# Muscle Hypertrophy Is Linked to Changes in the Oxidative and Proteolytic Systems during Early Tenderization of the Spanish Breed “Asturiana de los Valles”

**Authors:** Marina García-Macia, Verónica Sierra, Adrián Santos-Ledo, Beatriz de Luxán-Delgado, Yaiza Potes-Ochoa, Susana Rodríguez-González, Mamen Oliván, Ana Coto-Montes

PMC · DOI: 10.3390/foods13030443 · Foods · 2024-01-30

## TL;DR

This study shows how muscle hypertrophy in a Spanish cattle breed affects meat tenderness through changes in oxidative and proteolytic systems after slaughter.

## Contribution

The study reveals distinct oxidative and proteolytic patterns in different myostatin-mutant biotypes that influence early meat tenderization.

## Key findings

- mh/mh biotype showed higher antioxidant activity and sarcomere shortening, linked to tenderness.
- Proteasome activity was higher in mh/+ biotype, correlating with increased protein damage.
- Lysosome proteolysis and autophagy varied between biotypes, affecting myofiber disintegration.

## Abstract

For fresh meat consumers, eating satisfaction is of utmost importance and tenderness is one of the most important characteristics in this regard. Our study examined beef of different animal biotypes of the autochthonous breed “Asturiana de los Valles” (AV) to determine if early postmortem oxidative and proteolytic processes may influence the final tenderness of the product. This meat-specialized breed shows different biotypes depending on the frequency of a myostatin mutation “mh” that induces double-muscling or muscular hypertrophy (mh/mh, mh/+, +/+). Samples from the longissimus dorsi muscles of yearling bulls were analyzed during the first 24 h postmortem. Changes in the redox balance of muscle cells were significant in the first hours after slaughter; total antioxidant activity was higher in the mh/mh biotype and it followed the shortening of the sarcomeres, a key parameter in understanding meat tenderness. The two proteolytic systems studied (proteasome and lysosome) followed distinct patterns. Proteasome activity was higher in the (mh/+) biotype, which correlated with higher protein damage. Lysosome proteolysis was increased in the more tender biotypes (mh genotypes). Autophagic activation showed significant differences between the biotypes, with (mh/mh) showing more intense basal autophagy at the beginning of the postmortem period that decreased gradually (p < 0.001), while in the normal biotype (+/+), it was slightly delayed and then increased progressively (p < 0.001). These results suggest that this type of catalytic process and antioxidant activity could contribute to the earlier disintegration of the myofibers, particularly in the mh/mh biotypes, and influence the conversion of muscle into meat.

## Linked entities

- **Genes:** LOC5521725 (growth/differentiation factor 8) [NCBI Gene 5521725]

## Full-text entities

- **Genes:** MSTN (myostatin) [NCBI Gene 2660] {aka GDF8, MSLHP}
- **Diseases:** double-muscling (MESH:D005671), tenderness (MESH:D063806), muscular hypertrophy (MESH:D006984), Muscle Hypertrophy (MESH:C536106)

## Full text

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## Figures

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## References

41 references — full list in the complete paper: https://tomesphere.com/paper/PMC10855751/full.md

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Source: https://tomesphere.com/paper/PMC10855751