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dc.contributor.authorGagaoua, Mohammed
dc.contributor.authorBonnet, Muriel
dc.contributor.authorPicard, Brigitte
dc.date.accessioned2021-06-03T10:46:57Z
dc.date.available2021-06-03T10:46:57Z
dc.date.issued2020-08-26
dc.identifier.citationGagaoua, M.; Bonnet, M.; Picard, B. Protein Array-Based Approach to Evaluate Biomarkers of Beef Tenderness and Marbling in Cows: Understanding of the Underlying Mechanisms and Prediction. Foods 2020, 9, 1180. https://doi.org/10.3390/foods9091180en_US
dc.identifier.urihttp://hdl.handle.net/11019/2418
dc.descriptionpeer-revieweden_US
dc.description.abstractThis study evaluated the potential of a panel of 20 protein biomarkers, quantified by Reverse Phase Protein Array (RPPA), to explain and predict two important meat quality traits, these being beef tenderness assessed by Warner–Bratzler shear force (WBSF) and the intramuscular fat (IMF) content (also termed marbling), in a large database of 188 Protected Designation of Origin (PDO) Maine-Anjou cows. Thus, the main objective was to move forward in the progression of biomarker-discovery for beef qualities by evaluating, at the same time for the two quality traits, a list of candidate proteins so far identified by proteomics and belonging to five interconnected biological pathways: (i) energy metabolic enzymes, (ii) heat shock proteins (HSPs), (iii) oxidative stress, (iv) structural proteins and (v) cell death and protein binding. Therefore, three statistical approaches were applied, these being Pearson correlations, unsupervised learning for the clustering of WBSF and IMF into quality classes, and Partial Least Squares regressions (PLS-R) to relate the phenotypes with the 20 biomarkers. Irrespective of the statistical method and quality trait, seven biomarkers were related with both WBSF and IMF, including three small HSPs (CRYAB, HSP20 and HSP27), two metabolic enzymes from the oxidative pathway (MDH1: Malate dehydrogenase and ALDH1A1: Retinal dehydrogenase 1), the structural protein MYH1 (Myosin heavy chain-IIx) and the multifunctional protein FHL1 (four and a half LIM domains 1). Further, three more proteins were retained for tenderness whatever the statistical method, among which two were structural proteins (MYL1: Myosin light chain 1/3 and TNNT1: Troponin T, slow skeletal muscle) and one was glycolytic enzyme (ENO3: β-enolase 3). For IMF, two proteins were, in this trial, specific for marbling whatever the statistical method: TRIM72 (Tripartite motif protein 72, negative) and PRDX6 (Peroxiredoxin 6, positive). From the 20 proteins, this trial allowed us to qualify 10 and 9 proteins respectively as strongly related with beef tenderness and marbling in PDO Maine-Anjou cows.en_US
dc.language.isoenen_US
dc.publisherMDPI AGen_US
dc.relation.ispartofseriesFoods;1180
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subjectmeat tendernessen_US
dc.subjectfaten_US
dc.subjectproteomicsen_US
dc.subjectproteinsen_US
dc.subjectenzymesen_US
dc.subjectquantificationen_US
dc.subjectbiological pathwaysen_US
dc.subjectchemometricsen_US
dc.titleProtein Array-Based Approach to Evaluate Biomarkers of Beef Tenderness and Marbling in Cows: Understanding of the Underlying Mechanisms and Predictionen_US
dc.typeArticleen_US
dc.identifier.doihttps://doi.org/10.3390/foods9091180
dc.contributor.sponsorPays de Loire Regional Councilen_US
dc.source.volume9
dc.source.issue9
dc.source.beginpage1180
refterms.dateFOA2021-06-03T10:46:58Z
dc.source.journaltitleFoods


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