Functional proteomic and interactome analysis of proteins associated with beef tenderness in Angus cattle

Zhao, Chunping; Liu, Zan; Wang, Yan; Updike, M. Scott; Liu, George E.; Bequette, B.J.; Baldwin, R.L.; Song, Jiuzhou

doi:10.1016/j.livsci.2013.11.030

Cited by 38 publications

(23 citation statements)

References 45 publications

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“…Cytoskeletal proteins were proposed to participate in IMF deposition [ 22 , 85 , 86 ], and MYH1 has already been identified by proteomics as a negative biomarker of adiposity [ 71 ]. MYH1 was revealed in several studies and under different factors as a good biomarker of beef tenderness [ 4 , 34 , 35 , 54 , 67 , 87 , 88 ]. As reported by Picard et al [ 54 ] and Gagaoua et al [ 34 ], the direction of its relationships with tenderness depends on muscle type, breed, end-point cooking temperature and origin of the panelists.…”

Section: Discussionmentioning

confidence: 99%

Protein Array-Based Approach to Evaluate Biomarkers of Beef Tenderness and Marbling in Cows: Understanding of the Underlying Mechanisms and Prediction

Gagaoua

Bonnet

Picard

2020

Foods

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This 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.

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Section: Discussionmentioning

confidence: 99%

Protein Array-Based Approach to Evaluate Biomarkers of Beef Tenderness and Marbling in Cows: Understanding of the Underlying Mechanisms and Prediction

Gagaoua

Bonnet

Picard

2020

Foods

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“…composition (Table 4). Proteomic study revealed that MYH1 was associated with superior beef tenderness [38]. A microarray analysis at the transcriptomic level showed that MYH1 was related to the shear force of beef muscle [34].…”

Section: Plos Onementioning

confidence: 99%

Transcriptome profiling of longissimus lumborum in Holstein bulls and steers with different beef qualities

Wang

et al. 2020

PLoS ONE

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Previous research regarding Holstein cows has mainly focused on increasing milk yield. However, in order to maximize the economical profits of Holstein cattle farming, it is necessary to fully take advantage of Holstein bulls to produce high-grade beef. The present study aims to investigate different transcriptomic profiling of Holstein bulls and steers, via highthroughput RNA-sequencing (RNA-seq). The growth and beef quality traits of Holstein steers and bulls were characterized via assessment of weight, rib eye area, marbling score, shear force and intramuscular fat percentage of the longissimus lumborum (LL) muscle. The results indicated that castration improved the meat quality, yet reduced the meat yield. Subsequently, RNA-seq of the LL muscle from Holstein steers and bulls revealed a total of 56 differentially expressed genes (DEGs). We performed the functional enrichment analysis in Gene Ontology (GO) annotations of the DEGs using GOseq R package software and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis using KOBAS tool. Through the integrated analysis of DEGs with reported QTLs and SNPs, seven promising candidate genes potentially affecting the beef quality of LL muscle following castration were discovered, including muscle structural protein coding genes (MYH1, MYH4, MYH10) and functional protein coding genes (GADL1, CYP2R1, EEPD1, SHISA3). Among them, MYH10, GADL1, CYP2R1, EEPD1 and SHISA3 were novel candidate genes associated with beef quality traits. Notably, EEPD1 was associated with both meat quality and reproduction traits, thus indicating its overlapping role in responding to hormone change, and subsequently inducing beef quality improvement. Our findings provide a complete dataset of gene expression profile of LL in Holstein bulls and steers, and will aid in understanding how castration influence meat yield and quality.

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“…The disappearance of the protein band at 200 kDa indicates that the myosin heavy chain degraded first when it was exposed to heat treatment. Myosin is the most abundant protein in muscle and is located in the myofibril, with roles in muscle contraction and relaxation (Zhao et al, 2014). The oxidative modification of myosin's primary structure has been shown to decrease the thermal stability of myosin (Liu & Xiong, 2000;Lund, Heinonen, Baron, & Estevez, 2011).…”

Section: Effect Of the Cooking Conditions On Protein Degradationmentioning

confidence: 99%

“…the results indicate that thermal treatment can induce SH/S-S exchange reactions and other reactions that lead to an increase in sulfur-containing volatile compounds such as sulfur dioxide. SH groups can transform into sulfenic acid, sulfinic acid, and disulfide cross-links through various complex reactions triggered by oxidation(Zhao et al, 2014), and to S-S bonds.A cooking time from 50 to 60 min at 75-80°C was an inflection point for protein oxidation and might be a critical point for flavor formation at these temperatures. During protein oxidation, thiol groups of cysteine can be oxidized and form disulfide bridges, which likely cause protein polymerization and, subsequently, protein aggregation.…”

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confidence: 99%

Characterization of protein changes and development of flavor components induced by thermal modulation during the cooking of chicken meat

Zhu

Tian

Sun

et al. 2019

J Food Process Preserv

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With the development of new technology in the food industry, stewed chicken should now be prepared based on scientific processing parameters instead of traditional procedures. This study was designed to examine the effects of cooking temperature (75, 80, 85, 90, 95, and 100°C) and cooking time (10, 20, 30, 40, 50, 60, 90, and 120 min) on protein degradation, protein oxidation, and flavor formation in stewed chicken meat. Significantly greater nonprotein nitrogen and total free amino acid concentrations were observed when cooking at 80 and 90°C for 50 and 60 min. Cooking for 90–100 min resulted in a stable flavor profile according to e‐nose data. The results suggest that with a cooking temperature of 80–90°C and a cooking time of 50–60 min, protein degradation and protein oxidation are each maximized, indicating a critical point for increasing stewed chicken flavor formation. Practical applications Heating of meat modifies its eating quality, including texture, color, and flavor. The rate and extent of these changes are dependent on the amount of heat that is transferred to the meat and on the heating rate. The ability to exert control over these variables will define to what extent the meat becomes more palatable to the consumer after cooking, with tenderness, juiciness, and flavor being the main factors influencing choice and acceptance of cooked meat. Therefore, a continuing aim of the meat industry is to discover improvements in processing that ensure and enhance these desirable sensory attributes while still yielding a product that is safe to consume.

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Functional proteomic and interactome analysis of proteins associated with beef tenderness in Angus cattle

Cited by 38 publications

References 45 publications

Protein Array-Based Approach to Evaluate Biomarkers of Beef Tenderness and Marbling in Cows: Understanding of the Underlying Mechanisms and Prediction

Protein Array-Based Approach to Evaluate Biomarkers of Beef Tenderness and Marbling in Cows: Understanding of the Underlying Mechanisms and Prediction

Transcriptome profiling of longissimus lumborum in Holstein bulls and steers with different beef qualities

Characterization of protein changes and development of flavor components induced by thermal modulation during the cooking of chicken meat

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