Hostname: page-component-8448b6f56d-t5pn6 Total loading time: 0 Render date: 2024-04-19T18:55:00.064Z Has data issue: false hasContentIssue false
  • English
  • Français

Current advances in proteomic analysis and its use for the resolution of poultry meat quality problems

Published online by Cambridge University Press:  18 September 2007

H. Remignon ,
C. Molette ,
R. Babile  and
X. Fernandez
H. Remignon*
Affiliation:
ZQPA Laboratory (supported by INRA-PHASE), Ecole Nationale Supérieure Agrononmique de Toulouse, BP 32607, 31326 Castanet-Tolosan, France
C. Molette
Affiliation:
ZQPA Laboratory (supported by INRA-PHASE), Ecole Nationale Supérieure Agrononmique de Toulouse, BP 32607, 31326 Castanet-Tolosan, France
R. Babile
Affiliation:
ZQPA Laboratory (supported by INRA-PHASE), Ecole Nationale Supérieure Agrononmique de Toulouse, BP 32607, 31326 Castanet-Tolosan, France
X. Fernandez
Affiliation:
ZQPA Laboratory (supported by INRA-PHASE), Ecole Nationale Supérieure Agrononmique de Toulouse, BP 32607, 31326 Castanet-Tolosan, France
*
*Corresponding author: remignon@ensat.fr
Get access

Abstract

If proteins are the functional units of almost all biological processes, the proteome represents the set of proteins expressed in a cell at a given time and for given conditions. Because muscle is mainly composed of water and proteins, it seems evident that proteome analysis can give much information on structures and functions of proteins involved in several mechanisms which determine meat quality. This paper aims to present the most classical techniques (i.e. sample preparation and protein solubilisation, protein separation by 2-DE or SDS-Page, protein detection and quantification, computer analysis of 2DE-pattern and finally protein identification) that are currently applied to analyse the proteome.

Proteomic study related to meat quality are somewhat limited, especially in poultry, but some results are presented to illustrate how proteomic approaches can bring a new point of view on new or already known meat quality problems. It is the case in mammals where meat tenderness had been given a new highlight with proteomic study but also in turkeys where new hypothesis for explaining PSE meat syndrome can be developed from proteomic analysis. Some studies have also reported interesting results in muscle growth and development in chickens.

Meat quality is a complex problem which includes several factors of variation such as genetics, handling of animals during production, transportation and slaughter and also the handling of meat during product processing. Proteomic tools can give a new point of view on these problems and help the biologist to understand and finally resolve it.

Keywords

proteome analysispoultry meat qualityelectrophoresis
Type
Reviews
Information
World's Poultry Science Journal , Volume 62 , Issue 1 , March 2006 , pp. 123 - 130
Copyright
Copyright © Cambridge University Press 2006

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

Footnotes

From a paper presented at the XVIIth European Symposium on the Quality of Poultry Meat, 23–26 May 2005, Doorwerth, The Netherlands

References

Bouley, J., Meunier, B., Chambon, C., De Smet, S., Hocquette, J-F. and Picard, B. (2005) Proteomic analysis of bovine skeletal muscle hypertrophy. Proteomics 5(2): 490–500.Google Scholar
Doherty, M.K., McLean, L., Hayter, J.R., Pratt, J.M., Robertson, D.H.L., El-Shafei, A., Gaskell, S.J. and Beynon, R. (2004) The proteome of chicken muscle: Changes in soluble proteins expression during a growth in a layer strain. Proteomics 4: 2082–2093.CrossRefGoogle Scholar
Görg, A., Weiss, W. and Dunn, M.J. (2004) Current two-dimensional electrophoresis technology for proteomics. Proteomics 4: 3665–3685.Google Scholar
Hedegaard, J., Horn, P., Lametsch, R., Sondergaard Moller, H., Roepstorff, P., Bendixen, C. and Bendixen, E. (2004) UDP-Glucose pyrophosphorylase is upregulated in carriers of the porcine RN- mutation in the AMP-activated protein kinase. Proteomics 4: 2448–2454.CrossRefGoogle ScholarPubMed
Kim, N-K., Joh, J-H., Park, H-R., Kim, O-H., Park, B-E. and Lee, C-S. (2004) Differential expression profiling of the proteomes and their mRNAin porcine white and red muscles. Proteomics 4: 3422–3428.CrossRefGoogle Scholar
Lametsch, R. and Bendixen, E. (2001) Proteome analysis applied to meat science: Characterizing post mortem changes in porcine muscle. Journal of Agricultural and Food Chemistry 49: 4531–4537.Google Scholar
Lametsch, R., Roepstorff, P. and Bendixen, E. (2002) Identification of protein degradation during post-mortem storage of pig meat. Journal of Agricultural and Food Chemistry 52: 5508–5512.Google Scholar
Lamtesch, R., Karlsson, A., Rosenvold, K., Andersen, H.J., Roepstorff, P. and Bendixen, E. (2003) Postmortem changes of porcine muscle related to tenderness. Journal of Agricultural and Food Chemistry 51: 6992–6997.Google Scholar
O'farrell, P.H. (1975) High resolution two-dimensional electrophoresis of proteins. Journal of Biological Chemistry 250: 4007–4021.CrossRefGoogle ScholarPubMed
Monin, G., Larzul, C., Le Roy, P., Culioli, J., Mourot, J., Rousset-Akrim, S., Talmant, A., Touraille, C. and Sellier, P. (1999) Effects of the halothane genotype and slaughter weight on texture of pork. Journal of Animal Science 77: 408–415.CrossRefGoogle ScholarPubMed
Molette, C., Rémignon, H. and Babilé, R. (2003) Early post-mortem pH and turkey breast meat quality. Proceeding of the XVI European Symposium on the Quality of Poultry MeatSaint-Brieuc (France)September 23–23, 48–53.Google Scholar
Molette, C., Rémignon, H. and Babilé, R. (2005) Modifications of glycolyzing enzymes induce a lowest meat quality in turkey. Poultry Science 84: 119–127.CrossRefGoogle Scholar
Pandley, A. and Mann, A. (2000) Proteomics to study genes and genomes. Nature 405: 837–846.CrossRefGoogle Scholar
Ünlü, M., Morgan, M.E. and Minden, J.S. (1997) Difference gel electrophoresis: a single gel method for detecting changes in cell extracts. Electrophoresis 18: 2071–2077.CrossRefGoogle Scholar