The first evidence of global meat phosphoproteome changes in response to pre-slaughter stress
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Abstract
Pre-slaughter stress (PSS) impairs animal welfare and meat quality. Dark, firm and dry (DFD) are terms used to designate poor quality meats induced by PSS. Protein phosphorylation can be a potentially significant mechanism to explain rapid and multiple physiological and biochemical changes linked to PSS-dependent muscle-to-meat conversion. However, the role of reversible phosphorylation in the response to PSS is still little known. In this study, we report a comparative phosphoproteomic analysis of DFD and normal meats at 24 h post-mortem from the longissimus thoracis (LT) bovine muscle of male calves of the Rubia Gallega breed. For this purpose, two-dimensional gel electrophoresis (2-DE), in-gel multiplex identification of phosphoproteins with PRO-Q Diamond phosphoprotein-specific stain, tandem (MALDI-TOF/TOF) mass spectrometry (MS), novel quantitative phosphoproteomic statistics and bioinformatic tools were used
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Mato, A., Rodríguez-Vázquez, R., López-Pedrouso, M. et al. The first evidence of global meat phosphoproteome changes in response to pre-slaughter stress. BMC Genomics 20, 590 (2019). https://doi.org/10.1186/s12864-019-5943-3
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https://doi.org/10.1186/s12864-019-5943-3Sponsors
Mass spectrometry analysis, writing of the manuscript and article-processing charges were supported by grant RTA 2014–00034-C04 from the Instituto Nacional de Investigación y Tecnología Agraria (INIA, Spain). Meat samples were obtained by a project FEADER 2010–04 (Consellería de Medio Rural of Xunta de Galicia, Spain)
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© The Author(s). 2019. Open Access. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated