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 | Acesso ao texto completo restrito à biblioteca da Embrapa Hortaliças. Para informações adicionais entre em contato com cnph.biblioteca@embrapa.br. |
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Registro Completo |
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Biblioteca(s): |
Embrapa Hortaliças. |
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Data corrente: |
19/06/2008 |
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Data da última atualização: |
05/05/2010 |
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Autoria: |
ANDRIOLO, J. L.; MADALÓZ, J. C. C.; GODOI, R. dos S.; JANISCH, D. I.; BARROS, C. A. P. |
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Título: |
Tolerance to salinity of chicory plants grown in hydroponics. |
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Ano de publicação: |
2008 |
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Fonte/Imprenta: |
Ciência Rural, Santa Maria, v. 38, n. 4, p. 1142-1144, jul. 2008. |
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Idioma: |
Português |
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Palavras-Chave: |
Cultivar amarito; Cultivar Pão de Açúcar; Cultivo. |
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Thesagro: |
Almeirão; Cichorium Intybus; Solução Nutritiva. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 00663naa a2200229 a 4500
001 1780439
005 2010-05-05
008 2008 bl uuuu u00u1 u #d
100 1 $aANDRIOLO, J. L.
245 $aTolerance to salinity of chicory plants grown in hydroponics.
260 $c2008
650 $aAlmeirão
650 $aCichorium Intybus
650 $aSolução Nutritiva
653 $aCultivar amarito
653 $aCultivar Pão de Açúcar
653 $aCultivo
700 1 $aMADALÓZ, J. C. C.
700 1 $aGODOI, R. dos S.
700 1 $aJANISCH, D. I.
700 1 $aBARROS, C. A. P.
773 $tCiência Rural, Santa Maria$gv. 38, n. 4, p. 1142-1144, jul. 2008.
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Registro original: |
Embrapa Hortaliças (CNPH) |
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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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