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Registro Completo |
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Biblioteca(s): |
Embrapa Semiárido. |
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Data corrente: |
24/09/2003 |
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Data da última atualização: |
04/09/2024 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
SANTOS, R. F. dos; SILVA, P. C. G. da. |
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Afiliação: |
ROBERIO FERREIRA DOS SANTOS, CNPA; PEDRO CARLOS GAMA DA SILVA, CPATSA. |
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Título: |
Pesquisa agropecuária e agricultura familiar no Brasil. |
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Ano de publicação: |
1997 |
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Fonte/Imprenta: |
Raízes - Revista de Ciências Sociais e Econômicas, v. 16, n. 14, p. 125-136, jun. 1997. |
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ISSN: |
0102-552 X |
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Idioma: |
Português |
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Conteúdo: |
Pesquisa agropecuária e agricultura familiar no Brasil. O objetivo deste trabalho é tecer alguns comentários sobre agricultura familiar enquanto dependente da pesquisa agropecuária pública, dentro do novo modelo de atuação que vem sendo adotado na Embrapa, empresa líder no segmento de pesquisa. |
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Palavras-Chave: |
Pequeno produtor rural; Pesquisa agropecuária. |
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Thesagro: |
Agricultura familiar; Desenvolvimento rural; Políticas públicas. |
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Thesaurus Nal: |
Rural development; Small farms. |
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Categoria do assunto: |
B Sociologia Rural |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/doc/149643/1/Pesquisa-agropecuaria-agricultura-familiar.pdf
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Marc: |
LEADER 00991naa a2200229 a 4500
001 1149643
005 2024-09-04
008 1997 bl uuuu u00u1 u #d
022 $a0102-552 X
100 1 $aSANTOS, R. F. dos
245 $aPesquisa agropecuária e agricultura familiar no Brasil.
260 $c1997
520 $aPesquisa agropecuária e agricultura familiar no Brasil. O objetivo deste trabalho é tecer alguns comentários sobre agricultura familiar enquanto dependente da pesquisa agropecuária pública, dentro do novo modelo de atuação que vem sendo adotado na Embrapa, empresa líder no segmento de pesquisa.
650 $aRural development
650 $aSmall farms
650 $aAgricultura familiar
650 $aDesenvolvimento rural
650 $aPolíticas públicas
653 $aPequeno produtor rural
653 $aPesquisa agropecuária
700 1 $aSILVA, P. C. G. da
773 $tRaízes - Revista de Ciências Sociais e Econômicas$gv. 16, n. 14, p. 125-136, jun. 1997.
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Registro original: |
Embrapa Semiárido (CPATSA) |
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Registro Completo
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Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
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Data corrente: |
15/12/2015 |
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Data da última atualização: |
20/06/2024 |
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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: |
ARCANJO, D. D. R.; VASCONCELOS, A. G.; COMERMA-STEFFENSEN, S. G.; JESUS, J. R.; SILVA, L. P. da; PIRES JÚNIOR, O. R.; COSTA-NETO, C. M.; OLIVEIRA, E. B.; MIGLIOLO, L.; FRANCO, O. L.; RESTINI, C. B. A.; PAULO, M.; BENDHACK, L. M.; BEMQUERER, M. P.; OLIVEIRA, A. P.; SIMONSEN, U.; LEITE, J. R. de S. de A. |
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Afiliação: |
DANIEL DIAS RUFINO ARCANJO, UNIVERSIDADE FEDERAL DO PIAUÍ; ANDREANNE GOMES VASCONCELOS, UNIVERSIDADE FEDERAL DO PIAUÍ; SIMÓN GABRIEL, AARHUS UNIVERSITY; JOILSON RAMOS JESUS, UNIVERSIDADE FEDERAL DO PIAUÍ; LUCIANO PAULINO DA SILVA, CENARGEN; OSMINDO RODRIGUES PIRES JÚNIOR, UNIVERSIDADE DE BRASÍLIA; CLAUDIO MIGUEL COSTA-NETO, UNIVERSIDADE DE SÃO PAULO; EDUARDO BRANDT OLIVEIRA, UNIVERSIDADE DE SÃO PAULO; LUDOVICO MIGLIOLO, UNIVERSIDADE CATÓLICA DE BRASÍLIA; OCTÁVIO LUIZ FRANCO, UNIVERSIDADE CATÓLICA DE BRASÍLIA; CAROLINA BARALDI ARAÚJO RESTINI, UNIVERSIDADE DE RIBEIRÃO PRETO; MICHELE PAULO, UNIVERSIDADE DE SÃO PAULO; LUSIANE MARIA BENDHACK, UNIVERSIDADE DE SÃO PAULO; MARCELO PORTO BEMQUERER, CENARGEN; ALDEIDIA PEREIRA OLIVEIRA, UNIVERSIDADE FEDERAL DO PIAUÍ; ULF SIMONSEN, AARHUS UNIVERSITY; JOSÉ ROBERTO DE SOUZA DE ALMEIDA LEITE, UNIVERSIDADE FEDERAL DO PIAUÍ. |
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Título: |
A novel vasoactive proline-rich oligopeptide from the skin secretion of the frog Brachycephalus ephippium. |
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Ano de publicação: |
2015 |
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Fonte/Imprenta: |
Plos One, v. 10, dez. 2015. (Open Access) |
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DOI: |
10.1371/journal.pone.0145071 |
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Idioma: |
Inglês |
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Conteúdo: |
Proline-rich oligopeptides (PROs) are a large family which comprises the bradykinin-potentiating peptides (BPPs). They inhibit the activity of the angiotensin I-converting enzyme (ACE) and have a typical pyroglutamyl (Pyr)/proline-rich structure at the N- and C-terminus, respectively. Furthermore, PROs decrease blood pressure in animals. In the present study, the isolation and biological characterization of a novel vasoactive BPP isolated from the skin secretion of the frog Brachycephalus ephippium is described. This new PRO, termed BPP-Brachy, has the primary structure WPPPKVSP and the amidated form termed BPPBrachyNH2 inhibits efficiently ACE in rat serum. In silico molecular modeling and docking studies suggest that BPP-BrachyNH2 is capable of forming a hydrogen bond network as well as multiple van der Waals interactions with the rat ACE, which blocks the access of the substrate to the C-domain active site. Moreover, in rat thoracic aorta BPP-BrachyNH2 induces potent endothelium-dependent vasodilatation with similar magnitude as captopril. In DAF-FM DA-loaded aortic cross sections examined by confocal microscopy, BPP-BrachyNH2 was found to increase the release of nitric oxide (NO). Moreover, BPP-BrachyNH2 was devoid of toxicity in endothelial and smooth muscle cell cultures. In conclusion, the peptide BPP-BrachyNH2 has a novel sequence being the first BPP isolated from the skin secretion of the Brachycephalidae family. This opens for exploring amphibians as a source of new biomolecules. The BPP-BrachyNH2 is devoid of cytotoxicity and elicits endothelium-dependent vasodilatation mediated by NO. These findings open for the possibility of potential application of these peptides in the treatment of endothelial dysfunction and cardiovascular diseases. MenosProline-rich oligopeptides (PROs) are a large family which comprises the bradykinin-potentiating peptides (BPPs). They inhibit the activity of the angiotensin I-converting enzyme (ACE) and have a typical pyroglutamyl (Pyr)/proline-rich structure at the N- and C-terminus, respectively. Furthermore, PROs decrease blood pressure in animals. In the present study, the isolation and biological characterization of a novel vasoactive BPP isolated from the skin secretion of the frog Brachycephalus ephippium is described. This new PRO, termed BPP-Brachy, has the primary structure WPPPKVSP and the amidated form termed BPPBrachyNH2 inhibits efficiently ACE in rat serum. In silico molecular modeling and docking studies suggest that BPP-BrachyNH2 is capable of forming a hydrogen bond network as well as multiple van der Waals interactions with the rat ACE, which blocks the access of the substrate to the C-domain active site. Moreover, in rat thoracic aorta BPP-BrachyNH2 induces potent endothelium-dependent vasodilatation with similar magnitude as captopril. In DAF-FM DA-loaded aortic cross sections examined by confocal microscopy, BPP-BrachyNH2 was found to increase the release of nitric oxide (NO). Moreover, BPP-BrachyNH2 was devoid of toxicity in endothelial and smooth muscle cell cultures. In conclusion, the peptide BPP-BrachyNH2 has a novel sequence being the first BPP isolated from the skin secretion of the Brachycephalidae family. This opens for exploring amphibians as a source of ne... Mostrar Tudo |
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Palavras-Chave: |
Brachycephalus ephippium; Proline-rich oligopeptides. |
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Thesaurus NAL: |
secretion. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/182309/1/journal.pone.0145071.PDF
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Marc: |
LEADER 02864naa a2200361 a 4500
001 2031700
005 2024-06-20
008 2015 bl uuuu u00u1 u #d
024 7 $a10.1371/journal.pone.0145071$2DOI
100 1 $aARCANJO, D. D. R.
245 $aA novel vasoactive proline-rich oligopeptide from the skin secretion of the frog Brachycephalus ephippium.$h[electronic resource]
260 $c2015
520 $aProline-rich oligopeptides (PROs) are a large family which comprises the bradykinin-potentiating peptides (BPPs). They inhibit the activity of the angiotensin I-converting enzyme (ACE) and have a typical pyroglutamyl (Pyr)/proline-rich structure at the N- and C-terminus, respectively. Furthermore, PROs decrease blood pressure in animals. In the present study, the isolation and biological characterization of a novel vasoactive BPP isolated from the skin secretion of the frog Brachycephalus ephippium is described. This new PRO, termed BPP-Brachy, has the primary structure WPPPKVSP and the amidated form termed BPPBrachyNH2 inhibits efficiently ACE in rat serum. In silico molecular modeling and docking studies suggest that BPP-BrachyNH2 is capable of forming a hydrogen bond network as well as multiple van der Waals interactions with the rat ACE, which blocks the access of the substrate to the C-domain active site. Moreover, in rat thoracic aorta BPP-BrachyNH2 induces potent endothelium-dependent vasodilatation with similar magnitude as captopril. In DAF-FM DA-loaded aortic cross sections examined by confocal microscopy, BPP-BrachyNH2 was found to increase the release of nitric oxide (NO). Moreover, BPP-BrachyNH2 was devoid of toxicity in endothelial and smooth muscle cell cultures. In conclusion, the peptide BPP-BrachyNH2 has a novel sequence being the first BPP isolated from the skin secretion of the Brachycephalidae family. This opens for exploring amphibians as a source of new biomolecules. The BPP-BrachyNH2 is devoid of cytotoxicity and elicits endothelium-dependent vasodilatation mediated by NO. These findings open for the possibility of potential application of these peptides in the treatment of endothelial dysfunction and cardiovascular diseases.
650 $asecretion
653 $aBrachycephalus ephippium
653 $aProline-rich oligopeptides
700 1 $aVASCONCELOS, A. G.
700 1 $aCOMERMA-STEFFENSEN, S. G.
700 1 $aJESUS, J. R.
700 1 $aSILVA, L. P. da
700 1 $aPIRES JÚNIOR, O. R.
700 1 $aCOSTA-NETO, C. M.
700 1 $aOLIVEIRA, E. B.
700 1 $aMIGLIOLO, L.
700 1 $aFRANCO, O. L.
700 1 $aRESTINI, C. B. A.
700 1 $aPAULO, M.
700 1 $aBENDHACK, L. M.
700 1 $aBEMQUERER, M. P.
700 1 $aOLIVEIRA, A. P.
700 1 $aSIMONSEN, U.
700 1 $aLEITE, J. R. de S. de A.
773 $tPlos One$gv. 10, dez. 2015. (Open Access)
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Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
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