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Meat tenderness and muscle growth: is there any relationship?

TLDR
In this paper, the authors review the mechanisms of muscle growth, the biological basis of meat tenderness, and the relationship between these two processes and conclude that the calpain proteolytic system is a major regulator of muscle protein degradation.
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This article is published in Meat Science.The article was published on 2002-11-01 and is currently open access. It has received 393 citations till now. The article focuses on the topics: Meat tenderness & Tenderness.

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Citations
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Journal ArticleDOI

Some biochemical aspects pertaining to beef eating quality and consumer health: A review

TL;DR: In this paper, the authors highlight biochemical processes and products, from slaughter to the time of beef consumption, that relate to response to stress at slaughter, meat quality and consumer health.
Journal ArticleDOI

A second look into fibre typing--relation to meat quality.

TL;DR: This review describes the involvements of Ca2+-dependent mechanisms, and the energy state of the myofibres in the control of contractile and metabolic properties, and proposes some genetic and environmental factors as possible tools to control meat quality trough the modulation of fibre type characteristics.
Journal ArticleDOI

Genetic and environmental effects on meat quality

TL;DR: The day-to-day variation in tenderness is evident across experiments and this variation needs to be controlled in order to consistently produce tender meat.
Journal ArticleDOI

μ-Calpain is essential for postmortem proteolysis of muscle proteins,

TL;DR: The results of the current study show that even in a species in which m-Calpain is activated to some extent postmortem, micro-calpain is largely responsible for postmortem proteolysis, which excludes a major role for any of the other members of the calpain family or any other proteolytic system in postmortemroteolysis of muscle proteins.
Journal ArticleDOI

Feeding and meat quality - a future approach.

TL;DR: The traditional way of using feeding as a quality control tool in the production of meat is re-thinked and the potential of a nutrigenomic approach is introduced as a first step in the development of pro-active quality control systems which fulfil future demands from industry and consumers.
References
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Journal ArticleDOI

Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member.

TL;DR: Results suggest that GDF-8 functions specifically as a negative regulator of skeletal muscle growth, which is significantly larger than wild-type animals and show a large and widespread increase in skeletal muscle mass.
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Double muscling in cattle due to mutations in the myostatin gene

TL;DR: The similarity in phenotypes of double-muscled cattle and myostatin null mice suggests that mystatin performs the same biological function in these two species and is a potentially useful target for genetic manipulation in other farm animals.
Journal ArticleDOI

A deletion in the bovine myostatin gene causes the double-muscled phenotype in cattle.

TL;DR: It is demonstrated that a mutation in bovine MSTN, which encodes myostatin, a member of the TGFβ superfamily, is responsible for the double-muscled phenotype, and an 11-bp deletion in the coding sequence for the bioactive carboxy-termihal domain of the protein causing the muscular hypertrophy observed in Belgian Blue cattle is reported.
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Mutations in myostatin (GDF8) in Double-Muscled Belgian Blue and Piedmontese Cattle

TL;DR: It appears likely that the mh allele in these breeds involves mutation within theMyostatin gene and that myostatin is a negative regulator of muscle growth in cattle as well as mice.
Related Papers (5)
Frequently Asked Questions (13)
Q1. What are the contributions in "Meat tenderness and muscle growth: is there any relationship?§" ?

Their objectives for this manuscript are to review the mechanisms of muscle growth, the biological basis of meat tenderness, and the relationship between these two processes. Current evidence suggests that the calpain proteolytic system is a major regulator of muscle protein degradation. 

The hypothesis is that in living muscle, elevation of calpastatin suppresses m-calpain (and perhaps m-calpain), which in turn reduces the rate of protein degradation resulting in an increase in muscle growth. 

If muscle hypertrophy were caused by reduced protein degradation, the authors would expect increased meat toughness to occur only in hypertrophied muscles whose tenderness is affected by changes in postmortem proteolysis (e.g., longissimus). 

suppression of protein degradation seems to be the mechanism that is responsible for differences in the rates of muscle growth in domestic animals (Bohorov, Buttery, Correia, & Soar, 1987; Koohmaraie, Killefer, et al., 1995; Maruyama, Sunde, & Swick, 1978; Reeds, Hay, Dorwood, & Palmer, 1986). 

The mutation in calpain 3 that results in limb girdle muscular dystrophy causes loss of catalytic activity of calpain 3 (Ono et al.,1998). 

3. Decreased protein synthesis and decreased protein degradation, providing decrease in protein degradation is greater than the decrease in synthesis (most efficient method to increase muscle growth rate). 

The best evidence to support the above proposal is the observation that incubation of isolated myofibrils from several rat muscles in a relaxing solution released a small amount of myofilaments that constituted less than 5% of the total myofibrillar proteins (Etlinger, Zad, Fischman, & Rabinowitz, 1975). 

If the objective is to increase muscle mass without any regard for meat tenderness (for the production of ground beef or tenderness enhanced products), one can select for animals with high calpastatinactivity. 

The Goll et al. (1992) proposal stated that the proteasome complex is a good candidate to degrade the released myofilaments into amino acids. 

Of all the possible mechanisms of increasing muscle deposition, only the mechanism that involves suppression of protein degradation will result in decreased meat tenderness. 

The importance discussed earlier of recognizing that the relative contribution of sarcomere length, postmortem proteolysis, and collagen concentration to ultimate meat tenderness is muscle dependent is supported by the callipyge model. 

The objectives of this manuscript are to review the mechanisms of muscle growth, the biochemical basis for meat tenderness, and the relationship between these two important processes. 

In this example, three of 11 sheep are very tender at 24 h, two acceptable and six tough, so for five of 11 animals extensive tenderization has occurred in the first 24 h.