The effect of sarcoplasmic protein phosphorylation on glycolysis in postmortem ovine muscle

Chen, Li; Li, Zheng; Li, Xin; Chen, Jing; Everaert, Nadia; Zhang, Dequan

doi:10.1111/ijfs.13882

Cited by 26 publications

(18 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…After 1 day's storage, the phosphorylation levels of glucose‐6‐phosphate isomerase and pyruvate kinase (band 10) were higher at 25 °C. Consistently, Chen et al . reported that the phosphorylation levels of glucose‐6‐phosphate isomerase and pyruvate kinase were positively correlated with the glycolytic rate.…”

Section: Resultsmentioning

confidence: 53%

“…14 A negative correlation between the phosphorylation level of adenylate kinase isoenzyme 1 (band 18) and ATP content indicated that phosphorylated adenylate kinase isoenzyme 1 may contribute to muscle rigor and contraction. In band 10, the phosphorylation level changes at 25 and 15 ∘ C were inconsistent with those at 4 and −1.5 ∘ C. After 1 day's storage, the phosphorylation levels of glucose-6-phosphate isomerase and pyruvate kinase (band 10) were higher at 25 ∘ C. Consistently, Chen et al 17 reported that the phosphorylation levels of glucose-6-phosphate isomerase and pyruvate kinase were positively correlated with the glycolytic rate. Moreover, Schwägele et al 33 showed that the phosphorylated isoform of pyruvate kinase can have higher acid stability, indicating that phosphorylated pyruvate kinase can maintain high activity at low pH.…”

Section: Analysis Of the Phosphorylation Levels Of Individual Bands Amentioning

confidence: 77%

“…The rate and extent of a decline in pH are influenced by the phosphorylation state of the glycolytic enzymes and play an important role in meat quality . The pH values of the muscle samples stored at various temperatures are presented in Fig.…”

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

Effects of temperature on protein phosphorylation in postmortem muscle

Ren

Hou

et al. 2019

J Sci Food Agric

Self Cite

View full text Add to dashboard Cite

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

show abstract

Section: Resultsmentioning

confidence: 53%

Section: Analysis Of the Phosphorylation Levels Of Individual Bands Amentioning

confidence: 77%

See 1 more Smart Citation

Effects of temperature on protein phosphorylation in postmortem muscle

Ren

Hou

et al. 2019

J Sci Food Agric

Self Cite

View full text Add to dashboard Cite

show abstract

“…Glycolysis is a multistep conversion of glucose to pyruvate catalyzed by specific enzymes. Most of these enzymes, such as glycogen phosphorylase, phosphofructokinase, and pyruvate kinase, are identified as phosphoproteins and affect meat quality characteristics by regulating glycolysis cycle, protein degradation, and structure of meat (Chen et al., 2018; Huang, Larsen, et al., 2011; Wu et al., 2015; Scheffler & Gerrard, 2007; Li et al., 2012). As the core metabolic pathway in postmortem muscle, glycolysis is highly relevant to ultimate meat quality (Dalrymple & Hamm, 1975; Lomiwes, Farouk, Wu, & Young, 2014).…”

Section: Protein Phosphorylationmentioning

confidence: 99%

Effects of protein posttranslational modifications on meat quality: A review

Zhang

Ren

et al. 2020

Comp Rev Food Sci Food Safe

Self Cite

View full text Add to dashboard Cite

Meat quality plays an important role in the purchase decision of consumers, affecting producers and retailers. The formation mechanisms determining meat quality are intricate, as several endogenous and exogenous factors contribute during antemortem and postmortem periods. Abundant research has been performed on meat quality; however, unexpected variation in meat quality remains an issue in the meat industry. Protein posttranslational modifications (PTMs) regulate structures and functions of proteins in living tissues, and recent reports confirmed their importance in meat quality. The objective of this review was to provide a summary of the research on the effects of PTMs on meat quality. The effects of four common PTMs, namely, protein phosphorylation, acetylation, S‐nitrosylation, and ubiquitination, on meat quality were discussed, with emphasis on the effects of protein phosphorylation on meat tenderness, color, and water holding capacity. The mechanisms and factors that may affect the function of protein phosphorylation are also discussed. The current research confirms that meat quality traits are regulated by multiple PTMs. Cross talk between different PTMs and interactions of PTMs with postmortem biochemical processes need to be explored to improve our understanding on factors affecting meat quality.

show abstract

“…Meanwhile, GAPDH, which is an enzyme involved in glycolysis, was shown to be hyperphosphorylated after the Al 3 + treatment (Fig 4). The enzyme was activated by phosphorylation [48], and then, Al 3+ stress accelerated the glycolytic rate. Citric acid metabolism, as part of the tricarboxylic acid (TCA) cycle, occurs in mitochondria.…”

Section: Dpps Promotes Citric Acid Synthesis Under Al 3+ Stressmentioning

confidence: 99%

Quantitative phosphoproteomic analysis provides insights into the aluminum-responsiveness of Tamba black soybean

et al. 2020

View full text Add to dashboard Cite

Aluminum (Al 3+) toxicity is one of the most important limitations to agricultural production worldwide. The overall response of plants to Al 3+ stress has been documented, but the contribution of protein phosphorylation to Al 3+ detoxicity and tolerance in plants is unclear. Using a combination of tandem mass tag (TMT) labeling, immobilized metal affinity chromatography (IMAC) enrichment and liquid chromatography-tandem mass spectrometry (LC-MS/MS), Al 3+-induced phosphoproteomic changes in roots of Tamba black soybean (TBS) were investigated in this study. The Data collected in this study are available via ProteomeXchange with the identifier PXD019807. After the Al 3+ treatment, 189 proteins harboring 278 phosphosites were significantly changed (fold change > 1.2 or < 0.83, p < 0.05), with 88 upregulated, 96 downregulated and 5 up-/downregulated. Enrichment and protein interaction analyses revealed that differentially phosphorylated proteins (DPPs) under the Al 3+ treatment were mainly related to G-protein-mediated signaling, transcription and translation, transporters and carbohydrate metabolism. Particularly, DPPs associated with root growth inhibition or citric acid synthesis were identified. The results of this study provide novel insights into the molecular mechanisms of TBS post-translational modifications in response to Al 3+ stress.

show abstract

The effect of sarcoplasmic protein phosphorylation on glycolysis in postmortem ovine muscle

Cited by 26 publications

References 30 publications

Effects of temperature on protein phosphorylation in postmortem muscle

Effects of temperature on protein phosphorylation in postmortem muscle

Effects of protein posttranslational modifications on meat quality: A review

Quantitative phosphoproteomic analysis provides insights into the aluminum-responsiveness of Tamba black soybean

Contact Info

Product

Resources

About