Phosphorylation of myofibrillar proteins in post‐mortem ovine muscle with different tenderness

Chen, Lijuan; Li, Xin; Ni, N.; Liu, Yue; Chen, Li; Wang, Zhenyu; Shen, Qingwu; Zhang, Dequan

doi:10.1002/jsfa.7244

Cited by 80 publications

(85 citation statements)

References 46 publications

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“…These findings and hypotheses are consistent with our results, as Nellore had greater phosphorylation of MYLPF and tougher beef. A similar result was observed in a study with sheep, in which there was higher MYLPF phosphorylation in the group of animals classified as tough meat [14]. Moreover, greater phosphorylated MYLPF abundance has been reported in dark firm dry beef [68].…”

Section: Resultssupporting

confidence: 85%

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Differences in Beef Quality between Angus (Bos taurus taurus) and Nellore (Bos taurus indicus) Cattle through a Proteomic and Phosphoproteomic Approach

et al. 2017

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Proteins are the major constituents of muscle and are key molecules regulating the metabolic changes during conversion of muscle to meat. Brazil is one of the largest exporters of beef and most Brazilian cattle are composed by zebu (Nellore) genotype. Bos indicus beef is generally leaner and tougher than Bos taurus such as Angus. The aim of this study was to compare the muscle proteomic and phosphoproteomic profile of Angus and Nellore. Seven animals of each breed previously subjected the same growth management were confined for 84 days. Proteins were extracted from Longissimus lumborum samples collected immediately after slaughter and separated by two-dimensional electrophoresis. Pro-Q Diamond stain was used in phosphoproteomics. Proteins identification was performed using matrix assisted laser desorption/ionization time-of-flight mass spectrometry. Tropomyosin alpha-1 chain, troponin-T, myosin light chain-1 fragment, cytoplasmic malate dehydrogenase, alpha-enolase and 78 kDa glucose-regulated protein were more abundant in Nellore, while myosin light chain 3, prohibitin, mitochondrial stress-70 protein and heat shock 70 kDa protein 6 were more abundant in Angus (P<0.05). Nellore had higher phosphorylation of myosin regulatory light chain-2, alpha actin-1, triosephosphate isomerase and 14-3-3 protein epsilon. However, Angus had greater phosphorylation of phosphoglucomutase-1 and troponin-T (P<0.05). Therefore, proteins involved in contraction and muscle organization, myofilaments expressed in fast or slow-twitch fibers and heat shock proteins localized in mitochondria or sarcoplasmic reticulum and involved in cell flux of calcium and apoptosis might be associated with differences in beef quality between Angus and Nellore. Furthermore, prohibitin appears to be a potential biomarker of intramuscular fat in cattle. Additionally, differences in phosphorylation of myofilaments and glycolytic enzymes could be involved with differences in muscle contraction force, susceptibility to calpain, apoptosis and postmortem glycolysis, which might also be related to differences in beef quality among Angus and Nellore.

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Section: Resultssupporting

confidence: 85%

“…Phosphorylation stands out among the main post-translational modifications, and phosphoproteomics is a useful technique to study phosphorylated proteins. In muscle tissue, phosphorylation could modulate the interaction among myofilaments and the activity of metabolic enzymes [12, 13, 14]. …”

Section: Introductionmentioning

confidence: 99%

Differences in Beef Quality between Angus (Bos taurus taurus) and Nellore (Bos taurus indicus) Cattle through a Proteomic and Phosphoproteomic Approach

et al. 2017

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“…The phosphorylation levels of these three bands were increased in the four groups and were negatively correlated ( P < 0.05) with pH and ATP content. During muscle aging, the increased phosphorylation level of fructose‐bisphosphate aldolase (band 14) was consistent with the results of previous studies . Lactoylglutathione lyase is related to the apoptotic process (GO:0043066).…”

Section: Resultssupporting

confidence: 90%

“…A number of phosphorylated proteins have been identified in postmortem muscles with variable tenderness, colour stability, pH decline rate or genotype . These studies have uncovered certain pathways or mechanisms of regulation of meat quality by protein phosphorylation.…”

Section: Introductionmentioning

confidence: 99%

Effects of temperature on protein phosphorylation in postmortem muscle

Ren

Hou

et al. 2019

J Sci Food Agric

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BACKGROUND Phosphorylation is one of the most important post‐translational modifications. Currently, many postmortem protein phosphorylation studies in muscle have been related to meat quality such as tenderness and color stability. However, the effects of various storage temperatures (25, 15, 4 and −1.5 °C) on the phosphorylation level of protein are poorly understood. Changes in the protein phosphorylation levels in postmortem ovine muscle at various storage temperatures were determined in this study. RESULTS The obtained data showed that pH decline rate was significantly inhibited at −1.5 °C from 12 h to 7 days postmortem (P < 0.05). The ATP consumption rate was higher at 25 °C than that at other three temperatures (P < 0.05). Analysis of the temperature, pH and ATP content revealed that the ATP content was related to the phosphorylation levels of individual protein bands. Phosphorylated myofibrillar and sarcoplasmic proteins, such as myosin binding protein C, troponin T3, myosin light chain 1, glucose‐6‐phosphate isomerase and pyruvate kinase, were mainly involved in glycolysis and muscle contraction. CONCLUSION The global and specific protein phosphorylation levels can be influenced by the postmortem storage temperature of muscle. Phosphorylation of proteins was correlated with glycolysis and muscle contraction. Certain phosphorylated proteins, such as heat shock proteins, require further study to clarify their effects on meat traits. © 2019 Society of Chemical Industry

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“…Meanwhile, the phosphorylation level of MRLC was significantly negatively correlated with its degradation ( r = −0.764, P < 0.05) during 0.5–72 h post‐mortem, which closely coincided with the result of Chen et al . (). The degree of MHC degradation gradually increased in the three groups with increased time.…”

Section: Discussionmentioning

confidence: 97%

Phosphorylation of myosin regulatory light chain affects actomyosin dissociation and myosin degradation

Cao

Hou

Shen

et al. 2019

Int J of Food Sci Tech

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Summary This research aimed to investigate the influence of myosin regulatory light chain (MRLC) phosphorylation on actomyosin dissociation and myosin degradation in post‐mortem ovine longissimus thoracis (LT) muscle with a purpose for strategies to improve meat quality in practice. Data obtained show that the highest actomyosin dissociation occurred at 48 h post‐mortem. Based on the cluster analysis of the actomyosin dissociation degree at 48 h post‐mortem, samples were divided into high, middle and low‐actomyosin dissociation groups. During 0.5–72 h post‐mortem, the phosphorylation level of MRLC significantly decreased (P < 0.05), while actomyosin dissociation, and degradation of MRLC and myosin heavy chains (MHC) significantly increased (P < 0.05). The level of MRLC phosphorylation was negatively correlated with the degree of actomyosin dissociation (r = −0.794, P < 0.05), and the degradation of MRLC (r = −0.764, P < 0.05) and MHC (r = −0.826, P < 0.05). In conclusion, phosphorylation of MRLC may regulate actomyosin dissociation, as well as degradation of MRLC and MHC.

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Phosphorylation of myofibrillar proteins in post‐mortem ovine muscle with different tenderness

Abstract: Protein phosphorylation may influence meat rigor mortis through contractile machinery and glycolysis, which in turn affect meat tenderness.

Cited by 80 publications

References 46 publications

Differences in Beef Quality between Angus (Bos taurus taurus) and Nellore (Bos taurus indicus) Cattle through a Proteomic and Phosphoproteomic Approach

Differences in Beef Quality between Angus (Bos taurus taurus) and Nellore (Bos taurus indicus) Cattle through a Proteomic and Phosphoproteomic Approach

Effects of temperature on protein phosphorylation in postmortem muscle

Phosphorylation of myosin regulatory light chain affects actomyosin dissociation and myosin degradation

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