The first evidence of global meat phosphoproteome changes in response to pre-slaughter stress.
Beef quality
Bos taurus - DFD meat - meat phosphoproteome
Meat tenderness
Post-mortem metabolism
Pre-slaughter stress biomarkers
Journal
BMC genomics
ISSN: 1471-2164
Titre abrégé: BMC Genomics
Pays: England
ID NLM: 100965258
Informations de publication
Date de publication:
17 Jul 2019
17 Jul 2019
Historique:
received:
07
05
2019
accepted:
27
06
2019
entrez:
19
7
2019
pubmed:
19
7
2019
medline:
18
12
2019
Statut:
epublish
Résumé
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. Noticeable and statistically significant differences in the extent of protein phosphorylation were detected between sample groups at the qualitative and quantitative levels. Overall phosphorylation rates across significantly changed phosphoproteins were about three times higher in DFD than in normal meat. Significantly changed phosphoproteins involved a variable number of isoforms of 13 myofibrillar and sarcoplasmic nonredundant proteins. However, fast skeletal myosin light chain 2 followed by troponin T, F-actin-capping and small heat shock proteins showed the greatest phosphorylation change, and therefore they were the most important phosphoproteins underlying LT muscle conversion to DFD meat in the Rubia Gallega breed. This is the first study reporting global meat phosphoproteome changes in response to PSS. The results show that reversible phosphorylation is a relevant mechanism underlying PSS response and downstream effects on meat quality. This research opens up novel horizons to unravel the complex molecular puzzle underlying muscle-to-meat conversion in response to PSS.
Sections du résumé
BACKGROUND
BACKGROUND
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.
RESULTS
RESULTS
Noticeable and statistically significant differences in the extent of protein phosphorylation were detected between sample groups at the qualitative and quantitative levels. Overall phosphorylation rates across significantly changed phosphoproteins were about three times higher in DFD than in normal meat. Significantly changed phosphoproteins involved a variable number of isoforms of 13 myofibrillar and sarcoplasmic nonredundant proteins. However, fast skeletal myosin light chain 2 followed by troponin T, F-actin-capping and small heat shock proteins showed the greatest phosphorylation change, and therefore they were the most important phosphoproteins underlying LT muscle conversion to DFD meat in the Rubia Gallega breed.
CONCLUSIONS
CONCLUSIONS
This is the first study reporting global meat phosphoproteome changes in response to PSS. The results show that reversible phosphorylation is a relevant mechanism underlying PSS response and downstream effects on meat quality. This research opens up novel horizons to unravel the complex molecular puzzle underlying muscle-to-meat conversion in response to PSS.
Identifiants
pubmed: 31315554
doi: 10.1186/s12864-019-5943-3
pii: 10.1186/s12864-019-5943-3
pmc: PMC6637562
doi:
Substances chimiques
Muscle Proteins
0
Phosphoproteins
0
Proteome
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
590Subventions
Organisme : Instituto Nacional de Investigación y Tecnología Agraria
ID : RTA 2014-00034-C04
Organisme : Consellería de Medio Rural of Xunta de Galicia, Spain
ID : FEADER 2010-04
Références
Integr Comp Biol. 2002 Jul;42(3):508-16
pubmed: 21708746
J Anim Sci. 2002 Jul;80(7):1895-903
pubmed: 12162657
Biochem J. 1995 May 15;308 ( Pt 1):57-61
pubmed: 7755588
Science. 1999 Mar 5;283(5407):1488-93
pubmed: 10066163
Meat Sci. 1997 Feb;45(2):239-51
pubmed: 22061306
Proteomics. 2011 Oct;11(20):4063-76
pubmed: 21805635
Meat Sci. 2008 Sep;80(1):12-9
pubmed: 22063165
Meat Sci. 2008 Mar;78(3):297-304
pubmed: 22062282
Mol Cell. 2001 Sep;8(3):601-11
pubmed: 11583622
Bioinformatics. 2009 Jan 15;25(2):288-9
pubmed: 19033274
Biochemistry. 1989 Oct 17;28(21):8506-14
pubmed: 2557904
Mol Biosyst. 2016 Jun 21;12(7):2024-35
pubmed: 26931796
Meat Sci. 2010 Sep;86(1):56-65
pubmed: 20599326
Cell Mol Life Sci. 2009 Jan;66(1):135-44
pubmed: 18979206
J Proteomics. 2015 Oct 14;128:141-53
pubmed: 26254011
J Proteomics. 2016 Sep 16;147:85-97
pubmed: 26899368
Nucleic Acids Res. 2015 Jan;43(Database issue):D447-52
pubmed: 25352553
Meat Sci. 2018 Jul;141:103-111
pubmed: 29580736
Food Chem. 2018 Apr 1;244:238-245
pubmed: 29120776
Meat Sci. 2014 Jan;96(1):379-84
pubmed: 23973564
Meat Sci. 2001 May;58(1):69-78
pubmed: 22061922
J Proteomics. 2012 Jul 19;75(14):4381-98
pubmed: 22510581
J Cell Sci. 1997 Feb;110 ( Pt 3):357-68
pubmed: 9057088
Arch Biochem Biophys. 2011 Jun 15;510(2):120-8
pubmed: 21284933
Cell Res. 2012 Jan;22(1):127-41
pubmed: 21577235
Nucleic Acids Res. 2010 Jul;38(Web Server issue):W210-3
pubmed: 20478823
Data Brief. 2015 May 07;4:100-4
pubmed: 26217771
Methods Mol Biol. 1999;112:513-30
pubmed: 10027274
J Anim Sci. 2001 Feb;79(2):392-7
pubmed: 11219448
Food Chem. 2018 May 30;249:8-15
pubmed: 29407935
Meat Sci. 1999 Aug;52(4):453-9
pubmed: 22062710
Meat Sci. 2000 Sep;56(1):101
pubmed: 22061778
J Agric Food Chem. 2007 May 16;55(10):3998-4004
pubmed: 17429980
Animal. 2008 Oct;2(10):1501-17
pubmed: 22443909
Meat Sci. 1993;34(2):163-78
pubmed: 22060661
J Proteome Res. 2018 Aug 3;17(8):2834-2849
pubmed: 29916714
PLoS One. 2017 Jan 19;12(1):e0170294
pubmed: 28103301
Oncogene. 2004 Oct 21;23(49):8118-27
pubmed: 15378030
J Agric Food Chem. 2009 Nov 25;57(22):10755-64
pubmed: 19860418
Meat Sci. 2013 Dec;95(4):854-70
pubmed: 23790743
Food Chem. 2017 Mar 1;218:455-462
pubmed: 27719935
J Biol Chem. 1994 Aug 12;269(32):20780-4
pubmed: 8051180
Meat Sci. 2008 Dec;80(4):1068-73
pubmed: 22063838
Compr Rev Food Sci Food Saf. 2017 May;16(3):400-430
pubmed: 33371557
J Biol Chem. 2007 Jul 13;282(28):20447-54
pubmed: 17504755
FEBS Lett. 1987 Apr 20;214(2):249-52
pubmed: 3569523
J Proteomics. 2012 Jul 19;75(14):4360-80
pubmed: 22361340
Food Chem. 2017 Mar 15;219:304-310
pubmed: 27765231
EMBO J. 1998 Mar 16;17(6):1688-99
pubmed: 9501090
J Anim Sci. 1996 May;74(5):993-1008
pubmed: 8726731
J Anim Sci. 1997 Jan;75(1):249-57
pubmed: 9027573
Food Chem. 2012 Oct 15;134(4):1999-2006
pubmed: 23442649
Bioinformatics. 2009 Nov 15;25(22):3045-6
pubmed: 19744993
Proteomics. 2007 Dec;7(24):4457-67
pubmed: 18072206
J Cell Biol. 1991 Jul;114(2):255-61
pubmed: 2071672
Meat Sci. 1999 Feb;51(2):135-41
pubmed: 22061697
Meat Sci. 2014 Feb;96(2 Pt A):837-42
pubmed: 24200578
Meat Sci. 2000 Nov;56(3):319
pubmed: 22062084
Meat Sci. 2014 Sep;98(1):9-20
pubmed: 24824530
J Biol Chem. 2004 Jan 16;279(3):1585-93
pubmed: 14576165
Physiol Rev. 2011 Oct;91(4):1123-59
pubmed: 22013208
Pharmacol Ther. 1999 May-Jun;82(2-3):111-21
pubmed: 10454190
J Sci Food Agric. 2016 Mar 30;96(5):1474-83
pubmed: 25950868
Meat Sci. 2002 Jun;61(2):181-5
pubmed: 22064007
J Proteomics. 2015 Jun 03;122:73-85
pubmed: 25857277
J Proteomics. 2019 Feb 20;193:123-130
pubmed: 30312679
Am J Physiol. 1993 May;264(5 Pt 1):C1085-95
pubmed: 8388631
J Agric Food Chem. 2015 Dec 2;63(47):10287-94
pubmed: 26549830
Circ J. 2009 Feb;73(2):208-13
pubmed: 19110504
Nucleic Acids Res. 2017 Jan 4;45(D1):D362-D368
pubmed: 27924014
Physiol Rev. 2003 Apr;83(2):433-73
pubmed: 12663865
Proteomics. 2005 Dec;5(18):4684-8
pubmed: 16267815
Proteomics. 2007 Sep;7 Suppl 1:64-9
pubmed: 17893854
J Proteomics. 2019 Apr 30;198:59-65
pubmed: 30385412
J Proteomics. 2014 Jun 25;106:125-39
pubmed: 24769528
Proc Nutr Soc. 2003 May;62(2):337-47
pubmed: 14506881
Poult Sci. 2016 Nov 1;95(11):2696-2706
pubmed: 27418663
Mol Cell Biol. 2005 May;25(9):3519-34
pubmed: 15831458
J Proteomics. 2015 Jul 01;125:29-40
pubmed: 25956426