Research Article

Extensive analysis of the human platelet proteome by two-dimensional gel electrophoresis and mass spectrometry

  1. Angel García1,*,
  2. Sripadi Prabhakar1,
  3. Chris J. Brock1,
  4. Andrew C. Pearce2,
  5. Raymond A. Dwek1,
  6. Steve P. Watson2,3,
  7. Holger F. Hebestreit1,
  8. Nicole Zitzmann1

Article first published online: 26 JAN 2004

DOI: 10.1002/pmic.200300665

Issue

PROTEOMICS

PROTEOMICS

Volume 4, Issue 3, pages 656–668, March 2004

Additional Information

How to Cite

García, A., Prabhakar, S., Brock, C. J., Pearce, A. C., Dwek, R. A., Watson, S. P., Hebestreit, H. F. and Zitzmann, N. (2004), Extensive analysis of the human platelet proteome by two-dimensional gel electrophoresis and mass spectrometry. PROTEOMICS, 4: 656–668. doi: 10.1002/pmic.200300665

Author Information

  1. 1

    Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, UK

  2. 2

    Department of Pharmacology, University of Oxford, Mansfield Road, Oxford, UK

  3. 3

    Division of Medical Sciences, The Medical School, University of Birmingham, Edgbaston, Birmingham, UK

*Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK Fax: +44-1865-275216

Publication History

  1. Issue published online: 19 FEB 2004
  2. Article first published online: 26 JAN 2004
  3. Manuscript Received: 7 AUG 2003

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Keywords:

  • Electrospray ionisation-tandem mass spectrometry;
  • Platelets;
  • Two-dimensional gel electrophoresis

Abstract

Platelets play a key role in the control of bleeding and wound healing, contributing to the formation of vascular plugs. Under pathologic circumstances, they are involved in thrombotic disorders, including heart disease. Since platelets do not have a nucleus, proteomics offers a powerful alternative approach to provide data on protein expression in these cells, helping to address their biology. In this publication we extend the previously reported analysis of the pI 4–5 region of the human platelet proteome to the pI 5–11 region. By using narrow pI range two-dimensional electrophoresis (2-DE) for protein separation followed by high-throughput tandem mass spectrometry (MS/MS) for protein identification, we were able to identify 760 protein features, corresponding to 311 different genes, resulting in the annotation of 54% of the pI 5–11 range 2-DE proteome map. We evaluated the physicochemical properties and functions of the identified platelet proteome. Importantly, the main group of proteins identified is involved in intracellular signalling and regulation of the cytoskeleton. In addition, 11 hypothetical proteins are reported. In conclusion, this study provides a unique inventory of the platelet proteome, contributing to our understanding of platelet function and building the basis for the identification of new drug targets.

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