| 蛋白质磷酸化调控羊肉肌原纤维蛋白的功能 |
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| 引用本文： | 陈立娟,李 欣,李 铮,李培迪,李仲文,张德权.蛋白质磷酸化调控羊肉肌原纤维蛋白的功能[J].中国农业科学,2016,49(7):1360-1370. |
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| 作者姓名： | 陈立娟 李 欣 李 铮 李培迪 李仲文 张德权 |
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| 作者单位： | 中国农业科学院农产品加工研究所/农业部农产品加工综合性重点实验室，北京 100193 |
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| 基金项目： | 国家自然科学基金（31471604）、国家现代肉羊产业技术体系（CARS-39）、国家公益性行业（农业）科研专项（201303083） |
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| 摘 要： | 【目的】通过激活蛋白激酶的活性提高羊肉肌原纤维蛋白的磷酸化水平，分析磷酸化水平的提高对羊肉肌原纤维蛋白降解程度、收缩功能的影响，进一步揭示蛋白质磷酸化对羊肉肌肉嫩化的作用机理。【方法】通过添加蛋白激酶A激活剂Forskolin、蛋白激酶C激活剂佛波酯（PMA），提高蛋白激酶的活性，改变羊肉肌原纤维蛋白的磷酸化水平。比较激活剂处理组与空白对照组肌原纤维小片化指数（MFI）、条带降解程度、肌节长度等指标的差异，确定蛋白质磷酸化水平对羊肉肌肉收缩和肌肉降解的影响。【结果】将羊肉样品在蛋白激酶溶液中培养24 h，在培养结束后1、2和4 h，PMA处理组（PKC激活组）的蛋白激酶活性显著高于空白对照组（P＜0.05），而在培养后1和4 h，Forskolin处理组（PKA激活组）的蛋白激酶活性显著高于空白对照组（P＜0.05）。PMA处理组和Forskolin处理组的最高蛋白激酶活性出现在培养后1 h。Forskolin和PMA通过提高激酶活性显著提高肌联蛋白（Titin）、肌球蛋白结合蛋白C（Myosin binding protein C）、原肌球蛋白（Tropomyosin）、肌球蛋白轻链2（Myosin light chain 2）等蛋白质的磷酸化水平，肌球蛋白重链、肌动蛋白质的磷酸化水平没有显著变化，Forskolin组和PMA组的蛋白质降解程度及肌节长度均低于对照组。【结论】肌原纤维蛋白磷酸化水平提高不利于羊肉肌原纤维蛋白的降解。另一方面，磷酸化水平可能通过对肌球蛋白轻链2的作用增强羊肉肌肉的收缩作用力，通过促进相邻原肌球蛋白的相互作用促进肌细丝收缩，影响肉的僵直进程和嫩化进程。
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| 关 键 词： | 羊肉 蛋白质磷酸化 肌原纤维蛋白 肌肉收缩 蛋白质降解 |
| 收稿时间： | 2015-08-07 |
Protein Phosphorylation on the Function of Myofibrillar Proteins in Mutton Muscle |
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| CHEN Li-juan,LI Xin,LI Zheng,LI Pei-di,LI Zhong-wen,ZHANG De-quan.Protein Phosphorylation on the Function of Myofibrillar Proteins in Mutton Muscle[J].Scientia Agricultura Sinica,2016,49(7):1360-1370. |
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| Authors: | CHEN Li-juan LI Xin LI Zheng LI Pei-di LI Zhong-wen ZHANG De-quan |
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| Institution: | Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing 100193 |
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| Abstract: | 【Objective】The aim of this study was to analyze the effect of the phosphorylation level which was improved by activating the activity of protein kinase on myofibrillar proteins’ degradation and contraction.【Method】Improve the activity of protein kinases by adding protein kinase A activator Forskolin and protein kinase C activator PMA, followed by the increasing of the phosphorylation level of myofirillar proteins in mutton muscle. By comparing the myofibrillar fragmentation index (MFI), the degree of myofibrillar degradation, the sarcomere length, and other indicators between activator groups and control group to determine the effect of protein phosphorylation levels on lamb muscle contraction and degradation. 【Result】The activity of protein kinases in the PMA group (PKC activated group) were higher than the control group after 1 hour, 2 hour, and 4 hour incubation (P＜0.05). The activity of protein kinases in the Forskolin group (PKA activated group) were higher than in the control group after 1 hour and 4 hour incubation (P＜0.05). The highest activity of the protein kinases appeared after 1 hour incubation. PMA and Forskolin can improve the phosphorylation level of titin, myosin binding protein C, tropomyosin, myosin light chain 2, and a protein of 25 kDa by activating the protein kinases, but the phosphorylation level of myosin heavy chain and actin had no changes. The degradation degree of the PMA group and the Forskolin group were lower than the control group, and the sarcomere length of the PMA group and the Forskolin group was shorter than the control group. 【Conclusion】 On the one hand, the improvement of the myofirillar proteins phosphorylation level can reduce the degree of myofibrillar degradation, while on the other hand, the improvement of the myofirillar proteins phosphorylation level may enhance the force of muscle contraction through the effect on myosin light chain 2, may accelerate the contraction of filament through the effect on adjacent tropomyosin, and finally influence the rigor mortis and tenderization. |
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| Keywords: | mutton protein phosphorylation myofibrillar proteins muscle contraction protein degradation
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