Antiplatelet mechanism of a subtilisin-like serine protease from Solanum tuberosum (StSBTc-3).
Biochimie
; 218: 152-161, 2024 Mar.
Article
em En
| MEDLINE
| ID: mdl-37704077
The aims of this study are to characterize the antiplatelet activity of StSBTc-3, a potato serine protease with fibrino (geno) lytic activity, and to provide information on its mechanism of action. The results obtained show that StSBTc-3 inhibits clot retraction and prevents platelet aggregation induced by thrombin, convulxin, and A23187. Platelet aggregation inhibition occurs in a dose-dependent manner and is not affected by inactivation of StSBTc-3 with the inhibitor of serine proteases phenylmethylsulfonyl fluoride (PMSF). In addition, StSBTc-3 reduces fibrinogen binding onto platelets. In-silico calculations show a high binding affinity between StSBTc-3 and human α2bß3 integrin suggesting that the antiplatelet activity of StSBTc-3 could be associated with the fibronectin type III domain present in its amino acid sequence. Binding experiments show that StSBTc-3 binds to α2bß3 preventing the interaction between α2bß3 and fibrinogen and, consequently, inhibiting platelet aggregation. StSBTc-3 represents a promising compound to be considered as an alternative to commercially available drugs used in cardiovascular therapies.
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Texto completo:
1
Base de dados:
MEDLINE
Medicinas Complementares:
Homeopatia
Assunto principal:
Solanum tuberosum
Idioma:
En
Revista:
Biochimie
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
Argentina