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Registro Completo |
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Biblioteca(s): |
Embrapa Pantanal. |
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Data corrente: |
30/05/2000 |
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Data da última atualização: |
16/02/2023 |
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Autoria: |
SANTOS, S. A. |
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Afiliação: |
SANDRA APARECIDA SANTOS, CPAP. |
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Título: |
Formação do núcleo de conservação in situ de ovinos localmente adaptados do Pantanal : Embrapa Pantanal. |
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Ano de publicação: |
2020 |
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Fonte/Imprenta: |
In: PADUA, J. G.; ALBUQUERQUE, M. do S. M.; MELLO, S. C. M. de (Ed.). Bancos e coleções de germoplasma da Embrapa: conservação e uso. Brasília: Embrapa Recursos Genéticos e Biotecnologia, 2020. |
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Páginas: |
p. 129. |
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Idioma: |
Português |
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Notas: |
(Embrapa Recursos Genéticos e Biotecnologia. Documentos, 371). |
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Thesagro: |
Genética Animal; Ovino. |
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Thesaurus Nal: |
Animal genetics; Sheep. |
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Categoria do assunto: |
P Recursos Naturais, Ciências Ambientais e da Terra |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/216407/1/NucleoConservacaoOvinos-2020.pdf
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Marc: |
LEADER 00750naa a2200181 a 4500
001 1800894
005 2023-02-16
008 2020 bl uuuu u00u1 u #d
100 1 $aSANTOS, S. A.
245 $aFormação do núcleo de conservação in situ de ovinos localmente adaptados do Pantanal$bEmbrapa Pantanal.$h[electronic resource]
260 $c2020
300 $ap. 129.
500 $a(Embrapa Recursos Genéticos e Biotecnologia. Documentos, 371).
650 $aAnimal genetics
650 $aSheep
650 $aGenética Animal
650 $aOvino
773 $tIn: PADUA, J. G.; ALBUQUERQUE, M. do S. M.; MELLO, S. C. M. de (Ed.). Bancos e coleções de germoplasma da Embrapa: conservação e uso. Brasília: Embrapa Recursos Genéticos e Biotecnologia, 2020.
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Registro original: |
Embrapa Pantanal (CPAP) |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Gado de Leite. Para informações adicionais entre em contato com cnpgl.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Gado de Leite. |
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Data corrente: |
01/12/2022 |
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Data da última atualização: |
01/12/2022 |
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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: |
SOUSA, N. A. de; MARANI, M. M.; LOPES, A. L. F.; SILVA, E. M.; BARBOSA, E. A.; VASCONCELOS, A. G.; KUZNIEWSKI, F. T. B.; LUSTOSA, S. S.; GOMES, K. P.; COLUGNATI, D. B.; ROCHA, J. A.; SANTOS, L. H.; BEMQUERER, M. P.; QUELEMES, P.; VÉRAS, L.; MOREIRA, D. C.; GADELHA, K. K. L.; MAGALHÃES, P. J. C.; PLÁCIDO, A.; EATON, E.; NICOLAU, L.; MEDEIROS, J. V. R.; LEITE, J. R. S. A. |
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Afiliação: |
NAYARA ALVES DE SOUSA, Universidade Federal do Delta do Parnaíba; MARIELA M. MARANI, IPEEC-CONICET; ANDRÉ LUÍS FERNANDES LOPES, Universidade Federal do Delta do Parnaíba; EMANUELLE MORAIS SILVA, Universidade Federal do Delta do Parnaíba; EDER ALVES BARBOSA, Universidade de Brasília; ANDREANNE GOMES VASCONCELOS, Universidade de Brasília; FELIPE T. B. KUZNIEWSKI, Universidade de Brasília; SUELLEN SOUSA LUSTOSA, Universidade Federal do Delta do Parnaíba; KARINA PEREIRA GOMES, Universidade Federal de Goiás; DIEGO BASILE COLUGNATI, Universidade Federal de Goiás; JEFFERSON A. ROCHA, Universidade Federal do Maranhão; LUCIANNA HELENE SANTOS, Universidade Federal de Minas Gerais; MARCELO PORTO BEMQUERER, CNPGL; PATRICK QUELEMES, Universidade Federal do Delta do Parnaíba; LEIZ VÉRAS, Universidade Federal do Delta do Parnaíba; DANIEL C. MOREIRA, Universidade de Brasília; KALINNE KELLY LIMA GADELHA, Universidade Federal do Ceará; PEDRO JORGE CALDAS MAGALHÃES, Universidade Federal do Ceará; ALEXANDRA PLÁCIDO, Universidade do Porto; PETER EATON, Universidade do Porto; LUCAS NICOLAU, Universidade Federal do Delta do Parnaíba; JAND VENES R. MEDEIROS, Universidade Federal do Delta do Parnaíba; JOSÉ R. S. A. LEITE, Universidade de Brasília. |
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Título: |
BR-bombesin: a novel bombesin-related peptide from the skin secretion of the Chaco tree frog (Boana raniceps) with physiological gastric effects. |
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Ano de publicação: |
2022 |
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Fonte/Imprenta: |
Amino Acids, v. 54, p. 733-747, 2022. |
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DOI: |
https://doi.org/10.1007/s00726-021-03114-4 |
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Idioma: |
Inglês |
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Conteúdo: |
Bombesin mediates several biological activities in the gastrointestinal (GI) tract and central nervous system in mammals, including smooth muscle contraction, secretion of GI hormones and regulation of homeostatic mechanisms. Here, we report a novel bombesin-like peptide isolated from Boana raniceps. Its amino acid sequence, GGNQWAIGHFM-NH2, was identified and structurally confirmed by HPLC, MS/MS and 454-pyrosequencing; the peptide was named BR-bombesin. The effect of BR-bombesin on smooth muscle contraction was assessed in ileum and esophagus, and its anti-secretory activity was investigated in the stomach. BR-bombesin exerted significant contractile activity with a concentration?response curve similar to that of commercially available bombesin in ileum strips of Wistar rats. In esophageal strips, BR-bombesin acted as an agonist, as many other bombesin-related peptides act, although with different behavior compared to the muscarinic agonist carbachol. Moreover, BR-bombesin inhibited stomach secretion by approximately 50% compared to the untreated control group. This novel peptide has 80% and 70% similarity with the 10-residue C-terminal domain of human neuromedin B (NMB) and human gastrin releasing peptide (GRP10), respectively. Molecular docking analysis revealed that the GRP receptor had a binding energy equal to - 7.3 kcal.mol?1 and ? 8.5 kcal.mol?1 when interacting with bombesin and BR-bombesin, respectively. Taken together, our data open an avenue to investigate BR-bombesin in disorders that involve gastrointestinal tract motility and acid gastric secretion. MenosBombesin mediates several biological activities in the gastrointestinal (GI) tract and central nervous system in mammals, including smooth muscle contraction, secretion of GI hormones and regulation of homeostatic mechanisms. Here, we report a novel bombesin-like peptide isolated from Boana raniceps. Its amino acid sequence, GGNQWAIGHFM-NH2, was identified and structurally confirmed by HPLC, MS/MS and 454-pyrosequencing; the peptide was named BR-bombesin. The effect of BR-bombesin on smooth muscle contraction was assessed in ileum and esophagus, and its anti-secretory activity was investigated in the stomach. BR-bombesin exerted significant contractile activity with a concentration?response curve similar to that of commercially available bombesin in ileum strips of Wistar rats. In esophageal strips, BR-bombesin acted as an agonist, as many other bombesin-related peptides act, although with different behavior compared to the muscarinic agonist carbachol. Moreover, BR-bombesin inhibited stomach secretion by approximately 50% compared to the untreated control group. This novel peptide has 80% and 70% similarity with the 10-residue C-terminal domain of human neuromedin B (NMB) and human gastrin releasing peptide (GRP10), respectively. Molecular docking analysis revealed that the GRP receptor had a binding energy equal to - 7.3 kcal.mol?1 and ? 8.5 kcal.mol?1 when interacting with bombesin and BR-bombesin, respectively. Taken together, our data open an avenue to investigate BR-bo... Mostrar Tudo |
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Palavras-Chave: |
Peptídeo bioativo; Secreção gástrica. |
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Thesagro: |
Anfíbio; Peptídeo. |
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Categoria do assunto: |
L Ciência Animal e Produtos de Origem Animal |
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Marc: |
LEADER 02899naa a2200445 a 4500
001 2149045
005 2022-12-01
008 2022 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1007/s00726-021-03114-4$2DOI
100 1 $aSOUSA, N. A. de
245 $aBR-bombesin$ba novel bombesin-related peptide from the skin secretion of the Chaco tree frog (Boana raniceps) with physiological gastric effects.$h[electronic resource]
260 $c2022
520 $aBombesin mediates several biological activities in the gastrointestinal (GI) tract and central nervous system in mammals, including smooth muscle contraction, secretion of GI hormones and regulation of homeostatic mechanisms. Here, we report a novel bombesin-like peptide isolated from Boana raniceps. Its amino acid sequence, GGNQWAIGHFM-NH2, was identified and structurally confirmed by HPLC, MS/MS and 454-pyrosequencing; the peptide was named BR-bombesin. The effect of BR-bombesin on smooth muscle contraction was assessed in ileum and esophagus, and its anti-secretory activity was investigated in the stomach. BR-bombesin exerted significant contractile activity with a concentration?response curve similar to that of commercially available bombesin in ileum strips of Wistar rats. In esophageal strips, BR-bombesin acted as an agonist, as many other bombesin-related peptides act, although with different behavior compared to the muscarinic agonist carbachol. Moreover, BR-bombesin inhibited stomach secretion by approximately 50% compared to the untreated control group. This novel peptide has 80% and 70% similarity with the 10-residue C-terminal domain of human neuromedin B (NMB) and human gastrin releasing peptide (GRP10), respectively. Molecular docking analysis revealed that the GRP receptor had a binding energy equal to - 7.3 kcal.mol?1 and ? 8.5 kcal.mol?1 when interacting with bombesin and BR-bombesin, respectively. Taken together, our data open an avenue to investigate BR-bombesin in disorders that involve gastrointestinal tract motility and acid gastric secretion.
650 $aAnfíbio
650 $aPeptídeo
653 $aPeptídeo bioativo
653 $aSecreção gástrica
700 1 $aMARANI, M. M.
700 1 $aLOPES, A. L. F.
700 1 $aSILVA, E. M.
700 1 $aBARBOSA, E. A.
700 1 $aVASCONCELOS, A. G.
700 1 $aKUZNIEWSKI, F. T. B.
700 1 $aLUSTOSA, S. S.
700 1 $aGOMES, K. P.
700 1 $aCOLUGNATI, D. B.
700 1 $aROCHA, J. A.
700 1 $aSANTOS, L. H.
700 1 $aBEMQUERER, M. P.
700 1 $aQUELEMES, P.
700 1 $aVÉRAS, L.
700 1 $aMOREIRA, D. C.
700 1 $aGADELHA, K. K. L.
700 1 $aMAGALHÃES, P. J. C.
700 1 $aPLÁCIDO, A.
700 1 $aEATON, E.
700 1 $aNICOLAU, L.
700 1 $aMEDEIROS, J. V. R.
700 1 $aLEITE, J. R. S. A.
773 $tAmino Acids$gv. 54, p. 733-747, 2022.
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