Research Article

A proteomic analysis of changes in prothrombin and plasma proteins associated with the G20210A mutation

  1. Cecilia Gelfi1,*,
  2. Agnese Viganò1,
  3. Marilena Ripamonti1,
  4. Robin Wait2,
  5. Shajna Begum2,
  6. Eugenia Biguzzi3,
  7. Giancarlo Castaman4,
  8. Elena Maria Faioni5

Article first published online: 30 APR 2004

DOI: 10.1002/pmic.200300724

Issue

PROTEOMICS

PROTEOMICS

Special Issue: Proceedings of the AEPS Meeting, Melbourne, Australia 27-28 September 2003

Volume 4, Issue 7, pages 2151–2159, July 2004

Additional Information

How to Cite

Gelfi, C., Viganò, A., Ripamonti, M., Wait, R., Begum, S., Biguzzi, E., Castaman, G. and Faioni, E. M. (2004), A proteomic analysis of changes in prothrombin and plasma proteins associated with the G20210A mutation. PROTEOMICS, 4: 2151–2159. doi: 10.1002/pmic.200300724

Author Information

  1. 1

    Institute of Molecular Bioimaging and Physiology, CNR, Segrate, Milano, Italy

  2. 2

    Kennedy Institute of Rheumatology, Imperial College London, UK

  3. 3

    Angelo Bianchi Bonomi Hemophilia and Thrombosis Center, Department of Internal Medicine, Milano, Italy

  4. 4

    Division of Hematology, Ospe San Bortolo, Vicenza, Italy

  5. 5

    Hematology and Thrombosis Unit, DMCO-University of Milano and Ospedale San Paolo, Milano, Italy

*Institute of Molecular Bioimaging and Physiology, CNR, Via F.lli Cervi 93, 20090 Segrate, Milano, Italy Fax: +39-02-21717558

Publication History

  1. Issue published online: 22 JUN 2004
  2. Article first published online: 30 APR 2004
  3. Manuscript Received: 25 SEP 2003

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Keywords:

  • Proteome;
  • Prothrombin;
  • Thrombosis;
  • Two-dimensional map

Abstract

The G→A mutation at position 20210 of the prothrombin gene, localized in the 3'-polyadenylation untranslated region of the mRNA, is a recognized genetic risk factor for venous thromboembolism. The mechanism by which this base change confers an increased risk of thrombosis compared to noncarriers is undefined. Studies on the mRNA suggest enhanced cleavage site recognition and a change in the location of the 3'-cleavage/polyadenylation reaction, but no defined model has been proposed. The present study, based on proteomic investigation by two-dimensional gel electrophoresis and electrospray ionization (ESI) tandem mass spectrometry (MS/MS) protein identification, suggests that the G20210A mutation is associated with increased glycosylation of prothrombin, which confers greater stability to the protein. Additionally, proteomic investigation of pooled plasma showed that expression levels of six spots, three of them identified by ESI MS/MS, were altered in subjects carrying the mutation, suggesting a possible cooperative effect in the thrombotic risk increment induced by the mutation.

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