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Open Access Research article

Identification of differentially expressed genes in chickens differing in muscle glycogen content and meat quality

Vonick Sibut12, Christelle Hennequet-Antier1, Elisabeth Le Bihan-Duval1, Sylvain Marthey3, Michel J Duclos1 and Cécile Berri1*

Author Affiliations

1 INRA UR83 Recherches Avicoles, Institut National de la Recherche Agronomique, F-37380 Nouzilly, France

2 Institut Technique de l'Aviculture, Centre INRA de Tours, F-37380 Nouzilly, France

3 INRA Centre de Ressources Biologiques des Animaux Domestiques et d'Intérêt Economique, Institut National de la Recherche Agronomique, F-78352 Jouy en Josas Cedex, France

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BMC Genomics 2011, 12:112  doi:10.1186/1471-2164-12-112

Published: 16 February 2011

Abstract

Background

The processing ability of poultry meat is highly related to its ultimate pH, the latter being mainly determined by the amount of glycogen in the muscle at death. The genetic determinism of glycogen and related meat quality traits has been established in the chicken but the molecular mechanisms involved in variations in these traits remain to be fully described. In this study, Chicken Genome Arrays (20 K) were used to compare muscle gene expression profiles of chickens from Fat (F) and Lean (L) lines that exhibited high and low muscle glycogen content, respectively, and of individuals exhibiting extremely high (G+) or low (G-) muscle glycogen content originating from the F2 cross between the Fat and Lean lines. Real-time RT-PCR was subsequently performed to validate the differential expression of genes either selected from the microarray analysis or whose function in regulating glycogen metabolism was well known.

Results

Among the genes found to be expressed in chicken P. major muscle, 197 and 254 transcripts appeared to be differentially expressed on microarrays for the F vs. L and the G+ vs. G- comparisons, respectively. Some involved particularly in lipid and carbohydrate metabolism were selected for further validation studies by real-time RT-PCR. We confirmed that, as in mammals, the down-regulation of CEBPB and RGS2 coincides with a decrease in peripheral adiposity in the chicken, but these genes are also suggested to affect muscle glycogen turnover through their role in the cAMP-dependent signalling pathway. Several other genes were suggested to have roles in the regulation of glycogen storage in chicken muscle. PDK4 may act as a glycogen sensor in muscle, UGDH may compete for glycogen synthesis by using UDP-glucose for glucoronidation, and PRKAB1, PRKAG2, and PHKD may impact on glycogen turnover in muscle, through AMP-activated signalling pathways.

Conclusions

This study is the first stage in the understanding of molecular mechanisms underlying variations in poultry meat quality. Large scale analyses are now required to validate the role of the genes identified and ultimately to find molecular markers that can be used for selection or to optimize rearing practices.