Please use this identifier to cite or link to this item: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1032223
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dc.contributor.authorCAMPEIRO, J. D'A.pt_BR
dc.contributor.authorNESHICH, I. P.pt_BR
dc.contributor.authorSANT'ANNA, O. A.pt_BR
dc.contributor.authorLOPES, R.pt_BR
dc.contributor.authorIANZER, D.pt_BR
dc.contributor.authorASSAKURA, M. T.pt_BR
dc.contributor.authorNESHICH, G.pt_BR
dc.contributor.authorHAYASHI, M. A. F.pt_BR
dc.date.accessioned2015-12-22T11:11:11Zpt_BR
dc.date.available2015-12-22T11:11:11Zpt_BR
dc.date.created2015-12-22pt_BR
dc.date.issued2015pt_BR
dc.identifier.citationBiochemical Pharmacology, New York, v. 96, n. 3, p. 202-215, Aug. 2015.pt_BR
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/1032223pt_BR
dc.descriptionBradykinin-potentiating peptides (BPPs) from the South American pit viper snake venom were the first natural inhibitors of the human angiotensin I-converting enzyme (ACE) described. The pioneer characterization of the BPPs precursor from the snake venom glands by our group showed for the first time the presence of the C-type natriuretic peptide (CNP) in this same viper precursor protein. The confirmation of the BPP/CNP expression in snake brain regions correlated with neuroendocrine functions stimulated us to pursue the physiological correlates of these vasoactive peptides in mammals. Notably, several snake toxins were shown to have endogenous physiological correlates in mammals. In the present work, we expressed in bacteria the BPPs domain of the snake venom gland precursor protein, and this purified recombinant protein was used to raise specific polyclonal anti-BPPs antibodies. The correspondent single protein band immune-recognized in adult rat brain cytosol was isolated by 2DSDS/PAGE and/or HPLC, before characterization by MS fingerprint analysis, which identified this protein as superoxide dismutase (SOD, EC 1.15.1.1), a classically known enzyme with antioxidant activity and important roles in the blood pressure modulation. In silico analysis showed the exposition of the BPP-like peptide sequences on the surface of the 3D structure of rat SOD. These peptides were chemically synthesized to show the BPP-like biological activities in ex vivo and in vivo pharmacological bioassays. Taken together, our data suggest that SOD protein have the potential to be a source for putative BPP-like bioactive peptides, which once released may contribute to the blood pressure control in mammals.pt_BR
dc.language.isoengeng
dc.rightsopenAccesseng
dc.subjectBioinformáticapt_BR
dc.subjectPeptídeospt_BR
dc.subjectPressão sanguíneapt_BR
dc.subjectImmunorecognitionpt_BR
dc.subjectEndogenous correlatept_BR
dc.subjectSnake toxinpt_BR
dc.titleIdentification of snake bradykinin-potentiating peptides (BPPs)-simile sequences in rat brain: potential BPP-like precursor protein?pt_BR
dc.typeArtigo de periódicopt_BR
dc.date.updated2015-12-22T11:11:11Zpt_BR
dc.subject.thesagroVenenopt_BR
dc.subject.nalthesaurusBioinformaticspt_BR
dc.subject.nalthesaurusPeptidespt_BR
dc.subject.nalthesaurusBlood pressurept_BR
riaa.ainfo.id1032223pt_BR
riaa.ainfo.lastupdate2015-12-22pt_BR
dc.identifier.doihttp://dx.doi.org/10.1016/j.bcp.2015.05.012pt_BR
dc.contributor.institutionJOANA D'ARC CAMPEIRO, Unifesp; IZABELLA P. NESHICH, CNPTIA; OSVALDO A. SANT'ANNA, Instituto Butantan; ROBSON LOPES, Instituto Butantan; DANIELLE IANZER, Instituto Butantan; MARINA T. ASSAKURA, Instituto Butantan; GORAN NESHICH, CNPTIA; MIRIAN A. F. HAYASHI, Unifesp.pt_BR
Appears in Collections:Artigo em periódico indexado (CNPTIA)

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