Analysis of Methionine Oxidation in Myosin Isoforms in Porcine Skeletal Muscle by LC-MS/MS Analysis |
Jeong, Jin-Yeon
(Institute of Agriculture & Life Science, Gyeongsang National University)
Jung, Eun-Young (Division of Applied Life Science (BK21 plus), Gyeongsang National University) Jeong, Tae-Chul (Institute of Agriculture & Life Science, Gyeongsang National University) Yang, Han-Sul (Institute of Agriculture & Life Science, Gyeongsang National University) Kim, Gap-Don (Institute of Agriculture & Life Science, Gyeongsang National University) |
1 | Chen, M. and Cook, K. D. (2007) Oxidation artifacts in the electrospray mass spectrometry of Aβ peptide. Anal. Chem. 79, 2031-2036. DOI |
2 | Abreu, E., Quirox-Rothe, E., Mayoral, A. I., Vivo, J. M., Robina, Á., Guillén, M. T., Agüera, E., and Rivero, J. L. (2006) Myosin heavy chain fibre types and fibre sizes in nulliparous and primiparous ovariectomized Iberian sows: Interaction with two alternative rearing systems during the fattening period. Meat Sci. 74, 359-372. DOI |
3 | Armenteros, M. Heinonen, M., Ollilainen, V., Toldrá, F., and Estévez, M. (2009) Analysis of protein carbonyls in meat products by using the DNPH method, fluorescence spectroscopy and liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS). Meat Sci. 83, 104-112. DOI |
4 | Bernevic, B., Petre, B. A., Galetskiy, D., Werner, C., Wicke, M., Schellander, K., and Przybylski, M. (2011) Degradation and oxidation postmortem of myofibrillar proteins in porcine skeleton muscle revealed by high resolution mass spectrometric proteome analysis. Int. J. Mass Spectrom. 305, 217-227. DOI |
5 | Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254. DOI |
6 | Chang, K. C., Costa, N., Blackley, R., Southwood, O., Evans, G., Plastow, G., Wood, J. D., and Richardson, R. I. (2003) Relationships of myosin heavy chain fibre types to meat quality traits in traditional and modern pigs. Meat Sci. 64, 93-103. DOI |
7 | Choi, Y. M., Ryu, Y. C., and Kim, B. C. (2007) Influence of myosin heavy- and light chain isoforms on early postmortem glycolytic rate and pork quality. Meat Sci. 76, 281-288. DOI |
8 | Coirault, C., Guellich, A., Barbry, T., Samuel, J. L., Riou, B., and Lecarpentier, Y. (2007) Oxidative stress of myosin contributes to skeletal muscle dysfunction in rats with chronic heart failure. Am. J. Physiol. Heart Circ. Physiol. 292, H1009-H1017. DOI |
9 | Daneshvar, B., Frandsen, H., Artrup, H., and Dragsted, L. O. (1997) γ-Glutamyl semialdehyde and α-amino-adipic semialdehyde: Biomarkers of oxidative damage to proteins. Biomarkers 2, 117-123. DOI |
10 | Decker, E. A., Xiong, Y. L., Calvert, J. T., Crum, A. D., and Blanchard, S. P. (1993) Chemical, physical, and functional-properties of oxidized turkey white muscle myofibrillar proteins. J. Agric. Food Chem. 41, 186-189. DOI |
11 | Erickson, J. R., Joiner, M. L., Guan, X., Kutschke, W., Yang, J., Oddis, C. V., Bartlett, R. K., Lowe, J. S., O’Donnell, S. E., Aykin-Burns, N., Zimmerman, M. C., Zimmerman, K. M, Ham, A. J., Weiss, R. M., Spitz, D. R., Shea, M. A., Colbrau, R. J., Mohler, P. J., and Anderson, M. E. (2008) A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation. Cell 133, 462-474. DOI |
12 | Ghesquière, B. and Gevaert, K. (2014) Proteomics methods to study methionine oxidation. Mass Spectrom. Rev. 33, 147-156. DOI |
13 | Ghesquière, B., Jonckheere, V., Colaert, N., Van Durme, J., Timmerman, E., Goethals, M., Schymkowita, J., Rousseau, F., Vandekerckhove, J., and Gevaert, K. (2011) Redox proteomics of protein-bound methionine oxidation. Mol. Cell Proteomics 10, M110.006866. |
14 | Estévez, M., Ollilainen, V., and Heinonen, M. (2009) Analysis of protein oxidation markers α-aminoadipic and γ-glutamic semialdehydes in food proteins using liquid chromatography (LC)-electrospray ionization (ESI)-multistage tandem mass spectrometry (MS). J. Agric. Food Chem. 57, 3901-3910. DOI |
15 | Garrison, W. M. (1987) Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins. Chem. Rev. 87, 381-398. DOI |
16 | Hanan, T. and Shaklai, N. (1995) Peroxidative interaction of myoglobin and myosin. Eur. J. Biochem. 233, 930-936. DOI |
17 | Hardine, S. C., Larue, C. T., Oh, M. H., Jain, V., and Huber, S. C. (2009) Coupling oxidative signals to protein phosphorylation via methionine oxidation in Arabidopsis. Biochem. J. 422, 305-312. DOI |
18 | Jongberg, S., Gislason, N. E., Lund, M. N., Skibsted, L. H., and Waterhouse, A. L. (2011) Thiol-quinone adduct formation in myofibrillar proteins detected by LC-MS. J. Agric. Food Chem. 59, 6900-6905. DOI |
19 | Kim, G. D. (2014) Analysis of myosin heavy chain isoforms from logissimus toracis muscle of Hanwoo steer by electrophoresis and LC-MS/MS. Korean J. Food Sci. An. 34, 656-664. DOI |
20 | Kim, G. D., Jeong, J. Y., Yang, H. S., and Joo, S. T. (2015) Analysis of oxidized methionione in myosin isoforms of porcine longissimus thoracis muscle at 24 h postmortem. Proceed. 61st Int. Cong. Meat Sci. Technol., Clermont-Ferrand, France, pp. 163. |
21 | Levine, R. L. (1984) Mixed-function oxidation of histidine residues. Methods Enzymol. 107, 370-376. DOI |
22 | Kim, G. D., Ryu, Y. C., Jeong, J. Y., Yang, H. S., and Joo, S. T. (2013) Relationship between pork quality and characteristics of muscle fibers classified by the distribution of myosin heavy chain isoforms. J. Anim. Sci. 91, 5525-5534. DOI |
23 | Kim, G. D., Ryu, Y. C., Jo, C., Lee, J. G., Yang, H. S., Jeong, J. Y., and Joo, S. T. (2014) The characteristics of myosin heavy chain-based fiber types in porcine longissimus dorsi muscle. Meat Sci. 96, 712-718. DOI |
24 | Lefaucheur, L., Ecolan, P., Plantard, L., and Gueguen, N. (2002) New insights into muscle fiber types in the pig. J. Histochem. Cytochem. 50, 719-730. DOI |
25 | Liu, H., Ponniah, G., Neill, A., Patel, R., and Andrien, B. (2013) Accurate determination of protein methionine oxidation by stable isotope labelling and LC-MS analysis. Anal. Chem. 85, 11705-11709. DOI |
26 | Lund, M. N., Heinonen, M., Baron, C. P., and Estévez, M. (2011) Protein oxidation in muscle foods: A review. Mol. Nutr. Food Res. 55, 83-95. DOI |
27 | Lund, M. N., Lametsch, R., Hviid, M. S., Jensen, O. N., and Skibsted, L. H. (2007) High-oxygen packaging atmosphere influences protein oxidation and tenderness of porcine longissimus dorsi during chill storage. Meat Sci. 77, 295-303. DOI |
28 | Lund, M. N., Luxford, C., Skibsted, L. H., and Davies, M. J. (2008) Oxidation of myosin by heam proteins generates myosin radicals and protein cross-links. Biochem. J. 410, 565-574. DOI |
29 | Rayment, I. Rypniewski, W. R., Schmidt-Base, K., Smith, R., Tomchick, D. R., Benning, M. M., Winkelmann, D. A., Wesenberg, G., and Holden, H. M. (1993) Three dimensional structure of myosin subfragment-1: A molecular motor. Science 261, 50-58. DOI |
30 | Martinaud, A., Mercier, Y., Marinova, P., Tassy, C. Gatellier, P., and Renerre, M. (1997) Comparison of oxidative processes on myofibrillar proteins from beef during maturation and by different model oxidation systems. J. Agric. Food Chem. 45, 2481-2487. DOI |
31 | Oh-Ishie, M., Ueno, T., and Maeda, T. (2003) Proteomic method detects oxidatively induced protein carbonyls in muscles of a diabetes model Otsuka Long-Evans Tokushima fatty (Oletf) rat. Free Radical Biol. Med. 34, 11-22. DOI |
32 | Oliver, C. N., Ahn, B. W., Moerman, E. J., Goldstein, S., and Stadtman, E. R. (1987) Age-related changes in oxidized proteins. J. Biol. Chem. 262, 5488-5491. |
33 | Park, S., K., Gunawan, A. M., Scheffler, T. L., Grant, A. L., and Gerrard, D. E. (2009) Myosin heavy chain isoform content and energy metabolism can be uncoupled in pig skeletal muscle. J. Anim. Sci. 87, 522-531. |
34 | Rowe, L. J., Maddock, K. R., Lonergan, S. M., and Huff-Lonergan, E. (2004) Influence of early postmortem protein oxidation on beef quality. J. Anim. Sci. 82, 785-793. DOI |
35 | Shacter, E. (2000) Quantification and significance of protein oxidation in biological samples. Drug Met. Rev. 32, 307-326. DOI |
36 | Soladoye, O. P., Juárez, M. L., Aalhus, J. L., Shand, P., and Estévez, M. (2015) Protein oxidation in processed meat: Mechanisms and potential implications on human health. Compr. Rev. Food Sci. F. 14, 106-122. DOI |
37 | Stadtman, E. R. and Levine, R. L. (2003) Free radical-mediated oxidation of free amino acids and amino acid residues in proteins. Amino Acids 25, 207-218. DOI |
38 | Stadtman, E. R. (1993) Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu. Rev. Biochem. 62, 797-821. DOI |
39 | Stadtman, E. R. and Berlett, B. S. (1988) Fenton chemistry revisited: Amino acid oxidation. Basic Life Sci. 49, 131-136. |
40 | Winterbourn, C. C. (1990) Oxidative reactions of hemoglobin. Methods Enzymol. 186, 265-272. DOI |
41 | Tokunaga, M. Sutoh, K. Toyoshima, C. and Wayabashi, T. (1987) Location of the ATPase site of myosin determined by three-dimensional electron microscopy. Nature 329, 635-638. DOI |
42 | Vogt, W. (1995) Oxidation of methionyl residues in proteins: Tools, targets, and reversal. Free Radic. Biol. Med. 18, 93-105. DOI |
43 | Xiong, Y. L. (2000) Protein oxidation and implications for muscle food quality. In: Decker, E., Faustman, C., Clemente, J. L. B., Antioxidant in muscle foods. Chichester, UK, Wiley. pp. 85-111. |
![]() |