The N-terminal 1-16 peptide derived in vivo from protein seminal vesicle protein IV modulates α-thrombin activity: Potential clinical implications

Marilena Lepretti, Susan Costantini, Gaetano Ammirato, Gaia Giuberti, Michele Caraglia, Angelo M. Facchiano, Salvatore Metafora, Paola Stiuso

Research output: Contribution to journalArticle

Abstract

We have previously shown that seminal vesicle protein IV (SV-IV) and its 1-70 N-terminal fragment have anti-inflammatory activity and modulate anti-thrombin III (AT) activity. Moreover, mass spectrometry analysis of purified SV-IV has shown that the protein was found to be highly heterogeneous and 14% of the total SV-IV molecules are truncated forms, of particular interest the 1-16, 1-17, and 1-18 peptides. In this work we report experimental data which demonstrate that the 1-16 peptide (P1-16) possesses a marked effect on the AT activity by preventing the formation of the thrombin-AT complex. We found that the formation of thrombin-AT complex is markedly decreased in the presence of P1-16 used at equimolar concentration with thrombin as evaluated with SDS-PAGE. We also monitored the conformational changes of thrombin in the presence of different P1-16 concentrations, and calculated the Kd of thrombin/P1-16 system by circular dichroism technique. The probable interaction sites of P1-16 with thrombin have been also evaluated by molecular graphics and computational analyses. These results have potential implications in the treatment of sterility and thrombotic diseases.

Original languageEnglish
Pages (from-to)541-549
Number of pages9
JournalExperimental and Molecular Medicine
Volume40
Issue number5
DOIs
Publication statusPublished - Oct 2008

Keywords

  • Blood coagulation
  • Hemostasis
  • Svp4 protein
  • Thrombin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Molecular Medicine
  • Clinical Biochemistry

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