Thromb Haemost 2006; 96(03): 302-308
DOI: 10.1160/TH06-03-0138
Blood Coagulation, Fibrinolysis and Cellular Haemostasis
Schattauer GmbH

Identification of a new truncated form and deamidation products of fibrinopeptide B released by thrombin from human fibrinogen

Barbara Cardinali
1   S.S. Proteomica, Istituto Nazionale per la Ricerca sul Cancro, Genova
2   Dipartimento di Chimica e Chimica Industriale, Università di Genova, Genova
,
Gianluca Damonte
3   Dipartimento di Medicina Sperimentale e Centro di Eccellenza per la Ricerca Biomedica, Università di Genova, Genova
,
Luca Melone
3   Dipartimento di Medicina Sperimentale e Centro di Eccellenza per la Ricerca Biomedica, Università di Genova, Genova
,
Annalisa Salis
3   Dipartimento di Medicina Sperimentale e Centro di Eccellenza per la Ricerca Biomedica, Università di Genova, Genova
,
Francesca Tosetti
4   S.C. Oncologia Sperimentale A, Istituto Nazionale per la Ricerca sul Cancro, Genova, Italy
,
Mattia Rocco
1   S.S. Proteomica, Istituto Nazionale per la Ricerca sul Cancro, Genova
,
Aldo Profumo
1   S.S. Proteomica, Istituto Nazionale per la Ricerca sul Cancro, Genova
› Institutsangaben

Financial support: This study was partially supported by a FIRB RBAU01R5SE grant from the Ministero Università Ricerca Scientifica Tecnologica (MURST), Italy.
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Publikationsverlauf

Received 07. März 2006

Accepted after resubmission 17. Juli 2006

Publikationsdatum:
30. November 2017 (online)

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Summary

Quantification of fibrinopeptides release is widely used to investigate fibrinogen activation, and standard chromatographic or capillary electrophoretic procedures are readily available. However, in the analyses of fibrinopeptide mixtures derived from the action of thrombin on human fibrinogen, a few unidentified peaks are usually present. The composition of these peaks was studied by reverse-phase HPLC/MS, revealing a single major anomalous peptide having a molecular mass of 1384.4. A further MS/MS analysis allowed the identification of this form, as a Nterminally truncated fibrinopeptideB (fpB) lacking the first two residues (pyroglutamic acid and glycine). This previously unidentified, relatively low-abundance form (∼7%) has been found consistently in our fibrinopeptides preparations, and analysis of the parent Bβ-chain suggest that it is likely present in circulating fibrinogen. In addition, deamidated forms of all fpB species (including desArgB), resulting from the conversion of asparagine to aspartic acid, were also identified. Overall, these previously unreported forms constitute a substantial amount of fpB (up to ∼17% of the total), and should be taken into account for a reliable quantitative analysis of fpB release.