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 China
Li, X.
Chen, J.; Institute of Food Science and Technology Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing Ministry of Agriculture Beijing China
Everaert, Nadia ; Université de Liège - ULiège > Agronomie, Bio-ingénierie et Chimie (AgroBioChem) > Ingénierie des productions animales et nutrition
Zhang, D.; Institute of Food Science and Technology Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing Ministry of Agriculture Beijing China
Language :
English
Title :
The effect of sarcoplasmic protein phosphorylation on glycolysis in postmortem ovine muscle
Publication date :
2018
Journal title :
International Journal of Food Science and Technology
Aizawa, H., Yamada, S.-I., Xiao, T. et al. (2017). Difference in glycogen metabolism (glycogen synthesis and glycolysis) between normal and dysplastic/malignant oral epithelium. Archives of Oral Biology, 83, 340–347.
Amiri, M., Conserva, F., Panayiotou, C., Karlsson, A. & Solaroli, N. (2013). The human adenylate kinase 9 is a nucleoside mono- and diphosphate kinase. The International Journal of Biochemistry & Cell Biology, 45, 925–931.
Briskey, E.J. (1964). Etiological status and associated studies of pale, soft, exudative porcine musculature. Advances in Food Research, 13, 89–178.
Chen, L., Li, X., Ni, N. et al. (2016). Phosphorylation of myofibrillar proteins in post-mortem ovine muscle with different tenderness. Journal of the Science of Food and Agriculture, 96, 1474–1483.
Dzeja, P. & Terzic, A. (2009). Adenylate kinase and AMP signaling networks: Metabolic monitoring, signal communication and body energy sensing. International Journal of Molecular Sciences, 10, 1729–1772.
Graves, J.D. & Krebs, E.G. (1999). Protein phosphorylation and signal transduction. Pharmacology & Therapeutics, 82, 111–121.
Gupta, V. & Bamezai, R.N. (2010). Human pyruvate kinase M2: A multifunctional protein. Protein Science, 19, 2031–2044.
Gururaj, A., Barnes, C.J., Vadlamudi, R.K. & Kumar, R. (2004). Regulation of phosphoglucomutase 1 phosphorylation and activity by a signaling kinase. Oncogene, 23, 8118–8127.
Højlund, K., Bowen, B.P., Hwang, H. et al. (2009). In vivo phosphoproteome of human skeletal muscle revealed by phosphopeptide enrichment and HPLC− ESI− MS/MS. Journal of Proteome Research, 8, 4954–4965.
Honikel, K.O. (2014). Conversion of muscle to meat. In: (edited by Michael Dikeman, Carrick Devine, Encyclopedia of Meat Sciences (Second Edition), Pp. 353–357. Glycolysis Encyclopedia of Meat Sciences, 2nd ed. Pp. 353–357 Oxford: Academic Press.
Huang, H., Larsen, M.R., Karlsson, A.H., Pomponio, L., Costa, L.N. & Lametsch, R. (2011). Gelnt and HPLC− ESI− MS/MS. activity by a signaling kiroteins in postmortem porcine muscle with pH decline rate and time differences. Proteomics, 11, 4063–4076.
Huang, H., Larsen, M.R. & Lametsch, R. (2012). Changes in phosphorylation of myofibrillar proteins during postmortem development of porcine muscle. Food Chemistry, 134, 1999–2006.
Hunter, T. (2000). Signaling—2000 and beyond. Cell, 100, 113–127.
Immonen, K. & Puolanne, E. (2000). Variation of residual glycogen-glucose concentration at ultimate pH values below 5.75. Meat Science, 55, 279–283.
Jin, X., Wang, L.-S., Xia, L. et al. (2008). Hyper-phosphorylation of α-enolase in hypertrophied left ventricle of spontaneously hypertensive rat. Biochemical and Biophysical Research Communications, 371, 804–809.
Johnson, L. (1992). Glycogen phosphorylase: Control by phosphorylation and allosteric effectors. The FASEB Journal, 6, 2274–2282.
Li, M., Li, X., Xin, J. et al. (2017a). Effects of protein phosphorylation on color stability of ground meat. Food Chemistry, 219, 304–310.
Li, X., Chen, L., He, F., Li, M., Shen, Q. & Zhang, D. (2017b). A comparative analysis of phosphoproteome in ovine muscle at early postmortem in relationship to tenderness. Journal of the Science of Food and Agriculture, 97, 4571–4579.
Li, M., Li, Z., Li, X. et al. (2018). Comparative profiling of sarcoplasmic phosphoproteins in ovine muscle with different color stability. Food Chemistry, 240, 104–111.
Luther, M.A. & Lee, J.C. (1986). The role of phosphorylation in the interaction of rabbit muscle phosphofructokinase with F-actin. Journal of Biological Chemistry, 261, 1753–1759.
Marsin, A.S., Bertrand, L., Rider, M.H. et al. (2000). Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia. Current Biology, 10, 1247–1255.
Nettelblad, F.A. & Engström, L. (1987). The kinetic effects of in vitro phosphorylation of rabbit muscle enolase by protein kinase C: A possible new kind of enzyme regulation. FEBS Letters, 214, 249–252.
Ohlendieck, K. (2010). Proteomics of skeletal muscle glycolysis. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 1804, 2089–2101.
Scheffler, T. & Gerrard, D. (2007). Mechanisms controlling pork quality development: The biochemistry controlling postmortem energy metabolism. Meat Science, 77, 7–16.
Schwägele, F., Buesa, P.L.L. & Honikel, K.O. (1996a). Enzymological investigations on the causes for the PSE-syndrome, II. Comparative studies on glycogen phosphorylase from pig muscles. Meat Science, 44, 41–53.
Schwägele, F., Haschke, C., Honikel, K.O. & Krauss, G. (1996b). Enzymological investigations on the causes for the PSE-syndrome, I. Comparative studies on pyruvate kinase from PSE- and normal pig muscles. Meat Science, 44, 27–40.
Shen, Q., Means, W., Thompson, S. et al. (2006). Pre-slaughter transport, AMP-activated protein kinase, glycolysis, and quality of pork loin. Meat Science, 74, 388–395.
Sprang, S., Acharya, K., Goldsmith, E. et al. (1988). Structural changes in glycogen phosphorylase induced by phosphorylation. Nature, 336, 215.
Wang, Z., Zhang, C., Li, Z., Shen, Q. & Zhang, D. (2017). Comparative analysis of muscle phosphoproteome induced by salt curing. Meat Science, 133, 19–25.
Zhang, B. & Liu, J.Y. (2017). Serine phosphorylation of the cotton cytosolic pyruvate kinase GhPK6 decreases its stability and activity. FEBS Open Bio, 7, 358–366.
