Chen, Li ; Université de Liège - ULiège > Doct. sc. agro. & ingé. biol. (Paysage)
Li, Z.; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing, 100193, China
Everaert, Nadia ; Université de Liège - ULiège > Agronomie, Bio-ingénierie et Chimie (AgroBioChem) > Ingénierie des productions animales et nutrition
Lametsch, R.; Department of Food Science, Faculty of Science, University of Copenhagen, Frederiksberg, DK-1958, Denmark
Zhang, D.; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing, 100193, China
Language :
English
Title :
Quantitative phosphoproteomic analysis of ovine muscle with different postmortem glycolytic rates
Aizawa, H., Yamada, S.-I., Xiao, T., Shimane, T., Hayashi, K., Qi, F., et al. Difference in glycogen metabolism (glycogen synthesis and glycolysis) between normal and dysplastic/malignant oral epithelium. Archives of Oral Biology 83 (2017), 340–347.
Baba, T., Kobayashi, H., Kawasaki, H., Mineki, R., Naito, H., Ohmori, D., Glyceraldehyde-3-phosphate dehydrogenase interacts with phosphorylated Akt resulting from increased blood glucose in rat cardiac muscle. FEBS Letters 584:13 (2010), 2796–2800.
Bell, R.A.V., Storey, K.B., P06: Posttranslational modification of glyceraldehyde-3-phosphate dehydrogenase from a hibernating mammal: Insight into cold-adaptation and structural diversity of a housekeeping enzyme. Cryobiology 69:1 (2014), 196–197.
Chaudhry, R., & Bhimji, S. S. (2018). Biochemistry, glycolysis. In StatPearls. Treasure Island (FL).
Chen, L., Li, Z., Li, X., Chen, J., Everaert, N., Zhang, D., The effect of sarcoplasmic protein phosphorylation on glycolysis in postmortem ovine muscle. International Journal of Food Science and Technology, 2018.
Chen, L., Li, X., Ni, N., Liu, Y., Chen, L., Wang, Z., et al. Phosphorylation of myofibrillar proteins in post-mortem ovine muscle with different tenderness. Journal of the Science of Food and Agriculture 96:5 (2016), 1474–1483.
D'Alessandro, A., Marrocco, C., Rinalducci, S., Mirasole, C., Failla, S., Zolla, L., Chianina beef tenderness investigated through integrated Omics. Journal of proteomics 75:14 (2012), 4381–4398.
D'Alessandro, A., Zolla, L., Meat science: From proteomics to integrated omics towards system biology. Journal of Proteomics 78 (2013), 558–577.
Gao, X., Li, X., Li, Z., Du, M., Zhang, D., Dephosphorylation of myosin regulatory light chain modulates actin–myosin interaction adverse to meat tenderness. International Journal of Food Science & Technology 52:6 (2017), 1400–1407.
Graves, J.D., Krebs, E.G., Protein phosphorylation and signal transduction. Pharmacology and Therapeutics 82:2–3 (1999), 111–121.
Gururaj, A., Barnes, C.J., Vadlamudi, R.K., Kumar, R., Regulation of phosphoglucomutase 1 phosphorylation and activity by a signaling kinase. Oncogene, 23(49), 2004, 8118.
Heeley, D.H., Watson, M.H., Mak, A.S., Dubord, P., Smillie, L.B., Effect of phosphorylation on the interaction and functional properties of rabbit striated muscle alpha alpha-tropomyosin. Journal of Biological Chemistry 264:5 (1989), 2424–2430.
Honikel, K.O., Conversion of muscle to meat|glycolysis. Encyclopedia of meat sciences, second ed., 2014, Academic Press, Oxford, 353–357.
Hou, J., Cui, Z., Xie, Z., Xue, P., Wu, P., Chen, X., et al. Phosphoproteome analysis of Rat L6 myotubes using reversed-phase C18 prefractionation and titanium dioxide enrichment. Journal of Proteome Research 9:2 (2010), 777–788.
Huang, H., Larsen, M.R., Karlsson, A.H., Pomponio, L., Costa, L.N., Lametsch, R., Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences. Proteomics 11:20 (2011), 4063–4076.
Huang, H., Larsen, M.R., Lametsch, R., Changes in phosphorylation of myofibrillar proteins during postmortem development of porcine muscle. Food Chemistry 134:4 (2012), 1999–2006.
Huang, H., Larsen, M.R., Palmisano, G., Dai, J., Lametsch, R., Quantitative phosphoproteomic analysis of porcine muscle within 24 h postmortem. Journal of Proteomics 106 (2014), 125–139.
Immonen, K., Puolanne, E., Variation of residual glycogen-glucose concentration at ultimate pH values below 5.75. Meat Science 55:3 (2000), 279–283.
Jiang, S., He, H., Tan, L., Wang, L., Su, Z., Liu, Y., et al. Proteomic and phosphoproteomic analysis of renal cortex in a salt-load rat model of advanced kidney damage. Scientific Reports, 6, 2016, 35906.
Jin, X., Wang, L.-S., Xia, L., Zheng, Y., Meng, C., Yu, Y., et al. Hyper-phosphorylation of α-enolase in hypertrophied left ventricle of spontaneously hypertensive rat. Biochemical and Biophysical Research Communications 371:4 (2008), 804–809.
Larsen, M.R., Thingholm, T.E., Jensen, O.N., Roepstorff, P., Jørgensen, T.J., Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Molecular and Cellular Proteomics 4:7 (2005), 873–886.
Li, Z., Li, M., Du, M., Shen, Q.W., Zhang, D., Dephosphorylation enhances postmortem degradation of myofibrillar proteins. Food Chemistry 245 (2018), 233–239.
Li, Z., Li, X., Gao, X., Shen, Q.W., Du, M., Zhang, D., Phosphorylation prevents in vitro myofibrillar proteins degradation by μ-calpain. Food Chemistry 218 (2017), 455–462.
Li, Z., Li, M., Li, X., Xin, J., Wang, Y., Shen, Q.W., et al. Quantitative phosphoproteomic analysis among muscles of different color stability using tandem mass tag labeling. Food Chemistry 249 (2018), 8–15.
Li, C.T., Wick, M., Improvement of the physicochemical properties of pale soft and exudative (PSE) pork meat products with an extract from mechanically deboned turkey meat (MDTM). Meat Science 58:2 (2001), 189–195.
Lindahl, G., Henckel, P., Karlsson, A.H., Andersen, H.J., Significance of early postmortem temperature and pH decline on colour characteristics of pork loin from different crossbreeds. Meat Science 72:4 (2006), 613–623.
Lundby, A., Secher, A., Lage, K., Nordsborg, N.B., Dmytriyev, A., Lundby, C., et al. Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. Nature Communications, 3, 2012, 876.
Luther, M.A., Lee, J.C., The role of phosphorylation in the interaction of rabbit muscle phosphofructokinase with F-actin. Journal of Biological Chemistry 261:4 (1986), 1753–1759.
Marsin, A.S., Bertrand, L., Rider, M.H., Deprez, J., Beauloye, C., Vincent, M.F., et al. Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia. Current Biology 10:20 (2000), 1247–1255.
Melody, J., Lonergan, S.M., Rowe, L., Huiatt, T.W., Mayes, M.S., Huff-Lonergan, E., Early postmortem biochemical factors influence tenderness and water-holding capacity of three porcine muscles1. Journal of Animal Science 82:4 (2004), 1195–1205.
Muroya, S., Ohnishi-Kameyama, M., Oe, M., Nakajima, I., Shibata, M., Chikuni, K., Double phosphorylation of the myosin regulatory light chain during rigor mortis of bovine longissimus muscle. Journal of Agricultural and Food Chemistry 55:10 (2007), 3998–4004.
Paredi, G., Raboni, S., Bendixen, E., de Almeida, A.M., Mozzarelli, A., “Muscle to meat” molecular events and technological transformations: The proteomics insight. Journal of Proteomics 75:14 (2012), 4275–4289.
Reiss, N., Kanety, H., Schlessinger, J., Five enzymes of the glycolytic pathway serve as substrates for purified epidermal-growth-factor-receptor kinase. Biochemical Journal 239:3 (1986), 691–697.
Sale, E.M., White, M.F., Kahn, C.R., Phosphorylation of glycolytic and gluconeogenic enzymes by the insulin receptor kinase. Journal of Cellular Biochemistry 33:1 (1987), 15–26.
Schwägele, F., Buesa, P.L.L., Honikel, K.O., Enzymological investigations on the causes for the PSE-syndrome, II. Comparative studies on glycogen phosphorylase from pig muscles. Meat Science 44:1 (1996), 41–53.
Shen, Q.W., Du, M., Role of AMP-activated protein kinase in the glycolysis of postmortem muscle. Journal of the Science of Food and Agriculture 85:14 (2005), 2401–2406.
Shen, Q., Means, W., Thompson, S., Underwood, K., Zhu, M., McCormick, R., et al. Pre-slaughter transport, AMP-activated protein kinase, glycolysis, and quality of pork loin. Meat Science 74:2 (2006), 388–395.
Werner, C., Natter, R., Wicke, M., Changes of the activities of glycolytic and oxidative enzymes before and after slaughter in the longissimus muscle of Pietrain and Duroc pigs and a Duroc-Pietrain crossbreed. Journal of Animal Science 88:12 (2010), 4016–4025.
Zhang, B., Liu, J.Y., Serine phosphorylation of the cotton cytosolic pyruvate kinase GhPK6 decreases its stability and activity. FEBS Open Bio 7:3 (2017), 358–366.
Zhu, Y., Xu, H., Chen, H., Xie, J., Shi, M., Shen, B., Peng, C., Proteomic analysis of solid pseudopapillary tumor of the pancreas reveals dysfunction of the endoplasmic reticulum protein processing pathway. Mol Cell Proteomics 13:10 (2014), 2593–2603.