Fibrin(ogen)olytic and antiplatelet activities of a subtilisin-like protease from Solanum tuberosum (StSBTc-3)
| cic.isFulltext | true | es |
| cic.isPeerReviewed | true | es |
| cic.lugarDesarrollo | Universidad Nacional de Mar del Plata | es |
| cic.version | info:eu-repo/semantics/submittedVersion | es |
| dc.date.accessioned | 2017-03-15T14:24:44Z | |
| dc.date.available | 2017-03-15T14:24:44Z | |
| dc.identifier.uri | https://digital.cic.gba.gob.ar/handle/11746/5342 | |
| dc.title | Fibrin(ogen)olytic and antiplatelet activities of a subtilisin-like protease from Solanum tuberosum (StSBTc-3) | en |
| dc.type | Artículo | es |
| dcterms.abstract | Plant serine proteases have been widely used in food science and technology as well as in medicine. In this sense, several plant serine proteases have been proposed as potential anti-coagulants and antiplatelet agents. Previously, we have reported the purification and identification of a plant serine protease from Solanum tuberosum leaves. This potato enzyme, named as StSBTc-3, has a molecular weight of 72 kDa and it was characterized as a subtilisin like protease. In this work we determine and characterize the biochemical and medicinal properties of StSBTc-3. Results obtained show that, like the reported to other plant serine proteases, StSBTc-3 is able to degrade all chains of human fibrinogen and to produces fibrin clot lysis in a dose dependent manner. The enzyme efficiently hydrolyzes b subunit followed by partially hydrolyzed a and g subunits of human fibrinogen. Assays performed to determine StSBTc-3 substrate specificity using oxidized insulin b-chain as substrate, show seven cleavage sites: Asn3-Gln4; Cys7-Gly8; Glu13-Ala14; Leu15-Tyr16; Tyr16-Leu17; Arg22-Gly23 and Phe25-Tyr26, all of them were previously reported for other serine proteases with fibrinogenolytic activity. The maximum StSBTc-3 fibrinogenolytic activity was determined at pH 8.0 and at 37 C. Additionally, we demonstrate that StSBTc- 3 is able to inhibit platelet aggregation and is unable to exert cytotoxic activity on human erythrocytes in vitro at all concentrations assayed. These results suggest that StSBTc-3 could be evaluated as a new agent to be used in the treatment of thromboembolic disorders such as strokes, pulmonary embolism and deep vein thrombosis. | en |
| dcterms.creator.author | Pepe, Alfonso | es |
| dcterms.creator.author | Frey, María Eugenia | es |
| dcterms.creator.author | Muñoz, Fernando | es |
| dcterms.creator.author | Fernández, María Belén | es |
| dcterms.creator.author | Pedraza, Anabela | es |
| dcterms.creator.author | Galbán, Gustavo | es |
| dcterms.creator.author | García, Diana Noemí | es |
| dcterms.creator.author | Daleo, Gustavo Raúl | es |
| dcterms.creator.author | Guevara, María Gabriela | es |
| dcterms.extent | 8 p. | es |
| dcterms.isPartOf.issue | vol. 125 | es |
| dcterms.isPartOf.series | Biochimie | es |
| dcterms.issued | 2016-03-24 | |
| dcterms.language | Inglés | es |
| dcterms.license | Attribution-NonCommercial-NoDerivatives 4.0 International (BY-NC-ND 4.0) | es |
| dcterms.subject | Plant serine proteases | en |
| dcterms.subject | Anticoagulant and antithrombotic agents | en |
| dcterms.subject | Platelets | en |
| dcterms.subject.materia | Biología Celular, Microbiología | es |
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