Purification and characterization of tenerplasminin-1, a serine peptidase inhibitor with antiplasmin activity from the coral snake (Micrurus tener tener) venom

dc.creatorVivas, Jeilyn
dc.creatorIbarra, Carlos
dc.creatorSalazar, Ana M.
dc.creatorFerreira, Ana G. C. Neves
dc.creatorSánchez, Elda E.
dc.creatorPerales, Jonas
dc.creatorRodriguez-Acosta, Alexis
dc.creatorGuerrero, Belsy
dc.date2016-05-10T13:06:55Z
dc.date2016-05-10T13:06:55Z
dc.date2016
dc.date.accessioned2023-09-27T00:10:05Z
dc.date.available2023-09-27T00:10:05Z
dc.identifierVIVAS, Jeilyn; et al. Purification and characterization of tenerplasminin-1, a serine peptidase inhibitor with antiplasmin activity from the coral snake (Micrurus tener tener) venom. Comparative Biochemistry and Physiology, Part C: Toxicology & Pharmacology, v.179, p.107–115, Jan. 2016.
dc.identifier1532-0456
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/14143
dc.identifier10.1016/j.cbpc.2015.09.009
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8898117
dc.descriptionA plasmin inhibitor, named tenerplasminin-1 (TP1), was isolated from Micrurus tener tener (Mtt) venom. It showed a molecular mass of 6542 Da, similarly to Kunitz-type serine peptidase inhibitors. The amidolytic activity of plasmin (0.5 nM) on synthetic substrate S-2251 was inhibited by 91% following the incubation with TP1 (1 nM). Aprotinin (2 nM) used as the positive control of inhibition, reduced the plasmin amidolytic activity by 71%. Plasmin fibrinolytic activity (0.05 nM) was inhibited by 67% following incubation with TP1 (0.1 nM). The degradation of fibrinogen chains induced by plasmin, trypsin or elastase was inhibited by TP1 at a 1:2, 1:4 and 1:20 enzyme:inhibitor ratio, respectively. On the other hand, the proteolytic activity of crude Mtt venom on fi- brinogen chains, previously attributed to metallopeptidases, was not abolished by TP1. The tPA-clot lysis assay showed that TP1 (0.2 nM) acts like aprotinin (0.4 nM) inducing a delay in lysis time and lysis rate which may be associated with the inhibition of plasmin generated from the endogenous plasminogen activation. TP1 is the first serine protease plasmin-like inhibitor isolated from Mtt snake venom which has been characterized in relation to its mechanism of action, formation of a plasmin:TP1 complex and therapeutic potential as anti-fibrinolytic agent, a biological characteristic of great interest in the field of biomedical research. They could be used to regulate the fibrinolytic system in pathologies such as metastatic cancer, parasitic infections, hemophilia and other hemorrhagic syndromes, in which an intense fibrinolytic activity is observed.
dc.formatapplication/pdf
dc.languageeng
dc.publisherElsevier
dc.rightsrestricted access
dc.subjectSistema Fibrinolítco
dc.subjectAntiplasmina
dc.subjectVeneno de cobra
dc.subjectHemostasia
dc.subjectElapidae
dc.subjectFibrinolytic system
dc.subjectHemostasis
dc.subjectMicrurus tener tener
dc.subjectPlasmin inhibitor
dc.subjectSnake venom
dc.titlePurification and characterization of tenerplasminin-1, a serine peptidase inhibitor with antiplasmin activity from the coral snake (Micrurus tener tener) venom
dc.typeArticle


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