Xiaolan Huang1, Xin Li
Received:2023-06-01
Revised:2023-07-13
Online:2023-07-25
Published:2023-07-25
Contact:
Xin Li
Supported by:CLC Number:
Xiaolan Huang Xin Li. Research progress on effects of post-translational modification of pyruvate kinase on meat quality[J]. FOOD SCIENCE.
| [1]张德权, 陈丽, 侯成立. 生鲜肉贮藏温度术语浅析[J]. 肉类研究, 2021,35(05):44-49. DOI:10.7506/rlyj1001-8123-20201118-267. [2]SMALL A, HEWITT L. Transport and pre-slaughter management[M].Advances in sheep welfare. Woodhead Publishing, 2017: 227-243. DOI:10.1016/B978-0-08-100718-1.00012-1. [3]黄琳琳, 张一敏, 朱立贤, 等. 蛋白质氧化和翻译后修饰对肉品质的影响及机制研究进展[J]. 食品科学, 2021,42(09):241-247. DOI:10.7506/spkx1002-6630-20200330-435. [4]JING Y, NIAN Y Q, ZOU B, et al. Acetylation inhibition alleviates energy metabolism in muscles of minipigs varying with the type of muscle fibers[J]. Meat Science, 2022, 184108699. DOI:10.1016/j.meatsci.2021.108699.[5]邹波, 李春保. 乙酰化、能量代谢与肉品品质的关联[J]. 肉类研究, 2019,33(08):58-64. DOI:10.7506rlyj1001-8123-20190617-134. [6]BAR-EVEN A, FLAMHOLZ A, NOOR E, et al. Rethinking glycolysis: on the biochemical logic of metabolic pathways[J]. Nature chemical biology, 2012, 8(6): 509-517. DOI:10.1038/NCHEMBIO.971.[7]ZHENG S, LIU Q, LIU T, et al. Posttranslational modification of pyruvate kinase type M2 (PKM2): novel regulation of its biological roles to be further discovered[J]. J Physiol Biochem, 2021,77(3):355-363. DOI:10.1007/s13105-021-00813-0.[8]WEERNINK P A, RIJKSEN G, MASCINI E M, et al. Phosphorylation of pyruvate kinase type K is restricted to the dimeric form[J]. Biochimica et biophysica acta, 1992,1121(1-2):61. DOI:10.1016/0167-4838(92)90337-D.[9]SCHORMANN N, HAYDEN K L, LEE P, et al. An overview of structure, function, and regulation of pyruvate kinases[J]. Protein Science, 2019,28(10):1771-1784. DOI:10.1002/pro.3691. [10]MORGAN H P, MCNAC I W, NOWICKI M W, et al. Allosteric mechanism of pyruvate kinase from Leishmania mexicana uses a rock and lock model[J]. Journal of Biological Chemistry, 2010, 285(17): 12892-12898. DOI: 10.1074/jbc.M109.079905.[11]LARSEN T M, LAUGHLIN L T, HOLDEN H M, et al. Structure of rabbit muscle pyruvate kinase complexed with Mn2+, K+, and pyruvate[J]. Biochemistry, 1994, 33(20): 6301-6309. DOI:10.1021/bi00186a033. [12]OU Y, TAO W, ZHANG Y, et al. The conformational change of rabbit muscle pyruvate kinase induced by activating cations and its substrates[J]. International journal of biological macromolecules, 2010, 47(2): 228-232. DOI:10.1016/j.ijbiomac.2010.04.017.[13]NANDI S, RAZZAGHI M, SRIVASTAVA D, et al. Structural basis for allosteric regulation of pyruvate kinase M2 by phosphorylation and acetylation[J]. Journal of Biological Chemistry, 2020,295(51):17425-17440. DOI:10.1074/jbc.RA120.015800.[14]杨晶旭. 丙酮酸激酶M2协同别构调节的分子机制研究[D]. 上海交通大学, 2016:1-5. DOI:10.27307/d.cnki.gsjtu.2016.002783.[15]YUAN M, MCNAE I W, CHEN Y, et al. An allostatic mechanism for M2 pyruvate kinase as an amino-acid sensor[J]. Biochemical Journal, 2018, 475(10): 1821-1837. DOI:10.1042/BCJ20180171. [16]SYBILLE MAZUREK. Pyruvate kinase type M2: A key regulator of the metabolic budget system in tumor cells[J]. The International Journal of Biochemistry & Cell Biology, 2011, 43(7): 969-980. DOI:10.1016/j.biocel.2010.02.005[17]CHRISTOFK H R, VANDER HEIDEN M G, WU N, et al. Pyruvate kinase M2 is a phosphotyrosine-binding protein[J]. Nature, 2008, 452(7184): 181-186. DOI:10.1038/nature06667. [18]CHANETON B, HILLMANN P, ZHENG L, et al. Serine is a natural ligand and allosteric activator of pyruvate kinase M2[J]. Nature, 2012, 491(7424): 458-462. DOI:10.1038/nature11540.[19]K-E KELLER, TAN I-S, LEE Y-S. SAICAR stimulates pyruvate kinase isoform M2 and promotes cancer cell survival in glucose-limited conditions[J]. Science, 2012, 338(6110): 1069-1072. DOI:10.1126/science.1224409.[20]HUANG C, HOU C, IJAZ M, et al. Proteomics discovery of protein biomarkers linked to meat quality traits in post-mortem muscles: Current trends and future prospects: A review[J]. Trends in Food Science & Technology, 2020, 105: 416-432. DOI:10.1016/j.tifs.2020.09.030.[21]WU W, GAO X G, DAI Y, et al. Post-mortem changes in sarcoplasmic proteome and its relationship to meat color traits in M. semitendinosus of Chinese Luxi yellow cattle[J]. Food Research International, 2015, 72: 98-105. DOI:10.1016/j.foodres.2015.03.030.[22]MALHEIROS J M, BRAGA C P, GROVE R A, et al. Influence of oxidative damage to proteins on meat tenderness using a proteomics approach[J]. Meat Science, 2019, 148: 64-71. DOI:10.1016/j.meatsci.2018.08.016.[23]HUANG C, BLECKER C, CHEN L, et al. Integrating identification and targeted proteomics to discover the potential indicators of postmortem lamb meat quality[J]. Meat Science, 2023, 199: 109126. DOI:10.1016/j.meatsci.2023.109126.[24]NOGUCHI T, INOUE H, TANAKA T. The M1-and M2-type isozymes of rat pyruvate kinase are produced from the same gene by alternative RNA splicing[J]. Journal of Biological Chemistry, 1986, 261(29): 13807-13812. DOI:10.1016/S0021-9258(18)67091-7.[25]LINYUAN SHEN, GAN MAILIN, CHEN LEI, et al. miR-152 targets pyruvate kinase to regulate the glycolytic activity of pig skeletal muscles and affects pork quality[J]. Meat Science, 2022, 185108707. DOI:10.1016/j.meatsci.2021.108707.[26]王正荣,赵圣明,李亚,等. 冰温对鸡胸肉成熟过程中品质的影响[J]. 食品工业科技, 2018, 39(24): 298-301. DOI:10.13386/j.issn1002-0306.2018.24.050.[27]朱立贤, 张一敏, 毛衍伟. 宰后不同温度处理对牛背最长肌AMPK活性, 糖酵解及肉品质的影响[J]. 食品与发酵工业, 2018, 44(2): 148. DOI:10.13995/j.cnki.11-1802/ts.014734.[28]CHEN X, CHEN S, YU D. Protein kinase function of pyruvate kinase M2 and cancer[J]. Cancer Cell International, 2020, 20(1). DOI:10.1186/s12935-020-01612-1.[29]RAJALA A, SONI K, RAJALA R V. Metabolic and non-metabolic roles of pyruvate kinase M2 isoform in diabetic retinopathy[J]. Scientific Reports, 2020, 10(1). DOI10.1038/s41598-020-64487-2.[30]YANG W, XIA Y, HAWKE D, et al. PKM2 phosphorylates histone H3 and promotes gene transcription and tumorigenesis[J]. Cell, 2012, 150(4): 685-696. DOI:10.1016/j.cell.2012.07.018.[31]CHENG T Y, YANG Y C, WANG H P, et al. Pyruvate kinase M2 promotes pancreatic ductal adenocarcinoma invasion and metastasis through phosphorylation and stabilization of PAK2 protein[J]. Oncogene, 2018, 37(13): 1730-1742. DOI:10.1038/s41388-017-0086-y.[32]WEI Y, WANG D, JIN F, et al. Pyruvate kinase type M2 promotes tumour cell exosome release via phosphorylating synaptosome-associated protein 23[J]. Nature communications, 2017, 8(1): 14041. DOI:10.1038/ncomms14041.[33]赵保平,杨金增. 猪肌肉组织中糖原酵解酶活性和PSE肉的相关性[J]. 华中农业大学学报, 1993, 5(12). DOI:10.13300/j.cnki.hnlkxb.1993.05.017.[34]SCHW?GELE F, HASCHKE C, HONIKEL K O, et al. Enzymological investigations on the causes for the PSE-syndrome, I. Comparative studies on pyruvate kinase from PSE-and normal pig muscles[J]. Meat Science, 1996, 44(1-2): 27-40. DOI:10.1016/S0309-1740(96)00046-0.[35]HITOSUGI T, KANG S, VANDER HEIDEN M G, et al. Tyrosine phosphorylation inhibits PKM2 to promote the Warburg effect and tumor growth[J]. Science signaling, 2009, 2(97): 73-73. DOI:10.1126/scisignal.2000431.[36]PARK Y S, KIM D J, KOO H, et al. AKT-induced PKM2 phosphorylation signals for IGF-1-stimulated cancer cell growth[J]. Oncotarget, 2016,7(30):48155-48167. DOI:10.18632/oncotarget.10179. [37]LV L, LI D, ZHAO D I, et al. Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth[J]. Molecular cell, 2011, 42(6): 719-730. DOI:10.1016/j.molcel.2011.04.025. [38]LV L, XU Y P, ZHAO D, et al. Mitogenic and oncogenic stimulation of K433 acetylation promotes PKM2 protein kinase activity and nuclear localization[J]. Molecular cell, 2013, 52(3): 340-352. DOI:10.1016/j.molcel.2013.09.004.[39]H-L ZHOU, ZHANG R, ANAND P, et al. Metabolic reprogramming by the S-nitroso-CoA reductase system protects against kidney injury[J]. Nature, 2019, 565(7737): 96-100. DOI:10.1038/s41586-018-0749-z.[40]LIU K, LI F, HAN H, et al. Parkin Regulates the Activity of Pyruvate Kinase M2[J]. Journal of Biological Chemistry, 2016,291(19):10307-10317. DOI:10.1074/jbc.M115.703066.[41]WANG Y, LIU J, JIN X, et al. O-GlcNAcylation destabilizes the active tetrameric PKM2 to promote the Warburg effect[J]. Proceedings of the National Academy of Sciences, 2017,114(52):13732-13737. DOI:10.1073/pnas.1704145115. [42]ABEYWARDANA T, OH M, JIANG L, et al. CARM1 suppresses de novo serine synthesis by promoting PKM2 activity[J]. Journal of Biological Chemistry, 2018,293(39):15290-15303. DOI:10.1074/jbc.RA118.004512.[43]CHEN L, LI Z, EVERAERT N, et al. Quantitative phosphoproteomic analysis of ovine muscle with different postmortem glycolytic rates[J]. Food Chemistry, 2019,280:203-209. DOI:10.1016/j.foodchem.2018.12.056.[44]LI Z, LI M, LI X, et al. Quantitative phosphoproteomic analysis among muscles of different color stability using tandem mass tag labeling[J]. Food chemistry, 2018, 249: 8-15. DOI:10.1016/j.foodchem.2017.12.047.[45]ALLISON C P, BATES R O, BOOREN A M, et al. Pork quality variation is not explained by glycolytic enzyme capacity[J]. Meat science, 2003, 63(1): 17-22. DOI:10.1016/S0309-1740(02)00046-3.[46]JIANG S, LIU Y, SHEN Z, et al. Acetylome profiling reveals extensive involvement of lysine acetylation in the conversion of muscle to meat[J]. Journal of Proteomics, 2019,205:103412. DOI:10.1016/j.jprot.2019.103412.[47]ZHOU B, SHEN Z, LIU Y, et al. Proteomic analysis reveals that lysine acetylation mediates the effect of antemortem stress on postmortem meat quality development[J]. Food chemistry, 2019, 293: 396-407. DOI:10.1016/j.foodchem.2019.04.122[48]REN C, LI X, BAI Y Q, et al. Phosphorylation and acetylation of glycolytic enzymes cooperatively regulate their activity and lamb meat quality[J]. Food Chemistry, 2022,397:133739. DOI:10.1016/j.foodchem.2022.133739.[49]ZHANG L, LIU R, CHENG Y, et al. Effects of protein S-nitrosylation on the glycogen metabolism in postmortem pork[J]. Food chemistry, 2019, 272: 613-618. DOI:10.1016/j.foodchem.2018.08.103.[50]WANG Y, LIU R, HOU Q, et al. Comparison of activity, expression and S-nitrosylation of glycolytic enzymes between pale, soft and exudative and red, firm and non-exudative pork during post-mortem aging[J]. Food chemistry, 2020, 314: 126203. DOI:10.1016/j.foodchem.2020.126203.[51]LI X, ZHANG D, REN C, et al. Effects of protein posttranslational modifications on meat quality: A review[J]. Comprehensive Reviews in Food Science and Food Safety, 2021, 20(1): 289-331. DOI:10.1111/1541-4337.12668.[52]张爽, 张楠, 朱良齐, 等. 宰后早期猪肉, 牛肉和鸡肉中能量代谢及蛋白质磷酸化[J]. 食品科学, 2017, 38(9): 72-78. DOI:10.7506/spkx1002-6630-201709012.[53]JIANG Y, WANG Y, WANG T, et al. PKM2 phosphorylates MLC2 and regulates cytokinesis of tumour cells[J]. Nature communications, 2014, 5(1): 5566.[54]JOHNSON T O, ERMOLIEFF J, JIROUSEK M R. Protein tyrosine phosphatase 1B inhibitors for diabetes[J]. Nature Reviews Drug Discovery, 2002, 1(9): 696-709. DOI:10.1038/nrd895.[55]XU Z Q, SHAO Y G, LIU G , et al. Proteomics analysis as an approach to understand the formation of pale, soft, and exudative (PSE) pork[J]. Meat Science, 2021,177:108353. DOI:10.1016/j.meatsci.2020.108353.[56]XU Z Q, SHAO Y G, XU H , et al. Transcriptome-based analysis of early post-mortem formation of pale, soft, and exudative (PSE) pork[J]. Meat Science, 2022,194:108962. DOI:10.1016/j.meatsci.2022.108962.[57]BAI Y Q, LI X, ZHANG D Q, et al. Role of phosphorylation on characteristics of glycogen phosphorylase in lamb with different glycolytic rates post-mortem[J]. Meat science, 2020, 164: 108096. DOI: 10.1016/j.meatsci.2020.108096.[58]PARK S H, OZDEN O, LIU G, et al. SIRT2-Mediated Deacetylation and Tetramerization of Pyruvate Kinase Directs Glycolysis and Tumor GrowthSIRT2 Directs PKM2 Activity[J]. Cancer research, 2016, 76(13): 3802-3812. DOI:10.1158/0008-5472.CAN-15-2498.[59]LV L, XU Y P, ZHAO D, et al. Mitogenic and oncogenic stimulation of K433 acetylation promotes PKM2 protein kinase activity and nuclear localization[J]. Molecular cell, 2013, 52(3): 340-352. DOI:10.1016/j.molcel.2013.09.004.[60]ZHANG R, SHEN M, WU C, et al. HDAC8-dependent deacetylation of PKM2 directs nuclear localization and glycolysis to promote proliferation in hepatocellular carcinoma[J]. Cell Death & Disease, 2020, 11(12): 1036. DOI:10.1038/s41419-020-03212-3.[61]LI Z W, LI X, WANG Z Y, et al. Antemortem stress regulates protein acetylation and glycolysis in postmortem muscle[J]. Food Chemistry, 2016, 20294-98. DOI:10.1016/j.foodchem.2016.01.085.[62]LI Q, LI Z, LOU A, et al. Histone acetyltransferase inhibitors antagonize AMP-activated protein kinase in postmortem glycolysis[J]. Asian-Australasian Journal of Animal Sciences, 2017, 30(6): 857. DOI:10.5713/ajas.16.0556.[63]田铸,师希雄,张攀高,等. 蛋白质乙酰化对宰后肉品质调控的研究进展[J]. 食品与发酵工业, 2021, 47(04): 269-274. DOI:10.13995 /j.cnki.11-1802 /ts.024877.[64]姜声旺. 蛋白质乙酰化修饰对宰后猪肉品质的调控机制[D]. 湖南农业大学, 2021. DOI:10.27136/d.cnki.ghunu.2021.000013.[65]郎玉苗,孙宝忠,马立新,等. 蛋白质巯基亚硝基化及其对宰后成熟肉品质影响的研究进展[J]. 食品工业科技, 2018, 39(08): 330-334. DOI:10.13386 /j.issn1002-0306.2018.08.059.[66]LU W, HOU Q, ZHANG J, et al. Targeted energy metabolomics analysis of postmortem pork in an in vitro model as influenced by protein S-nitrosylation[J]. Meat Science, 2023,197:109073. DOI:10.1016/j.meatsci.2022.109073.[67]LIU R, YANG L, YANG T, et al. Effect of nitric oxide treatment on pork meat quality, microstructure, and total bacterial count during postmortem aging[J]. Meat Science, 2022, 190: 108806. DOI:10.1016/j.meatsci.2022.108806.[68]刘瑞,周光宏,张万刚. 一氧化氮和蛋白质亚硝基化对鲜肉品质的影响研究进展[J]. 中国畜牧杂志, 2017, 53(04): 1-2. DOI:10.19556/j.0258-7033.2017-04-001. |
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