Explaining meat quality of bulls and steers by differential proteome and phosphoproteome analysis of skeletal muscle
Autor(a) principal: | |
---|---|
Data de Publicação: | 2019 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | LOCUS Repositório Institucional da UFV |
Texto Completo: | https://doi.org/10.1016/j.jprot.2019.03.004 http://www.locus.ufv.br/handle/123456789/24353 |
Resumo: | The objective of this study was to evaluate the differential proteome and phosphoproteome between bulls and steers during conversion of muscle to meat, as well as after 14 days of aging. Twelve male Nellore (Bos taurus indicus) calves were used, and six calves were randomly selected for surgical castration. Calves were fed the same diet and were harvested after 230 days on feed. Longissimus muscle was sampled just after stunning (0d postmortem), at deboning (1d postmortem) and after aging (14d postmortem) for differential proteome analysis. Castration upregulated (P < 0.05) the abundance of glycolytic enzymes, while the oxidative phosphorylation protein ATP5B was downregulated (P < 0.05). In addition, abundance of troponin T fast isoform (TNNT3) was upregulated by castration (P < 0.05), while the slow isoform (TNNT1) tended to be decreased (P < 0.10). The creatine kinase M-type was markedly fragmented postmortem. Abundance of phosphorylated PGM1 increased during the first 24 h postmortem and was highly correlated with carcass pH. Further, abundance of the phosphorylated myofibrillar proteins ACTA1 and MYLPF were positively correlated with sarcomere shortening. Overall, our finds demonstrated that abundance and phosphorylation of glycolytic enzymes are associated with changes in beef tenderness and intramuscular fat. |
id |
UFV_1dd5e168b477fbb84f777616a235ca00 |
---|---|
oai_identifier_str |
oai:locus.ufv.br:123456789/24353 |
network_acronym_str |
UFV |
network_name_str |
LOCUS Repositório Institucional da UFV |
repository_id_str |
2145 |
spelling |
Silva, Luiz H. P.Assis, Débora E. F.Benedeti, Pedro D. B.Duarte, Marcio S.Chizzotti, Mario L.Rodrigues, Rafael T. S.2019-04-08T14:06:39Z2019-04-08T14:06:39Z2019-05-151874-3919https://doi.org/10.1016/j.jprot.2019.03.004http://www.locus.ufv.br/handle/123456789/24353The objective of this study was to evaluate the differential proteome and phosphoproteome between bulls and steers during conversion of muscle to meat, as well as after 14 days of aging. Twelve male Nellore (Bos taurus indicus) calves were used, and six calves were randomly selected for surgical castration. Calves were fed the same diet and were harvested after 230 days on feed. Longissimus muscle was sampled just after stunning (0d postmortem), at deboning (1d postmortem) and after aging (14d postmortem) for differential proteome analysis. Castration upregulated (P < 0.05) the abundance of glycolytic enzymes, while the oxidative phosphorylation protein ATP5B was downregulated (P < 0.05). In addition, abundance of troponin T fast isoform (TNNT3) was upregulated by castration (P < 0.05), while the slow isoform (TNNT1) tended to be decreased (P < 0.10). The creatine kinase M-type was markedly fragmented postmortem. Abundance of phosphorylated PGM1 increased during the first 24 h postmortem and was highly correlated with carcass pH. Further, abundance of the phosphorylated myofibrillar proteins ACTA1 and MYLPF were positively correlated with sarcomere shortening. Overall, our finds demonstrated that abundance and phosphorylation of glycolytic enzymes are associated with changes in beef tenderness and intramuscular fat.engJournal of ProteomicsVolume 199, Pages 51-66, May 2019Elsevier B. V.info:eu-repo/semantics/openAccessCastrationIntramuscular fatMeat agingPhosphoproteinZebu cattleExplaining meat quality of bulls and steers by differential proteome and phosphoproteome analysis of skeletal muscleinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINALartigo.pdfartigo.pdfTexto completoapplication/pdf4368322https://locus.ufv.br//bitstream/123456789/24353/1/artigo.pdf91bdeda16349ce3a9dfc10b2ed173fbeMD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/24353/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52123456789/243532019-04-08 11:08:25.192oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452019-04-08T14:08:25LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false |
dc.title.en.fl_str_mv |
Explaining meat quality of bulls and steers by differential proteome and phosphoproteome analysis of skeletal muscle |
title |
Explaining meat quality of bulls and steers by differential proteome and phosphoproteome analysis of skeletal muscle |
spellingShingle |
Explaining meat quality of bulls and steers by differential proteome and phosphoproteome analysis of skeletal muscle Silva, Luiz H. P. Castration Intramuscular fat Meat aging Phosphoprotein Zebu cattle |
title_short |
Explaining meat quality of bulls and steers by differential proteome and phosphoproteome analysis of skeletal muscle |
title_full |
Explaining meat quality of bulls and steers by differential proteome and phosphoproteome analysis of skeletal muscle |
title_fullStr |
Explaining meat quality of bulls and steers by differential proteome and phosphoproteome analysis of skeletal muscle |
title_full_unstemmed |
Explaining meat quality of bulls and steers by differential proteome and phosphoproteome analysis of skeletal muscle |
title_sort |
Explaining meat quality of bulls and steers by differential proteome and phosphoproteome analysis of skeletal muscle |
author |
Silva, Luiz H. P. |
author_facet |
Silva, Luiz H. P. Assis, Débora E. F. Benedeti, Pedro D. B. Duarte, Marcio S. Chizzotti, Mario L. Rodrigues, Rafael T. S. |
author_role |
author |
author2 |
Assis, Débora E. F. Benedeti, Pedro D. B. Duarte, Marcio S. Chizzotti, Mario L. Rodrigues, Rafael T. S. |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Silva, Luiz H. P. Assis, Débora E. F. Benedeti, Pedro D. B. Duarte, Marcio S. Chizzotti, Mario L. Rodrigues, Rafael T. S. |
dc.subject.pt-BR.fl_str_mv |
Castration Intramuscular fat Meat aging Phosphoprotein Zebu cattle |
topic |
Castration Intramuscular fat Meat aging Phosphoprotein Zebu cattle |
description |
The objective of this study was to evaluate the differential proteome and phosphoproteome between bulls and steers during conversion of muscle to meat, as well as after 14 days of aging. Twelve male Nellore (Bos taurus indicus) calves were used, and six calves were randomly selected for surgical castration. Calves were fed the same diet and were harvested after 230 days on feed. Longissimus muscle was sampled just after stunning (0d postmortem), at deboning (1d postmortem) and after aging (14d postmortem) for differential proteome analysis. Castration upregulated (P < 0.05) the abundance of glycolytic enzymes, while the oxidative phosphorylation protein ATP5B was downregulated (P < 0.05). In addition, abundance of troponin T fast isoform (TNNT3) was upregulated by castration (P < 0.05), while the slow isoform (TNNT1) tended to be decreased (P < 0.10). The creatine kinase M-type was markedly fragmented postmortem. Abundance of phosphorylated PGM1 increased during the first 24 h postmortem and was highly correlated with carcass pH. Further, abundance of the phosphorylated myofibrillar proteins ACTA1 and MYLPF were positively correlated with sarcomere shortening. Overall, our finds demonstrated that abundance and phosphorylation of glycolytic enzymes are associated with changes in beef tenderness and intramuscular fat. |
publishDate |
2019 |
dc.date.accessioned.fl_str_mv |
2019-04-08T14:06:39Z |
dc.date.available.fl_str_mv |
2019-04-08T14:06:39Z |
dc.date.issued.fl_str_mv |
2019-05-15 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
https://doi.org/10.1016/j.jprot.2019.03.004 http://www.locus.ufv.br/handle/123456789/24353 |
dc.identifier.issn.none.fl_str_mv |
1874-3919 |
identifier_str_mv |
1874-3919 |
url |
https://doi.org/10.1016/j.jprot.2019.03.004 http://www.locus.ufv.br/handle/123456789/24353 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartofseries.pt-BR.fl_str_mv |
Volume 199, Pages 51-66, May 2019 |
dc.rights.driver.fl_str_mv |
Elsevier B. V. info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
Elsevier B. V. |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Journal of Proteomics |
publisher.none.fl_str_mv |
Journal of Proteomics |
dc.source.none.fl_str_mv |
reponame:LOCUS Repositório Institucional da UFV instname:Universidade Federal de Viçosa (UFV) instacron:UFV |
instname_str |
Universidade Federal de Viçosa (UFV) |
instacron_str |
UFV |
institution |
UFV |
reponame_str |
LOCUS Repositório Institucional da UFV |
collection |
LOCUS Repositório Institucional da UFV |
bitstream.url.fl_str_mv |
https://locus.ufv.br//bitstream/123456789/24353/1/artigo.pdf https://locus.ufv.br//bitstream/123456789/24353/2/license.txt |
bitstream.checksum.fl_str_mv |
91bdeda16349ce3a9dfc10b2ed173fbe 8a4605be74aa9ea9d79846c1fba20a33 |
bitstream.checksumAlgorithm.fl_str_mv |
MD5 MD5 |
repository.name.fl_str_mv |
LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV) |
repository.mail.fl_str_mv |
fabiojreis@ufv.br |
_version_ |
1801212938948706304 |