Beef tenderness and intramuscular fat proteomic biomarkers: muscle type effect

Abstract

Tenderness and intramuscular fat content are key attributes for beef sensory qualities. Recently some proteomic analysis revealed several proteins which are considered as good biomarkers of these quality traits. This study focuses on the analysis of 20 of these proteins representative of several biological functions: muscle structure and ultrastructure, muscle energetic metabolism, cellular stress and apoptosis. The relative abundance of the proteins was measured by Reverse Phase Protein Array (RPPA) in five muscles known to have different tenderness and intramuscular lipid contents: Longissimus thoracis (LT), Semimembranosus (SM), Rectus abdominis (RA), Triceps brachii (TB) and Semitendinosus (ST). The main results showed a muscle type effect on 16 among the 20 analyzed proteins. They revealed differences in protein abundance depending on the contractile and metabolic properties of the muscles. The RA muscle was the most different by 11 proteins differentially abundant comparatively to the four other muscles. Among these 11 proteins, six were less abundant namely enolase 3 (ENO3), phosphoglucomutase 1 (PGK1), aldolase (ALDOA), myosin heavy chain IIX (MyHC-IIX), fast myosin light chain 1 (MLC1F), triosephosphate isomerase 1 (TPI1) and five more abundant: Heat shock protein (HSP27, HSP70-1A1, αB-crystallin (CRYAB), troponin T slow (TNNT1), and aldolase dehydrogenase 1 (ALDH1A1). Four proteins: HSP40, four and a half LIM domains protein 1 (FHL1), glycogen phosphorylase B (PYGB) and malate dehydrogenase (MDH1) showed the same abundance whatever the muscle. The correlations observed between the 20 proteins in all the five muscles were used to construct a correlation network. The proteins the most connected with the others were in the following order MyHC-IIX, CRYAB, TPI1, PGK1, ALDH1A1, HSP27 and TNNT1. This knowledge is important for understanding the biological functions related to beef tenderness and intramuscular fat content.

Assessment of muscle Longissimus thoracis et lumborum marbling by image analysis and relationships between meat quality parameters

“…Finally, in our study marbling percentage (Image J), USDA score, and chemical IMF were negatively ( P < 0.05) correlated with WBSF of cooked meat (Image J: r = −0.29; USDA: r = −0.26; IMF: r = −0.29). Although these variables were poorly correlated, their negative relationship is already known, as well as the consequent positive correlation between meat tenderness and fat content [ 28 , 29 ]…”

Reverse Phase Protein array for the quantification and validation of protein biomarkers of beef qualities: The case of meat color from Charolais breed

“…5) and high levels of ALDH1A1, MHC1, Hsp20 and SOD1 ( Fig. 4d) (Picard et al, 2018). In the same manner, Tripartite motif-containing 72 (TRIM72), which is exclusively expressed in skeletal muscle, might act as a sensor of oxidation on membrane damage (Cai et al, 2009), thereby influencing meat color aspects.…”

“…The relative abundances of a list of 29 protein biomarkers candidates previously used to predict beef tenderness, pH and/or color traits (Gagaoua, Bonnet, Ellies-Oury, et al, 2018;Joseph et al, 2012;Picard et al, 2018;Wu et al, 2015;Wu et al, 2016) were quantified using specific antibodies. All antibodies had been previously validated for their specificity by western-blot (Fig.…”

Review: Enhancing intramuscular fat development via targeting fibro-adipogenic progenitor cells in meat animals

“…The content of IMF varies among different muscles in the same animal (Sharma et al, 1987;Font-i-Furnols et al, 2019, likely due to the difference in muscle fiber composition and locomotion (Picard et al, 2018). The content of IMF is higher in the belly and lower in the ham (Kouba and Bonneau, 2009).…”