Validation of protein biological markers of lamb meat quality characteristics based on the different muscle types

Huang, Caiyan; Zhang, Dequan; Wang, Zhenyu; Zhao, Yingxin; Blecker, Christophe; Li, Shaobo; Zheng, Xiaochun; Chen, Li

doi:10.1016/j.foodchem.2023.136739

Cited by 6 publications

(7 citation statements)

References 40 publications

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“…The degradation of desmin, troponin-T, and μ-calpain, and the relative abundance of caspase-3 were analyzed by western blotting approach. The detailed experimental procedure of western blotting was described as our previous study ( Huang et al, 2023 , Huang et al, 2023 ). The samples were lysed on ice by RIPA lysis buffer (Sigma, USA) added to protease inhibitor cocktail (Sigma, USA), and then the protein concentration was determined by the BCA protein assay kit (Thermo Fisher Scientific Inc. Waltham, MA).…”

Section: Methodsmentioning

confidence: 99%

“…The protein bands were performed using an ECL detection kit and captured using the ChemiDocTMMP imaging system. The targeted protein bands' intensity was analyzed according to our previous study ( Huang et al, 2023 , Huang et al, 2023 ). The muscle sample was collected at 30 min postmortem as a reference sample.…”

Section: Methodsmentioning

confidence: 99%

“…Among these isoforms, PKM2 plays an essential role in catalyzing the glycolysis final step, and its activity is subject to regulation by glycolytic intermediates ( Yang & Lu, 2015 ). Many studies have revealed that the different abundance of PGK1 and PKM2 proteins are closely related to meat quality attributes by proteomics approaches ( Huang et al, 2023 , Huang et al, 2023 , Kim et al, 2019 ). Moreover, Bai et al (2023) reported that the muscle chilling treatment could influence the PGK activity by regulate its phosphorylation and acetylation level, thus influencing the postmortem meat quality.…”

Section: Introductionmentioning

confidence: 99%

“…Furthermore, our previous studies have demonstrated a close association between the activity of PKM2 and PGK1 as well as lamb meat quality traits. They can be used as valuable biological markers for characterizing lamb meat quality ( Huang et al, 2023 , Huang et al, 2023 , Huang et al, 2023 , Huang et al, 2023 ). Therefore, based on current research progress, it has been primarily observed that PGK1 and PKM2 are closely associated with meat quality.…”

Section: Introductionmentioning

confidence: 99%

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Effects of phosphoglycerate kinase 1 and pyruvate kinase M2 on metabolism and physiochemical changes in postmortem muscle

Huang,

Zhang,

Blecker

et al. 2024

Food Chemistry: X

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Effects of phosphoglycerate kinase 1 and pyruvate kinase M2 on metabolism and physiochemical changes in postmortem muscle

Huang,

Zhang,

Blecker

et al. 2024

Food Chemistry: X

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“…2 A proteomics study found a decreasing expression of PKM during the post-mortem stage linked to low beef tenderness. 3 PKM is identified as a powerful predictor for lamb, 4 beef, 5 and pork 6 meat quality like tenderness, color, and water holding capacity. Besides the well-known role of PKM as a glycolytic enzyme, it also moonlights as a protein kinase upon phosphorylation by transferring the phosphoryl group from PEP to a protein substrate.…”

Section: ■ Introductionmentioning

confidence: 99%

Acetylation and Phosphorylation Regulate the Role of Pyruvate Kinase as a Glycolytic Enzyme or a Protein Kinase in Lamb

Ren,

Li,

et al. 2024

J. Agric. Food Chem.

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Protein post-translational modifications (PTMs) play an essential role in meat quality development. However, the effect of specific PTM sites on meat proteins has not been investigated yet. The characteristics of pyruvate kinase M (PKM) were found to exhibit a close correlation with final meat quality, and thus, serine 99 (S99) and lysine 137 (K137) in PKM were mutated to study their effect on PKM function. The structural and functional properties of five lamb PKM variants, including wild-type PKM (wtPKM), PKM_S99D (S99 phosphorylation), PKM_S99A (PKM S99 dephosphorylation), PKM_K137Q (PKM K137 acetylation), and PKM_K137R (PKM K137 deacetylation), were evaluated. The results showed that the secondary structure, tertiary structure, and polymer formation were affected among different PKM variants. In addition, the glycolytic activity of PKM_K137Q was decreased because of its weakened binding with phosphoenolpyruvate. In the PKM_K137R variant, the actin phosphorylation level exhibited a decrease, suggesting a low kinase activity of PKM_K137R. The results of molecular simulation showed a 42% reduction in the interface area between PKM_K137R and actin, in contrast to wtPKM and actin. These findings are significant for revealing the mechanism of how PTMs regulate PKM function and provide a theoretical foundation for the development of precise meat quality preservation technology.

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Integrated metabolome, proteome, and transcriptome analysis explored the molecular mechanism of phosphoglycerate kinase 1 and pyruvate kinase M2 characterizing the postmortem meat quality

Huang,

Xiang,

Wang

et al. 2024

Food Frontiers

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Phosphoglycerate kinase 1 (PGK1) and pyruvate kinase M2 (PKM2) have been identified as the postmortem meat quality biomarkers. However, the precise molecular mechanism through which they affect and regulate the development of meat quality remains unclear. In this work, the high‐ and low‐activity groups (n = 10) were selected from 60 lamb muscles at 24 h postmortem based on the activity levels of PGK1 and PKM2. The metabolomic, proteomic, and transcriptomic analyses combined with deeply integrated multi‐omics analysis were used to elucidate the mechanisms by which PGK1 and PKM2 characterize meat quality. The results indicated that glycolysis played a crucial role in regulating PGK1 and PKM2 activity at the metabolome, proteome, and transcriptome levels. In glycolysis pathway, we identified several key components closely related to PGK1 and PKM2 activity, including differential metabolites (adenosine triphosphate, adenosine diphosphate, glucose‐6‐phosphate, nicotinamide adenine dinucleotide phosphate, fructose‐6‐phosphate, dihydroxyacetone phosphate, 3‐phosphoglycerate, NAD+ nicotinamide adenine dinucleotide, lactate, and pyruvate), different abundance proteins (lactate dehydrogenase B and fructose bisphosphate aldolase B), and differentially expressed genes (hexokinase and fructose‐1,6‐bisphosphatase 1). It was concluded that PGK1 and PKM2 may affect the formation of meat quality by regulating these critical substrates. Additionally, PGK1 and PKM2 could also affect the tricarboxylic acid cycle, oxidative phosphorylation, and muscle contraction in postmortem and then influence meat quality. This integrative omics study offers valuable insight into unraveling the molecular mechanisms underlying postmortem meat quality development.

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Validation of protein biological markers of lamb meat quality characteristics based on the different muscle types

Cited by 6 publications

References 40 publications

Effects of phosphoglycerate kinase 1 and pyruvate kinase M2 on metabolism and physiochemical changes in postmortem muscle

Effects of phosphoglycerate kinase 1 and pyruvate kinase M2 on metabolism and physiochemical changes in postmortem muscle

Acetylation and Phosphorylation Regulate the Role of Pyruvate Kinase as a Glycolytic Enzyme or a Protein Kinase in Lamb

Integrated metabolome, proteome, and transcriptome analysis explored the molecular mechanism of phosphoglycerate kinase 1 and pyruvate kinase M2 characterizing the postmortem meat quality

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