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| Registros recuperados : 5 | |
| 1. |  | SALIM, J. A.; MAZONI, I.; MANCINI, A. L.; MORAES, F. R.; JARDINE, J. G.; NESHICH, I. P.; NESHICH, G. MSSP: a web-based application for analysis of selected parameter from multiple structures in a graphical manner. In: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB, 2009. Não paginado. X-Meeting 2009.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 2. | | JARDINE, J. G.; NESHICH, G.; MAZONI, I.; YANO, I. H.; NESHICH, I. P. A.; SALIM, J. A; DE MORAES, F. R. Molecular modeling and structural analysis of the protein twitching motility of Xylella fastidiosa. In: CONGRESSO BRASILEIRO DE BIOTECNOLOGIA E RODADA E FEIRA DE NEGÓCIOS, 4., 2012, Guarujá. [Resumos]... [S.l.: s.n.], 2012. Não paginado. Brasil Biotec 2012.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 3. | | CAMPEIRO, J. D'A.; NESHICH, I. P.; SANT'ANNA, O. A.; LOPES, R.; IANZER, D.; ASSAKURA, M. T.; NESHICH, G.; HAYASHI, M. A. F. Identification of snake bradykinin-potentiating peptides (BPPs)-simile sequences in rat brain: potential BPP-like precursor protein? Biochemical Pharmacology, New York, v. 96, n. 3, p. 202-215, Aug. 2015.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 4. | | MAZONI, I.; BORRO, L. C.; MANCINI, A.; SALIM, J. A.; MORAES, F. R.; JARDINE, J. G.; NESHICH, I. P.; NESHICH, G. Computational analysis of the secondary structure elements based on the physical chemical and geometrical descriptors and statistics data. In: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB, 2009. Não paginado X-Meeting 2009.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 5. | | BRANDÃO, M. M.; ARRUDA, L. H.; NESHICH, G.; NESHICH, I. P.; PEREIRA, J. G. C.; MALAGÓ JÚNIOR, W.; SILVA-FILHO, M. C. Structural and phylogenetic analysis of Spodoptera frugiperda chymotrypsins involved on insect chemical protective barrier against plant Proteinase Inhibitors (PIs). In: ANNUAL MEETING OF THE SBBq, 40., 2011, Foz do Iguaçu. [Proceedings...]. São Paulo, SP: Brazilian Society for Biochemistry and Molecular Biology, 2011. Não paginado.| Biblioteca(s): Embrapa Agricultura Digital. |
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| Registros recuperados : 5 | |
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Registro Completo
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Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
22/12/2015 |
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Data da última atualização: |
22/12/2015 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 1 |
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Autoria: |
CAMPEIRO, J. D'A.; NESHICH, I. P.; SANT'ANNA, O. A.; LOPES, R.; IANZER, D.; ASSAKURA, M. T.; NESHICH, G.; HAYASHI, M. A. F. |
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Afiliação: |
JOANA 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. |
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Título: |
Identification of snake bradykinin-potentiating peptides (BPPs)-simile sequences in rat brain: potential BPP-like precursor protein? |
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Ano de publicação: |
2015 |
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Fonte/Imprenta: |
Biochemical Pharmacology, New York, v. 96, n. 3, p. 202-215, Aug. 2015. |
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DOI: |
http://dx.doi.org/10.1016/j.bcp.2015.05.012 |
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Idioma: |
Inglês |
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Conteúdo: |
Bradykinin-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. MenosBradykinin-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 bio... Mostrar Tudo |
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Palavras-Chave: |
Bioinformática; Endogenous correlate; Immunorecognition; Peptídeos; Pressão sanguínea; Snake toxin. |
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Thesagro: |
Veneno. |
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Thesaurus NAL: |
Bioinformatics; Blood pressure; Peptides. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/136051/1/Identification-snake-Campeiro.pdf
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Marc: |
LEADER 02743naa a2200337 a 4500
001 2032223
005 2015-12-22
008 2015 bl uuuu u00u1 u #d
024 7 $ahttp://dx.doi.org/10.1016/j.bcp.2015.05.012$2DOI
100 1 $aCAMPEIRO, J. D'A.
245 $aIdentification of snake bradykinin-potentiating peptides (BPPs)-simile sequences in rat brain$bpotential BPP-like precursor protein?$h[electronic resource]
260 $c2015
520 $aBradykinin-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.
650 $aBioinformatics
650 $aBlood pressure
650 $aPeptides
650 $aVeneno
653 $aBioinformática
653 $aEndogenous correlate
653 $aImmunorecognition
653 $aPeptídeos
653 $aPressão sanguínea
653 $aSnake toxin
700 1 $aNESHICH, I. P.
700 1 $aSANT'ANNA, O. A.
700 1 $aLOPES, R.
700 1 $aIANZER, D.
700 1 $aASSAKURA, M. T.
700 1 $aNESHICH, G.
700 1 $aHAYASHI, M. A. F.
773 $tBiochemical Pharmacology, New York$gv. 96, n. 3, p. 202-215, Aug. 2015.
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