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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
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Malheiros, J. M. [1] ; Enriquez-Valencia, C. E. [2] ; Braga, C. P. [3] ; Vieira, J. C. S. [4] ; Vieira, D. S. [5] ; Pereira, G. L. [6] ; Curi, R. A. [6] ; Machado Neto, O. R. [6] ; Oliveira, H. N. [6] ; Padilha, P. M. [4] ; Chardulo, L. A. L. [6]
Total Authors: 11
Affiliation:
[1] Sao Paulo State Univ UNESP, Coll Agr & Vet Sci FCAV, Sao Paulo - Brazil
[2] Univ Ciencias Aplicadas & Ambientales UDCA, Bogota - Colombia
[3] Univ Nebraska, Redox Biol Ctr, Dept Biochem, Lincoln, NE - USA
[4] Sao Paulo State Univ UNESP, Inst Biosci IB, Botucatu, SP - Brazil
[5] Sao Paulo State Univ UNESP, Sch Vet Med, Sao Paulo - Brazil
[6] Sao Paulo State Univ UNESP, Sch Vet Med & Anim Sci FMVZ, Botucatu, SP - Brazil
Total Affiliations: 6
Document type: Journal article
Source: JOURNAL OF PROTEOMICS; v. 248, SEP 30 2021.
Web of Science Citations: 0
Abstract

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. (AU)

FAPESP's process: 15/13021-1 - An metalloproteomics and expression approach of the structural, proteolytic and tissue skeletal muscle regulatory proteins in post-mortem and the relationship with growth and meat tenderness in Nellore animals (Bos indicus).
Grantee:Luis Artur Loyola Chardulo
Support type: Regular Research Grants