Quantitative phosphoproteomic analysis of caprine muscle with high and low meat quality

Liu, Manshun; Wei, Yanchao; Li, Xin; Quek, Siew Young; Zhao, Jing; Zhong, Huazhen; Zhang, Dequan; Liu, Yongfeng

doi:10.1016/j.meatsci.2018.01.001

Cited by 23 publications

(24 citation statements)

References 46 publications

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“…In the 1% NaCl+0.06% L-his vs 1% NaCl treatment, serine was the most frequently phosphorylated sites (80.8%) followed by threonine (15.1%) and then tyrosine, which account for only 4.1% of the phosphorylated sites of differentially expressed phosphoprotein. This was in accordance with the results of Liu et al (2018), who also reported that serine residues were the most phosphorylated sites in caprine muscle. The assignment of the phosphorylation site information of differentially expressed phosphoproteins between NaCl and L-histidine treatments were listed in Table S1 (Supplementary data).…”

Section: Phosphorylation Level Of Depssupporting

confidence: 93%

Changes in phosphorylation of chicken breast muscle in response to L-histidine introduction under low-NaCl conditions

Chen

Guo

et al. 2021

CyTA - Journal of Food

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In an attempt to positively regulate meat quality at low NaCl concentration, the influence of L-histidine (L-his) introduction on the postmortem phosphorylation of chicken breast muscle protein that had been cured for 16 h at 1% NaCl was investigated at 90 min postmortem in the present study. The 633 different phosphoproteins (﹥1.2-fold) induced by L-his introduction during salting were identified, and a majority of these proteins were involved in glycolysis, calcium signalling pathway and muscle contraction. Myosin, actin, titin, troponin C (TnC), myosin lightchain kinase (MLCK) and γ-phosphorylase kinase (γ-PHK) were the main differentially expressed proteins (DEPs) that were associated with muscle contraction. An advantageous regulation of phosphoglucomutase-1 phosphorylation, fructose-1,6-bisphosphatase and pyruvate dehydrogenase E1 component was obtained in glycolytic metabolism after treatment with L-his. Cambios en la fosforilación del músculo de la pechuga de pollo en respuesta a la introducción de L-histidina en condiciones de bajo NaCl RESUMENEn un intento por regular positivamente la calidad de la carne a baja concentración de NaCl, el presente estudio investigó cómo influye la introducción de L-histidina (L-his) en la fosforilación postmortem de la proteína del músculo de la pechuga de pollo curada durante 16 horas a 1% de NaCl después de 90 minutos post-mortem. Los resultados de este procedimiento permitieron verificar la presencia de 633 fosfoproteínas diferentes (﹥1.2 veces) inducidas por la introducción de L-his durante la salazón; la mayoría de las mismas estaba implicada en la glucólisis, la vía de señalización del calcio y la contracción muscular. Además, se comprobó que las principales proteínas expresadas diferencialmente (DEPs) asociadas con la contracción muscular fueron la miosina, la actina, la titina, la troponina C (TnC), la cadena ligera de miosina quinasa (MLCK) y la γfosforilasa quinasa (γ-PHK). Al respecto, tras el tratamiento con L-hisse se obtuvo una regulación ventajosa de la fosforilación de la fosfoglucomutasa-1, la fructosa-1,6-bisfosfatasa y el componente E1 de la enzima piruvato deshidrogenasa en el metabolismo glucolítico.

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Section: Phosphorylation Level Of Depssupporting

confidence: 93%

Changes in phosphorylation of chicken breast muscle in response to L-histidine introduction under low-NaCl conditions

Chen

Guo

et al. 2021

CyTA - Journal of Food

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“…An in vitro study indicated that protein phosphorylation probably affected ovine meat color by regulating postmortem glycolysis and mediating myoglobin redox stability (Li et al., , ). Quantitative phosphoproteomic analysis of caprine muscle revealed that differential phosphorylation of proteins, including PFK, myosin light chain 2, and heat shock protein (HSP) 27, were observed to be critical biomarkers regulating muscle rigor mortis, which resulted in varying meat quality (Liu et al., ). Manipulating the phosphorylation level of myofibrillar proteins in vitro altered their proteolytic susceptibility to μ‐calpain.…”

Section: Potential Mechanism Regulating Meat Quality Developmentmentioning

confidence: 99%

“…Chen et al (2016) examined lamb muscle with different tenderness; using gel-based phosphoproteome profiling, they found a higher level of global phosphorylation in tough meat than in the tender meat, and the main differential proteins identified were correlated with the contractile machinery and glycolysis. An in vitro study indicated that protein phosphorylation probably affected ovine meat color by regulating postmortem glycolysis and mediating myoglobin redox stability (Li et al, 2017a(Li et al, , 2018. Quantitative phosphoproteomic analysis of caprine muscle revealed that differential phosphorylation of proteins, including PFK, myosin light chain 2, and heat shock protein (HSP) 27, were observed to be critical biomarkers regulating muscle rigor mortis, which resulted in varying meat quality (Liu et al, 2018).…”

Section: Protein Modificationmentioning

confidence: 99%

Stress Effects on Meat Quality: A Mechanistic Perspective

Xing

Gao

Tume

et al. 2018

Comp Rev Food Sci Food Safe

166

121

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Stress inevitably occurs from the farm to abattoir in modern livestock husbandry. The effects of stress on the behavioral and physiological status and ultimate meat quality have been well documented. However, reports on the mechanism of stress effects on physiological and biochemical changes and their consequent effects on meat quality attributes have been somewhat disjointed and limited. Furthermore, the causes of variability in meat quality traits among different animal species, muscle fibers within an animal, and even positions within a piece of meat in response to stress are still not entirely clear. This review 1st summarizes the primary stress factors, including heat stress, preslaughter handling stress, oxidative stress, and other stress factors affecting animal welfare; carcass quality; and eating quality. This review further delineates potential stress‐induced pathways or mediators, including AMP‐activated protein kinase‐mediated energy metabolism, crosstalk among calcium signaling pathways and reactive oxygen species, protein modification, apoptosis, calpain and cathepsin proteolytic systems, and heat shock proteins that exert effects that cause biochemical changes during the early postmortem period and affect the subsequent meat quality. To obtain meat of high quality, further studies are needed to unravel the intricate mechanisms involving the aforementioned signaling pathways or mediators and their crosstalk.

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“…Reversible phosphorylation by the concerted action of a complex network of protein kinases and protein phosphatases plays a key regulatory role in the biochemical processes underlying muscle contraction and metabolism during the post - mortem muscle-to-meat conversion [2–5]. Post - mortem changes in the phosphorylation status of myofibrillar proteins and glycolytic enzymes in bovine, ovine and porcine muscles have been linked to differences in the meat quality traits of tenderness and color stability [2, 4, 6–8]. The available evidence suggests that reversible phosphorylation of proteins involved in muscle contraction and glycolysis can influence meat quality due to its post - mortem effects on pH decline and the development of rigor mortis [4, 9–11].…”

Section: Introductionmentioning

confidence: 99%

The first evidence of global meat phosphoproteome changes in response to pre-slaughter stress

et al. 2019

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Background Pre-slaughter stress (PSS) impairs animal welfare and meat quality. Dark, firm and dry (DFD) are terms used to designate poor quality meats induced by PSS. Protein phosphorylation can be a potentially significant mechanism to explain rapid and multiple physiological and biochemical changes linked to PSS-dependent muscle-to-meat conversion. However, the role of reversible phosphorylation in the response to PSS is still little known. In this study, we report a comparative phosphoproteomic analysis of DFD and normal meats at 24 h post - mortem from the longissimus thoracis (LT) bovine muscle of male calves of the Rubia Gallega breed. For this purpose, two-dimensional gel electrophoresis (2-DE), in-gel multiplex identification of phosphoproteins with PRO-Q Diamond phosphoprotein-specific stain, tandem (MALDI-TOF/TOF) mass spectrometry (MS), novel quantitative phosphoproteomic statistics and bioinformatic tools were used. Results Noticeable and statistically significant differences in the extent of protein phosphorylation were detected between sample groups at the qualitative and quantitative levels. Overall phosphorylation rates across significantly changed phosphoproteins were about three times higher in DFD than in normal meat. Significantly changed phosphoproteins involved a variable number of isoforms of 13 myofibrillar and sarcoplasmic nonredundant proteins. However, fast skeletal myosin light chain 2 followed by troponin T, F-actin-capping and small heat shock proteins showed the greatest phosphorylation change, and therefore they were the most important phosphoproteins underlying LT muscle conversion to DFD meat in the Rubia Gallega breed. Conclusions This is the first study reporting global meat phosphoproteome changes in response to PSS. The results show that reversible phosphorylation is a relevant mechanism underlying PSS response and downstream effects on meat quality. This research opens up novel horizons to unravel the complex molecular puzzle underlying muscle-to-meat conversion in response to PSS. Electronic supplementary material The online version of this article (10.1186/s12864-019-5943-3) contains supplementary material, which is available to authorized users.

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Quantitative phosphoproteomic analysis of caprine muscle with high and low meat quality

Cited by 23 publications

References 46 publications

Changes in phosphorylation of chicken breast muscle in response to L-histidine introduction under low-NaCl conditions

Changes in phosphorylation of chicken breast muscle in response to L-histidine introduction under low-NaCl conditions

Stress Effects on Meat Quality: A Mechanistic Perspective

The first evidence of global meat phosphoproteome changes in response to pre-slaughter stress

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