Application of proteomic to investigate the different degrees of meat tenderness in Nellore breed.

This study describes the association between meat tenderness and abundance of soluble muscle proteins in Nellore bulls (Bos indicus) using a proteomic approach. We evaluated shear force (SF) of Longissimus thoracis muscle 24 h after slaughter and selected three experimental groups of animals with moderately tender (TE; SF = 3.9 ± 0.7 kg), moderately tough (TO; SF = 5.6 ± 0.7 kg) and very tough meat (TO+; SF = 7.9 ± 1.4 kg). Proteome was investigated by two-dimensional electrophoresis (2D-PAGE) in combination with electrospray ionization-tandem mass spectrometry (ESI-MS/MS). The metabolic proteins triosephosphate isomerase (TPI1) and phosphoglucomutase 1 (PGM1), the structural protein profilin 1 (PFN1), and cytosol aminopeptidase (LAP3) were up-regulated (P < 0.05) in the TE meat group when compared to the TO and TO+ groups. Actin structural proteins (ACTA1, ACTB, and ACTG1), the oxidative stress protein peroxiredoxin (PRDX6, PRDX2, PRDX1, and PARK7), heat shock protein isoforms, and co-chaperones (CDC37 and STIP1) were up-regulated (P < 0.05) in the TO and TO+ meat groups. In addition, we also identified proteins PFN1, LAP3, PRDX1, PRDX2, HSPD1, and ARHGDIA to be associated with beef tenderness. The results reported herein demonstrated that meat tenderness in Nellore cattle depends on the modulation and expression of a set of proteins involved in different biological pathways. SIGNIFICANCE: The manuscript entitled "Application of proteomic to investigate the different degrees of meat tenderness in Nellore breed" describes a classical proteomics work using two-dimensional gel electrophoresis (2D-PAGE), followed by mass spectrometry coupled to electrospray ionization ion trap (ESI-MS/MS) in order to understand the biochemical engineering involved in the process of meat tenderness. We evaluated shear force (SF) of Longissimus thoracis muscle samples of Nellore cattle (n = 90) and select three experimental groups of animals with moderately tender (TE; SF = 3.9 ± 0.7), moderately tough (TO; SF = 5.6 ± 0.7) and very tough meat (TO+; SF = 7.9 ± 1.4). The proteomic approach allowed observing that meat tenderness is influenced by structural proteins (ACTA1, ACTG1, ACTB, MYL1 and PFN1), co-chaperones (CDC37 and STIP1), heat shock proteins (HSP90AA1, HSP90AB1, HSPD1, HSPA1L, HSPA1A and HSPB1), regulatory protein (ARHGDIA), metabolic proteins (TPI1 and PGM1) and oxidative stress proteins (PRDX1, PRDX2, PRDX6, PARK7). Our results suggest that meat tenderness in Nellore depends on the modulation and expression of a set of proteins involved in different biological pathways.

Proteomic investigation of liver from beef cattle (Bos indicus) divergently ranked on residual feed intake.

Proteomics studies can be used to identify proteins that affect feed efficiency traits, related to cost and profitability of meat production. We used a proteomic approach based on two-dimensional electrophoresis (2D-PAGE) in combination with mass spectrometry (ESI-MS) to study liver samples of Nellore bulls divergently ranked according to residual feed intake (RFI). The study showed that 71 protein spots were expressed differentially (P < 0.05) among RFI groups and 47 were identified by ESI-MS. In RFI, efficient animals (low RFI) eat less than predictions, based on their weights and growth rate, while inefficient animals (high RFI) that eat more than predicted. Data from 18 animals (9 high vs. 9 low RFI) aged 24-26 months in feedlot finishing were used. Immediately after slaughter, liver samples were collected and protein extracts were separated. The gels of RFI groups were scanned and the images analyzed, whereby we found 279 and 215 liver protein spots in high and low RFI bulls, respectively. The proteins identified were related to the following biological functions: (I) oxygen transport and blood flow; (II) mitochondrial function and energy metabolism; (III) amino acid metabolism, ion transport, and cell survival. The study suggests hemoglobin subunit beta and heat shock protein 71 kDa and as molecular markers to study FE in Nellore cattle. Moreover, proteins such as 3-ketoacyl-CoA thiolase and glutamate dehydrogenase 1 were found in liver from high and low RFI animals, respectively. Such protein expression could be associated with changes in the oxidative capacity of RFI phenotypes.