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

Vonick Sibut,Elisabeth Le Bihan-Duval,Cécile Berri,Sylvain Marthey,Michel J Duclos,Christelle Hennequet-Antier

doi:10.1186/1471-2164-12-112

Vonick Sibut, Elisabeth Le Bihan-Duval + Show 4 more

Open Access

https://doi.org/10.1186/1471-2164-12-112

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Abstract

BackgroundThe 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.ResultsAmong 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.ConclusionsThis 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.

Highlights

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
At 9 weeks of age, body weight was similar between F and L birds and between G+ and G- birds generated from the F2FL population
Studying phenotypically extreme chickens for muscle glycogen content generated from a F2 cross population helped to distinguish mechanisms involved in lipid and carbohydrate metabolism, which are highly related in the chicken

Summary

Introduction

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. There is no information available suggesting that a major gene could be involved in the control of glycogen content in muscle. Several studies have suggested that breast muscle glycogen content is related to growth and body composition: it decreases with growth rate and breast meat yield [2,11] and increases with carcass fatness [12,13]

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