The seminal vesicle protein No. 4 (SV-IV) secreted from the rat seminal vesicle epithelium, possesses immunosuppressive and anti-inflammatory properties and it is a potent inhibitor of platelet aggregation both in vivo and in vitro. This research aimed to investigate the possible effect of SV-TV on the process of human blood coagulation. Preliminary experiments showed that the recalcification time (RT) of platelet-poor plasma (PPP) samples, obtained from both normal subjects and patients affected by some hemorrhagic disorders, was found to be markedly reduced in the presence of micromolar amounts of SV-IV. It was demonstrated that the concentration of free antithrombin III (AT III) occurring in blood sera obtained from PPP samples recalcified in the presence of SV-IV was significantly decreased in comparison with sera obtained from PPP recalcified in the absence of SV-IV. It was also shown that PPP treatment with SV-IV significantly reduced the concentration of free AT III without affecting the levels of other plasma serine protease inhibitors, such as alpha(2)-macroglobulin, alpha(1)-antitrypsin and C-1-inhibitor. In addition, the RT of PPP treated with a specific rabbit anti-AT III polyclonal antiserum (anti-AT III treated PPP) was not modified by SV-IV. These findings were confirmed by the observation that the addition of SV-IV into an in vitro coagulation system, containing pure fibrinogen, alpha-thrombin and AT-III, resulted in complete suppression of thrombin inhibition by AT III. No other steps of the blood clotting process (prothrombinase complex, factor XIII, fibrinogen concentration) were affected by SV-IV.

Rat Protein-SV-IV (seminal-vesicle Protein No-4) Accelerates Human Blood-coagulation In-vitro By Selective-inhibition of Antithrombin-III / B., Dimicco; G., Colonna; Porta, Raffaele; S., Metafora. - In: BIOCHEMICAL PHARMACOLOGY. - ISSN 0006-2952. - STAMPA. - 48:(1994), pp. 345-352. [10.1016/0006-2952(94)90106-6]

Rat Protein-SV-IV (seminal-vesicle Protein No-4) Accelerates Human Blood-coagulation In-vitro By Selective-inhibition of Antithrombin-III

PORTA, RAFFAELE;
1994

Abstract

The seminal vesicle protein No. 4 (SV-IV) secreted from the rat seminal vesicle epithelium, possesses immunosuppressive and anti-inflammatory properties and it is a potent inhibitor of platelet aggregation both in vivo and in vitro. This research aimed to investigate the possible effect of SV-TV on the process of human blood coagulation. Preliminary experiments showed that the recalcification time (RT) of platelet-poor plasma (PPP) samples, obtained from both normal subjects and patients affected by some hemorrhagic disorders, was found to be markedly reduced in the presence of micromolar amounts of SV-IV. It was demonstrated that the concentration of free antithrombin III (AT III) occurring in blood sera obtained from PPP samples recalcified in the presence of SV-IV was significantly decreased in comparison with sera obtained from PPP recalcified in the absence of SV-IV. It was also shown that PPP treatment with SV-IV significantly reduced the concentration of free AT III without affecting the levels of other plasma serine protease inhibitors, such as alpha(2)-macroglobulin, alpha(1)-antitrypsin and C-1-inhibitor. In addition, the RT of PPP treated with a specific rabbit anti-AT III polyclonal antiserum (anti-AT III treated PPP) was not modified by SV-IV. These findings were confirmed by the observation that the addition of SV-IV into an in vitro coagulation system, containing pure fibrinogen, alpha-thrombin and AT-III, resulted in complete suppression of thrombin inhibition by AT III. No other steps of the blood clotting process (prothrombinase complex, factor XIII, fibrinogen concentration) were affected by SV-IV.
1994
Rat Protein-SV-IV (seminal-vesicle Protein No-4) Accelerates Human Blood-coagulation In-vitro By Selective-inhibition of Antithrombin-III / B., Dimicco; G., Colonna; Porta, Raffaele; S., Metafora. - In: BIOCHEMICAL PHARMACOLOGY. - ISSN 0006-2952. - STAMPA. - 48:(1994), pp. 345-352. [10.1016/0006-2952(94)90106-6]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/473595
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