi, R.; Walter, D.; Sickmann, A. Clin. Proteomics 2008, 4, 25. https://doi.org/10.1007/s12014-008-9006-z
  13. Zhang, H.; Guo, T.; Li, X.; Datta, A.; Park, J. E.; Yang, J.; Lim, S. K.; Tam J. P.; Sze, S. K. Mol. Cell Proteomic 2010, 9, 635. https://doi.org/10.1074/mcp.M900314-MCP200
  14. Hao, P.; Guo, T.; Sze S. K. Plos One 2011, 6, 1.
  15. Tian, Y.; Zhou, Y.; Elliott, S.; Aebersold, R.; Zhang, H. Nat. Protoc. 2007, 2, 334. https://doi.org/10.1038/nprot.2007.42
  16. Ahmed, M.; Neville M. J.; Edelmann, M. J.; Kessler, B. M.; Karpe, F. Obesity (Silver Spring) 2010, 18, 27. https://doi.org/10.1038/oby.2009.208
  17. Schaub, N. P.; Jones, K. J.; Nyalwidhe, J. O.; Cazares, L. H.; Karbassi, I.D.; Semmes, O. J.; Feliberti, E. C.; Perry, R. R.; Drake, R. R. J. Am. Coll. Surg. 2009, 208, 970. https://doi.org/10.1016/j.jamcollsurg.2008.12.024
  18. Mareckova, Z.; Heller, S.; Horky, K. Vnitr Lek 1999, 45, 46.

Cited by

  1. Interaction modes and approaches to glycopeptide and glycoprotein enrichment vol.139, pp.4, 2014, https://doi.org/10.1039/C3AN01813J
  2. The Use of Electrostatic Repulsion-Hydrophilic Interaction Chromatography (ERLIC) for Proteomics Research vol.5, pp.4, 2014, https://doi.org/10.5478/MSL.2014.5.4.95