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Manipulating tissue metabolism by amino acids

  • S. TESSERAUD (a1), N. EVERAERT (a2), S. BOUSSAID-OM EZZINE (a1), A. COLLIN (a1), S. MÉTAYER-COUSTARD (a1) and C. BERRI (a1)...

Abstract

Protein metabolism is considered to be regulated by amino acids, with major consequences on tissue development. There is evidence that lysine greatly affects carcass composition and muscle growth. In particular, a drastic effect of dietary provision of lysine has been observed on breast muscle development in chickens. Other essential amino acids, such as threonine and valine, do not have as pronounced an effect as lysine on body composition. Increasing lysine can also improve chicken breast muscle quality by increasing its ultimate pH and water holding capacity, but the underlying mechanisms are still unknown. Studies conducted over the last ten years indicate that, in addition to being substrates for protein synthesis, amino acids act as modulators of signal transduction pathways that control metabolism and cell functions. For instance, certain amino acids can modulate the activity of the intracellular protein kinases involved in the control of mRNA translation. Interestingly, enhanced responses to amino acids have been reported during the neonatal period, suggesting that early protein nutrition impacts on the development of broiler chicks. Methionine and cysteine have a very significant place among amino acids because they have several additional roles: they are precursors of essential molecules, for example cysteine is used for the synthesis of the antioxidant glutathione, and thus participates in the control of oxidative status, methionine is a source of the methyl groups needed for all biological methylation reactions, including methylation of DNA and histones, etc. These findings together indicate the importance of optimizing amino acid nutrition and providing a rationale for nutritional advice.

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Corresponding author

Corresponding author: sophie.tesseraud@tours.inra.fr

References

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Keywords

Manipulating tissue metabolism by amino acids

  • S. TESSERAUD (a1), N. EVERAERT (a2), S. BOUSSAID-OM EZZINE (a1), A. COLLIN (a1), S. MÉTAYER-COUSTARD (a1) and C. BERRI (a1)...

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