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| 6. |  | GARRIDO, M. da S.; AZEVEDO, R. L.; CARVALHO, C. A. L. de; MARTINS, L. C. B. Formigas associadas com a cochonilha rosada [Pseudococcus maritimus (Ehrhorn)] (Hemiptera: Sternorrhyncha: Pseudococcidae) em túberas de inhame no recôncavo da Bahia. Magistra, Cruz das Almas-BA, v. 20, n.2, p. 193-196, abr./jun., 2008.| Biblioteca(s): Embrapa Semiárido. |
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| 15. | | VIANA, C. H. P.; MARQUES, O. M.; CARVALHO, C. A. L. de. Rutelinae (Coleoptera: Scarabaeidae) colerados em armadilha luminosa em Cruz das Almas, Bahia Magistra, Cruz das Almas, BA, v.13, n.1, p.9-13, 2001| Biblioteca(s): Embrapa Mandioca e Fruticultura. |
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| 18. | | LINS, R. D.; DANTAS, A. C. V. L.; FANCELLI, M.; CARVALHO, C. A. L. de; LEITE, J. B. V. Infestação da broca-do-rizoma em variedades e híbridos de bananeira em Una, Bahia. Magistra, Cruz das Almas, v. 20, n. 1, p. 105-108, jan./mar. 2008.| Biblioteca(s): Embrapa Mandioca e Fruticultura. |
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| 20. | | BARRETO, A. Q.; BRITO, S. X.; CARVALHO, C. A. L. de; NASCIMENTO, A. S. do; LEDO, C. A. da S. Contact action of neem extract (Azadirachta indica A. Juss) on Tetragonisca angustula Latreille (Hymenoptera: Apidae) under controlled conditions. Magistra, Cruz das Almas-BA, v. 24, número especial, p. 52-56, dez. 2012. Semana Entomológica da Bahia (SINSECTA), 03 a 09 de dezembro de 2012| Biblioteca(s): Embrapa Mandioca e Fruticultura. |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Pecuária Sudeste. Para informações adicionais entre em contato com cppse.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Pecuária Sudeste. |
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Data corrente: |
02/12/2020 |
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Data da última atualização: |
02/12/2020 |
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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: |
POLETI, M. D.; REGITANO, L. C. de A.; SOUZA, G. H. M. F.; CESAR, A. S. M.; SIMAS, R. C.; VIGNATTO, B. S.; MONTENEGRO, H.; PÉRTILLE, F.; BALIEIRO, J. C. C.; CAMERON, L. C.; ELER, J. P.; COUTINHO, L. L. |
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Afiliação: |
Mirele D. Poleti, USP; LUCIANA CORREIA DE ALMEIDA REGITANO, CPPSE; Gustavo H. M. F. Souza, Applications and Development Laboratory Waters Corporation, São Paulo; Aline S. M. Cesar, USP, ESALq; Rosineide C. Simas, USP, ESALq; Bárbara Silva-Vignato, USP, ESALq; Horácio Montenegro, USP, ESALq; Fábio Pértille, USP, ESALq; Júlio C. C. Balieiro, USP; Luiz C. Cameron, UNIRIO; Joanir P. Eler, USP; Luiz L. Coutinho, USP, ESALq. |
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Título: |
Proteome alterations associated with the oleic acid and cis-9, trans-11 conjugated linoleic acid content in bovine skeletal muscle. |
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Ano de publicação: |
2020 |
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Fonte/Imprenta: |
Journal of Proteomics, v. 222, p. 1-14, e103792, jun. 2020. |
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DOI: |
https://doi.org/10.1016/j.jprot.2020.103792 |
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Idioma: |
Inglês |
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Conteúdo: |
Oleic acid (OA) and cis-9, trans-11 conjugated linoleic acid (c9t11-CLA) are fatty acids found in beef with beneficial effects in human health. This study investigated differentially abundant proteins (DAPs) in skeletal muscle of bovines with extreme values of OA, and c9t11-CLA. For each one of the fatty acids, twenty muscle samples were divided into two groups (N = 10_High; N = 10_Low) and analyzed by high definition mass spectrometry. We identified 103 and 133 DAPs between the groups for each fatty acid. We found 64 and 45 upregulated and 39 and 68 down-regulated proteins for OA and c9t11-CLA, respectively. Comparative analysis between proteomic and transcriptomic data revealed eight and ten genes with a consistent between mRNA expression levels and protein abundance for OA and c9t11-CLA, respectively. Unconventional myosin-Id (MYO1D), mineralocorticoid receptor (NR3C2), geranylgeranyl transferase type-2 subunit-alpha (RABGGTA), and uveal autoantigen with coiled-coil domains and ankyrin repeats (UACA) were found as putative candidate proteins for OA content. Fatty acid synthase (FASN), tubulin alpha-4A chain (TUBA4A), vinculin (VCL), NADH dehydrogenase 1 alpha subcomplex 5 (NDUFA5), and prefoldin subunit 6 (PFDN6) for c9t11-CLA. Our findings contribute to a deeper understanding of the molecular mechanisms behind the regulation of the OA and c9t11-CLA content in cattle skeletal muscle. Significance: Questions about the association between meat intake and disease incidence in humans has driven animal scientist to pursue a better understanding of the biological processes associated with differences in the intramuscular fat composition. The beneficial effects of oleic acid and conjugated linoleic acid in human health have been demonstrated by improving the immune system and preventing atherosclerosis, different types of cancers, hypertension, and diabetes. Previous genome-wide association and gene expression studies identified genomic regions and differentially expressed genes associated with the fatty acid profile in skeletal muscle. In this work, differences were evaluated at the protein level. The use of a label-free quantitative proteomic approach, compared with muscle transcriptome results obtained by RNA-sequencing, allowed us to earn new insights into the variability in fatty acid deposition in skeletal muscle of farm animals. This study opens new avenues to explore the effect of the fatty acids in the skeletal muscle of livestock animals, which is associated with nutritional values of the meat, and perhaps to understand the mechanisms correlated with metabolic diseases in other species. MenosOleic acid (OA) and cis-9, trans-11 conjugated linoleic acid (c9t11-CLA) are fatty acids found in beef with beneficial effects in human health. This study investigated differentially abundant proteins (DAPs) in skeletal muscle of bovines with extreme values of OA, and c9t11-CLA. For each one of the fatty acids, twenty muscle samples were divided into two groups (N = 10_High; N = 10_Low) and analyzed by high definition mass spectrometry. We identified 103 and 133 DAPs between the groups for each fatty acid. We found 64 and 45 upregulated and 39 and 68 down-regulated proteins for OA and c9t11-CLA, respectively. Comparative analysis between proteomic and transcriptomic data revealed eight and ten genes with a consistent between mRNA expression levels and protein abundance for OA and c9t11-CLA, respectively. Unconventional myosin-Id (MYO1D), mineralocorticoid receptor (NR3C2), geranylgeranyl transferase type-2 subunit-alpha (RABGGTA), and uveal autoantigen with coiled-coil domains and ankyrin repeats (UACA) were found as putative candidate proteins for OA content. Fatty acid synthase (FASN), tubulin alpha-4A chain (TUBA4A), vinculin (VCL), NADH dehydrogenase 1 alpha subcomplex 5 (NDUFA5), and prefoldin subunit 6 (PFDN6) for c9t11-CLA. Our findings contribute to a deeper understanding of the molecular mechanisms behind the regulation of the OA and c9t11-CLA content in cattle skeletal muscle. Significance: Questions about the association between meat intake and disease incidence i... Mostrar Tudo |
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Palavras-Chave: |
Label free proteomic. |
|
Thesagro: |
Bos Indicus; Gado Nelore. |
|
Thesaurus NAL: |
Beef; Fatty acids; Transcriptome. |
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Categoria do assunto: |
G Melhoramento Genético |
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Marc: |
LEADER 03666naa a2200337 a 4500
001 2127488
005 2020-12-02
008 2020 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1016/j.jprot.2020.103792$2DOI
100 1 $aPOLETI, M. D.
245 $aProteome alterations associated with the oleic acid and cis-9, trans-11 conjugated linoleic acid content in bovine skeletal muscle.$h[electronic resource]
260 $c2020
520 $aOleic acid (OA) and cis-9, trans-11 conjugated linoleic acid (c9t11-CLA) are fatty acids found in beef with beneficial effects in human health. This study investigated differentially abundant proteins (DAPs) in skeletal muscle of bovines with extreme values of OA, and c9t11-CLA. For each one of the fatty acids, twenty muscle samples were divided into two groups (N = 10_High; N = 10_Low) and analyzed by high definition mass spectrometry. We identified 103 and 133 DAPs between the groups for each fatty acid. We found 64 and 45 upregulated and 39 and 68 down-regulated proteins for OA and c9t11-CLA, respectively. Comparative analysis between proteomic and transcriptomic data revealed eight and ten genes with a consistent between mRNA expression levels and protein abundance for OA and c9t11-CLA, respectively. Unconventional myosin-Id (MYO1D), mineralocorticoid receptor (NR3C2), geranylgeranyl transferase type-2 subunit-alpha (RABGGTA), and uveal autoantigen with coiled-coil domains and ankyrin repeats (UACA) were found as putative candidate proteins for OA content. Fatty acid synthase (FASN), tubulin alpha-4A chain (TUBA4A), vinculin (VCL), NADH dehydrogenase 1 alpha subcomplex 5 (NDUFA5), and prefoldin subunit 6 (PFDN6) for c9t11-CLA. Our findings contribute to a deeper understanding of the molecular mechanisms behind the regulation of the OA and c9t11-CLA content in cattle skeletal muscle. Significance: Questions about the association between meat intake and disease incidence in humans has driven animal scientist to pursue a better understanding of the biological processes associated with differences in the intramuscular fat composition. The beneficial effects of oleic acid and conjugated linoleic acid in human health have been demonstrated by improving the immune system and preventing atherosclerosis, different types of cancers, hypertension, and diabetes. Previous genome-wide association and gene expression studies identified genomic regions and differentially expressed genes associated with the fatty acid profile in skeletal muscle. In this work, differences were evaluated at the protein level. The use of a label-free quantitative proteomic approach, compared with muscle transcriptome results obtained by RNA-sequencing, allowed us to earn new insights into the variability in fatty acid deposition in skeletal muscle of farm animals. This study opens new avenues to explore the effect of the fatty acids in the skeletal muscle of livestock animals, which is associated with nutritional values of the meat, and perhaps to understand the mechanisms correlated with metabolic diseases in other species.
650 $aBeef
650 $aFatty acids
650 $aTranscriptome
650 $aBos Indicus
650 $aGado Nelore
653 $aLabel free proteomic
700 1 $aREGITANO, L. C. de A.
700 1 $aSOUZA, G. H. M. F.
700 1 $aCESAR, A. S. M.
700 1 $aSIMAS, R. C.
700 1 $aVIGNATTO, B. S.
700 1 $aMONTENEGRO, H.
700 1 $aPÉRTILLE, F.
700 1 $aBALIEIRO, J. C. C.
700 1 $aCAMERON, L. C.
700 1 $aELER, J. P.
700 1 $aCOUTINHO, L. L.
773 $tJournal of Proteomics$gv. 222, p. 1-14, e103792, jun. 2020.
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