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      Post-mortem changes in chicken muscle

      World's Poultry Science Journal
      CABI Publishing

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          Abstract

          This paper details the post-mortem changes that take place in the muscular tissue of poultry and the consequences of these on the resulting meat quality at the point of consumption. The history of the development if the modern meat type chicken, the form and function of its muscles, the factors that determine muscle growth and their effects on meat quality are all described. Past studies tend to have been concentrated on the processes occuring in mammalian tissue and those mainly on beef, with little attention being directed at the changes taking place in poultry muscle. In this context the view that modern broilers grow “at the edge of what is metabolically possible” is important. This hypothesis owes its origin to the fact that muscle, and thus protein, accretion is accomplished through a dynamic equilibrium between synthesis and degradation. Evidence is provided to show that the muscle cell reaches a certain maximum synthesis capacity, to grow beyond which requires it to decrease its rate of degradation. This property is possibly of considerable influence in meat ageing and forms the basis for the proposition that the breast muscle of poultry is especially suited to study the effects of post-mortem proteolytic degradation on meat ageing and product quality.

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          Most cited references117

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          Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation.

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            Type beta transforming growth factor is an inhibitor of myogenic differentiation.

            We have investigated the effect of type beta transforming growth factor (TGF-beta) on the differentiation of skeletal muscle myoblasts. TGF-beta potently (ID50 approximately 10 pM) prevents established cell lines and primary cultures of rat and chicken embryo myoblasts from fusing into multinucleated myotubes. Inhibition of morphological differentiation by TGF-beta correlates with inhibition of the expression of muscle-specific mRNAs and proteins, strong induction of extracellular matrix type I collagen and fibronectin, and a marked tendency of the treated myoblasts to aggregate into densely multilayered arrays or clusters. Myogenic differentiation can resume after removal of TGF-beta from the medium. Examination of the time of action of TGF-beta shows that myoblasts stochastically reach a point beyond which they become insensitive to the inhibitory action of TGF-beta. This resistance of committed myoblasts to the inhibitory action of TGF-beta is not associated with any measurable change in the number or affinity of TGF-beta receptors in those cells. The results indicate that TGF-beta is a potent inhibitor of myogenesis and may regulate muscle development in vivo.
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              Titin: major myofibrillar components of striated muscle.

              Electrophoretic analyses of protein components of striated muscle myofibril purified from various vertebrate and invertebrate species revealed that proteins much larger than myosin heavy chain are present in significant amounts. To define possible roles of these heretofore unidentified proteins, we purified a combination of two uncommonly large proteins, designated as titin, from chicken breast myofibrils. Chemical and immunological studies indicated that titin is distinct from myosin, actin, and filamin. Specific titin anti body crossreacts with similar protein in both skeletal and cardiac myofibrils of many vertebrate and invertebrate species. Immunofluorescent staining of glycerinated chicken breast myofibrils indicated that titin is present in M lines, Z lines, the junctions of A and I bands, and perhaps throughout the entire A bands. Similar staining studies of myofibrils from other species suggest that titinlike proteins may be organized in all myofibrils according to a common architectural plan. We conclude that titin is a structurally conserved myofibrillar component of vertebrate and invertebrate striated muscles.
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                Author and article information

                Journal
                World's Poultry Science Journal
                Worlds Poult. Sci. J.
                CABI Publishing
                0043-9339
                1743-4777
                December 2000
                September 18 2007
                December 2000
                : 56
                : 4
                : 319-346
                Article
                10.1079/WPS20000023
                1d2b154b-cae4-4ddf-aef4-53de8cbf699a
                © 2000

                https://www.cambridge.org/core/terms

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