Changes in protein abundance between tender and tough meat from bovine Longissimus thoracis muscle assessed by isobaric Tag for Relative and Absolute Quantitation (iTRAQ) and 2-dimensional gel electrophoresis analysis
Changes in protein abundance between tender and tough meat from bovine Longissimus thoracis muscle assessed by isobaric Tag for Relative and Absolute Quantitation (iTRAQ) and 2-dimensional gel electrophoresis analysis
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DOI：
10.2527/jas.2011-4721
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发表时间：
2012-06-01
影响因子：
3.3
通讯作者：
Veiseth-Kent, E.
中科院分区：
文献类型：
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作者：
Bjarnadottir, S. G.;Hollung, K.;Veiseth-Kent, E.
本研究的目的是寻找牛胸最长肌嫩度的潜在生物标志物，并比较等压标记相对和绝对定量(ITRAQ)和双向凝胶电泳法(2-DE)的结果。实验包括4个嫩样和4个硬样，基于7d的剪切力测量，取自年轻的挪威红(NRF)公牛，于死后1h采集。在iTRAQ(P<；0.1)和2-DE分析(P<；0.05)中，许多以前与嫩度有关的蛋白质在软质和坚韧样品之间的丰度都发生了变化。此外，在本研究中，发现3种以前与嫩度无关的蛋白质在嫩肉和硬肉样品中的丰度发生了显著变化。这些蛋白质包括通过三羧酸循环控制流量的相关蛋白质[2-氧代戊二酸脱氢酶复合体E2(OGDC-E2)]，细胞凋亡(Galectin-1)和调节细胞内钙释放的作用(Annexin A6)。尽管iTRAQ和2-DE分析中显著变化的蛋白质的重叠率相对较低，但在两种分析中都发现了某些被预测具有相同功能的蛋白质，并在两组之间显示了相似的变化，例如结构蛋白质和与细胞凋亡和能量代谢相关的蛋白质。
The aim of this study was to find potential biomarkers for meat tenderness in bovine Longissimus thoracis muscle and to compare results from isobaric Tag for Relative and Absolute Quantitation (iTRAQ) and 2-dimensional gel electrophoresis (2-DE) analysis. The experiment included 4 tender and 4 tough samples, based on shear force measurements at 7 d postmortem, from young Norwegian red (NRF) bulls, taken at 1 h postmortem. A number of the proteins which have previously been related to tenderness were found to change in abundance between tender and tough samples, both in iTRAQ (P < 0.1) and 2-DE analysis (P < 0.05). Furthermore, 3 proteins that have not previously been related to tenderness were found to change significantly in abundance between tender and tough meat samples in the present study. These include proteins related to control of flux through the tricarboxylate cycle [2-oxoglutarate dehydrogenase complex component E2 (OGDC-E2)], apoptosis (galectin-1) and regulatory role in the release of Ca2+ from intracellular stores (annexin A6). Even though the overlap in significantly changing proteins was relatively low between iTRAQ and 2-DE analysis, certain proteins predicted to have the same function were found in both analyses and showed similar changes between the groups, such as structural proteins and proteins related to apoptosis and energy metabolism.