BmTI-A, a Kunitz type inhibitor from Rhipicephalus microplus able to interfere in vessel formation

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dc.citation.volume219
dc.contributor.authorSoares, Tatiane S. [UNIFESP]
dc.contributor.authorOliveira, Felipe [UNIFESP]
dc.contributor.authorTorquato, Ricardo J. S. [UNIFESP]
dc.contributor.authorSasaki, Sergio D.
dc.contributor.authorAraujo, Mariana S. [UNIFESP]
dc.contributor.authorPaschoalin, Thaysa [UNIFESP]
dc.contributor.authorTanaka, Aparecida S. [UNIFESP]
dc.coverageAmsterdam
dc.date.accessioned2020-08-21T16:59:48Z
dc.date.available2020-08-21T16:59:48Z
dc.date.issued2016
dc.description.abstractRhipicephalus microplus is an ectoparasite responsible for transmissions of babesiosis and anaplasmosis causing large losses to livestock production. To survive R. microplus tick produces several active molecules, such as protease inhibitors. This ectoparasite has been described as a rich source of serine protease inhibitors most of them are Kunitz-BPTI members named BmTIs which have no clear function yet. In the present work, we described the expression and functional characterization of rBmTI-A which showed to be similar to the native BmTI-A, a double-headed Kunitz-BPTI inhibitor, capable to inhibit trypsin, human neutrophil elastase (HNE), human plasma kalikrein (HuPK) and human plasmin. rBmTI-A was able to cause a decrease of HUVEC cell viability. Besides, the rBmTI-A showed to be a potent inhibitor of "in vitro" vessel formation. Our results suggested that BmTI-A may participate in the blood acquisition process interfering in the vessel formation during the tick parasite life stage, around 20 days. In conclusion, BmTI-A is a promising molecule to be used in the drug design and development of new method of R. microplus control. (C) 2016 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv Fed Sao Paulo UNIFESP, Dept Biochem, Escola Paulista Med, Rua 3 Maio 100, BR-04044020 Sao Paulo, SP, Brazil
dc.description.affiliationUniv Fed ABC, Ctr Ciencias Nat & Humanas, Rua Catequese 242, BR-09090400 Santo Andre, SP, Brazil
dc.description.affiliationUniv Fed Sao Paulo UNIFESP, Dept Microbiol Immunol & Parasitol, Escola Paulista Med, BR-04023062 Sao Paulo, SP, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo UNIFESP, Dept Biochem, Escola Paulista Med, Rua 3 Maio 100, BR-04044020 Sao Paulo, SP, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo UNIFESP, Dept Microbiol Immunol & Parasitol, Escola Paulista Med, BR-04023062 Sao Paulo, SP, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundação de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
dc.description.sponsorshipINCT-Entomologia Molecular, Brazil
dc.description.sponsorshipPRONEX
dc.description.sponsorshipIDFAPESP: 02/13960-8
dc.description.sponsorshipIDFAPESP: 05/03514-9
dc.description.sponsorshipIDFAPESP: 12/03657-8
dc.description.sponsorshipIDCNPq: 308780/2013-2
dc.format.extent44-52
dc.identifierhttp://dx.doi.org/10.1016/j.vetpar.2016.01.021
dc.identifier.citationVeterinary Parasitology. Amsterdam, v. 219, p. 44-52, 2016.
dc.identifier.doi10.1016/j.vetpar.2016.01.021
dc.identifier.issn0304-4017
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/57770
dc.identifier.wosWOS:000371943700007
dc.language.isoeng
dc.publisherElsevier Science Bv
dc.relation.ispartofVeterinary Parasitology
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectTicken
dc.subjectRhipicephalus microplusen
dc.subjectKallikreinen
dc.subjectPlasminen
dc.subjectProtease inhibitoren
dc.subjectKunitzen
dc.subjectAngiogenesisen
dc.titleBmTI-A, a Kunitz type inhibitor from Rhipicephalus microplus able to interfere in vessel formationen
dc.typeinfo:eu-repo/semantics/article
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