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KMID : 0620920080400050541
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Experimental & Molecular Medicine
2008 Volume.40 No. 5 p.541 ~ p.549
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The N-terminal 1-16 peptide derived in vivo from protein seminal vesicle protein IV modulates α -thrombin activity: potential clinical implications
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Marilena Lepretti
Susan Costantini
Gaetano Ammirato
Gaia Giuberti
Michele Caraglia
Angelo M. Facchiano
Salvatore Metafora5 and Paola Stiuso
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Abstract
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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.
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KEYWORD
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blood coagulation, hemostasis, Svp4 protein, thrombin
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