Early post mortem expression of genes related to tenderization in two Italian Simmental young bulls' skeletal muscles differing in contractile type

Abstract

The early post mortem expression of eight genes potentially involved in meat ageing process and the tenderness of two Italian Simmental young bulls' (Bos taurus) skeletal muscles differing in their contractile type were evaluated. Samples of Longissimus lumborum (LL) and Infraspinatus (IS) muscles were collected from 17 bulls. The messenger RNA (mRNA) abundances of calpain-1, calpain-2, calpastatin, caspase 3, caspase 9, heat shock protein 27 (Hsp27), Hsp40 and Hsp70 were detected by quantitative PCR. The myosin heavy chain-slow and -fast isoform content, the pH48h and the lipid content of the muscles were in line with the contractile and metabolic type. In comparison with the fast LL, the slow IS showed a lower calpain-1/calpastatin mRNA content ratio after slaughtering and a higher Warner-Bratzler Initial Yield value after 7 days of ageing. Hsp27 and Hsp70 mRNA abundances were significantly lower in LL than IS, highlighting their potential role in the ageing process of bovine muscles.

El sistema proteolítico calpaina en la tenderización de la carne: Un enfoque molecular.

“…Calpastatin gene expression has an average of nearly 30% in high WBSF groups compared with low WBSF at 6 days postmortem (42). Moreover, calpain-1 mRNA abundance was slightly higher and calpastatin mRNA was lower in longissimus lumborum than infraspinatus (41), suggesting that the higher proportion of glycolytic fibers could improve the tenderness of certain muscles by accelerating post mortem aging due to the presence of a higher calpain/calpastatin ratio (43). Other researcher reveal that the slightly lower tenderness of meat from Zebu animals is probably not a result of lower expression of genes encoding proteases, but rather is due to the increased expression of CAST (44).…”

“…Algunos autores sugieren que el tipo de músculo y/o el tipo de fibra pueden influir en la expresión y/o actividades de la calpaína y la calpastatina y por lo tanto podrían explicar la proteólisis post mortem y la tenderización de la carne (39)(40)(41). Se encontraron diferencias en la subunidad pequeña (CAPNS1) y variantes en la expresión de CAST en los músculos con fibras de tipo lento en comparación con los músculos con fibras de tipo rápido (40).…”

“…Some authors suggest that muscle type and/or fiber type can influence calpain and calpastatin expression and/or activities and therefore could account for post mortem proteolysis and meat tenderization (39)(40)(41). Differences in the small subunit (CAPNS1) and variants in CAST expression were found in slow-type muscles compared to fast-type muscles (40).…”

Comparison of longissimus thoracis physical quality traits and the expression of tenderness-related genes between Goudali zebu breed and Italian Simmental × Goudali crossbreed

“…Becila et al (2010) provided evidences that cell death in post-mortem muscle occurs via an apoptotic process, in which caspase 3 and caspase 9 operate. Although caspases are the main effectors of apoptosis, their importance in meat tenderisation process is still debated (Sacc a et al 2015a). For their physiological role as chaperones, anti-apoptotic and anti-oxidative factors, heat shock proteins are involved in the transformation of muscle to meat (Cassar-Malek and Picard 2016).…”

“…For their physiological role as chaperones, anti-apoptotic and anti-oxidative factors, heat shock proteins are involved in the transformation of muscle to meat (Cassar-Malek and Picard 2016). Among these, alphaB-cristallyn and heat shock protein 27 (Hsp27) have been shown to be involved in myofibrillar proteins protection (Guillemin et al 2011;Lomiwes et al 2014) and Hsp27 was reported as related to tenderness (Bernard et al 2007;Sacc a et al 2015a). Besides having a significant role in cell thermotolerance, Hsp70 has been shown to inhibit the apoptotic pathways and appears to be a good biomarker of low tenderness (Kregel 2002;Picard et al 2014).…”