Quantitative phosphoproteomic analysis of ovine muscle with different postmortem glycolytic rates

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Quantitative phosphoproteomic analysis of ovine muscle with different postmortem glycolytic rates. / Chen, Li; Li, Zheng; Everaert, Nadia; Lametsch, Rene; Zhang, Dequan.

In: Food Chemistry, Vol. 280, 2019, p. 203-209.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Chen, L, Li, Z, Everaert, N, Lametsch, R & Zhang, D 2019, 'Quantitative phosphoproteomic analysis of ovine muscle with different postmortem glycolytic rates', Food Chemistry, vol. 280, pp. 203-209. https://doi.org/10.1016/j.foodchem.2018.12.056

APA

Chen, L., Li, Z., Everaert, N., Lametsch, R., & Zhang, D. (2019). Quantitative phosphoproteomic analysis of ovine muscle with different postmortem glycolytic rates. Food Chemistry, 280, 203-209. https://doi.org/10.1016/j.foodchem.2018.12.056

Vancouver

Chen L, Li Z, Everaert N, Lametsch R, Zhang D. Quantitative phosphoproteomic analysis of ovine muscle with different postmortem glycolytic rates. Food Chemistry. 2019;280:203-209. https://doi.org/10.1016/j.foodchem.2018.12.056

Author

Chen, Li ; Li, Zheng ; Everaert, Nadia ; Lametsch, Rene ; Zhang, Dequan. / Quantitative phosphoproteomic analysis of ovine muscle with different postmortem glycolytic rates. In: Food Chemistry. 2019 ; Vol. 280. pp. 203-209.

Bibtex

@article{0769a8e647284a4eb71ee05e560cb539,
title = "Quantitative phosphoproteomic analysis of ovine muscle with different postmortem glycolytic rates",
abstract = "Phosphorylation regulates protein structure, function, cell signaling and enzyme activities within cells. Postmortem changes of muscle to meat are partially determined by the structure, function and enzyme activities of proteins. To further understand the mechanisms regulating postmortem changes, ovine muscles with different glycolytic rates were subjected to quantitative phosphoproteomic analysis. Totally 116 unique phosphopeptides matched to 99 phosphoproteins were detected to be different in abundance among the fast, moderate and slow glycolytic rate muscles. Of which, 24 phosphoproteins clustered into glycolysis and muscle contraction were selected after bioinformatics analysis. Quantitative analysis showed that phosphorylation of pyruvate kinase, phosphoglucomutase 1, enolase and fructose-bisphosphate aldolase was correlated with glycolytic rate early postmortem. In addition, some myofibrillar proteins were detected to be differentially phosphorylated. In summary, this study revealed that protein phosphorylation at early postmortem may indirectly affect the glycolysis pathway through the regulation of proteins involved in glycolysis and muscle contraction.",
keywords = "Glycolysis, Glycolytic rate, Muscle contraction, Phosphoproteomic, Protein phosphorylation",
author = "Li Chen and Zheng Li and Nadia Everaert and Rene Lametsch and Dequan Zhang",
year = "2019",
doi = "10.1016/j.foodchem.2018.12.056",
language = "English",
volume = "280",
pages = "203--209",
journal = "Food Chemistry",
issn = "0308-8146",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Quantitative phosphoproteomic analysis of ovine muscle with different postmortem glycolytic rates

AU - Chen, Li

AU - Li, Zheng

AU - Everaert, Nadia

AU - Lametsch, Rene

AU - Zhang, Dequan

PY - 2019

Y1 - 2019

N2 - Phosphorylation regulates protein structure, function, cell signaling and enzyme activities within cells. Postmortem changes of muscle to meat are partially determined by the structure, function and enzyme activities of proteins. To further understand the mechanisms regulating postmortem changes, ovine muscles with different glycolytic rates were subjected to quantitative phosphoproteomic analysis. Totally 116 unique phosphopeptides matched to 99 phosphoproteins were detected to be different in abundance among the fast, moderate and slow glycolytic rate muscles. Of which, 24 phosphoproteins clustered into glycolysis and muscle contraction were selected after bioinformatics analysis. Quantitative analysis showed that phosphorylation of pyruvate kinase, phosphoglucomutase 1, enolase and fructose-bisphosphate aldolase was correlated with glycolytic rate early postmortem. In addition, some myofibrillar proteins were detected to be differentially phosphorylated. In summary, this study revealed that protein phosphorylation at early postmortem may indirectly affect the glycolysis pathway through the regulation of proteins involved in glycolysis and muscle contraction.

AB - Phosphorylation regulates protein structure, function, cell signaling and enzyme activities within cells. Postmortem changes of muscle to meat are partially determined by the structure, function and enzyme activities of proteins. To further understand the mechanisms regulating postmortem changes, ovine muscles with different glycolytic rates were subjected to quantitative phosphoproteomic analysis. Totally 116 unique phosphopeptides matched to 99 phosphoproteins were detected to be different in abundance among the fast, moderate and slow glycolytic rate muscles. Of which, 24 phosphoproteins clustered into glycolysis and muscle contraction were selected after bioinformatics analysis. Quantitative analysis showed that phosphorylation of pyruvate kinase, phosphoglucomutase 1, enolase and fructose-bisphosphate aldolase was correlated with glycolytic rate early postmortem. In addition, some myofibrillar proteins were detected to be differentially phosphorylated. In summary, this study revealed that protein phosphorylation at early postmortem may indirectly affect the glycolysis pathway through the regulation of proteins involved in glycolysis and muscle contraction.

KW - Glycolysis

KW - Glycolytic rate

KW - Muscle contraction

KW - Phosphoproteomic

KW - Protein phosphorylation

U2 - 10.1016/j.foodchem.2018.12.056

DO - 10.1016/j.foodchem.2018.12.056

M3 - Journal article

C2 - 30642488

AN - SCOPUS:85059115393

VL - 280

SP - 203

EP - 209

JO - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

ER -

ID: 212302216