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 analysis1

Abstract

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 Ca(2+) 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.

Skeletal muscle proteome and meat quality of broiler chickens subjected to gas stunning prior slaughter or slaughtered without stunning

“…The finding coincides with the lower pH and higher Note: a, b means within a row with different superscripts are significantly different at P < 0.05 Nota: a, b los promedios en una misma fila con diferente superíndice son significativamente distintos a P < 0,05 tenderness in gas-stunned birds compared with their Halal counterparts. In line with the current finding, increased expression of creatine kinase has been associated with increased meat tenderness in cows (Bjarnadóttir et al, 2012;Zapata, Zerby, & Wick, 2009). Gas stunning up-regulated (P < 0.05) pyruvate kinase isozyme.…”

In-depth characterisation of the lamb meat proteome from longissimus lumborum

“…For example, the study on porcine LTL exudate proteome [28] identified several enzymes involved in energy metabolism (e.g., phosphoglycerate kinase 1, alphaenolase and malate dehydrogenase, cytoplasmic) whose ovine analogues were also detected in the sarcoplasmic fraction of our study. Also, while both our and the bovine study [82] identified the abundant skeletal muscle proteins such as myosin-1 (myosin heavy chain 1), troponin T, fast skeletal muscle and glucose-6-phosphate isomerase, some proteins were detected only in the bovine study, e.g., cysteine and glycine-rich protein 3.…”

“…Currently, most of them are differential studies aiming to identify only the proteins that exhibit differential abundance, to the best of our knowledge. A few studies focusing on LTL did involve identification of the proteome in their samples, including one for bovine [82] and three for porcine [28,83,84]. They are briefly summarised in Table 1.…”

Ractopamine-induced changes in sarcoplasmic proteome profile of post-rigor pork <i>semimembranosus</i> muscle

“…A positive correlation between MLC 1 and shear force has been observed in pork longissimus (Hwang et al, 2005). Furthermore, in beef longissimus thoracis, MLC 1 was of greater abundance in tough meat than in tender meat (Bjarnadottir et al, 2012).…”