Hostname: page-component-8448b6f56d-t5pn6 Total loading time: 0 Render date: 2024-04-20T02:00:51.562Z Has data issue: false hasContentIssue false
  • English
  • Français

Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type

Published online by Cambridge University Press:  14 January 2011

N. Guillemin ,
C. Jurie ,
I. Cassar-Malek ,
J.-F. Hocquette ,
G. Renand  and
B. Picard
N. Guillemin
Affiliation:
UR1213, Unité de Recherches sur les Herbivores, INRA, PHASE Department, Centre de Clermont-Ferrand/Theix, 63122 Saint-Genès-Champanelle, France
C. Jurie
Affiliation:
UR1213, Unité de Recherches sur les Herbivores, INRA, PHASE Department, Centre de Clermont-Ferrand/Theix, 63122 Saint-Genès-Champanelle, France
I. Cassar-Malek
Affiliation:
UR1213, Unité de Recherches sur les Herbivores, INRA, PHASE Department, Centre de Clermont-Ferrand/Theix, 63122 Saint-Genès-Champanelle, France
J.-F. Hocquette
Affiliation:
UR1213, Unité de Recherches sur les Herbivores, INRA, PHASE Department, Centre de Clermont-Ferrand/Theix, 63122 Saint-Genès-Champanelle, France
G. Renand
Affiliation:
UMR1313, Génétique Animale et Biologie Intégrative, INRA, GA Department, 78350 Jouy-en-Josas, France
B. Picard*
Affiliation:
UR1213, Unité de Recherches sur les Herbivores, INRA, PHASE Department, Centre de Clermont-Ferrand/Theix, 63122 Saint-Genès-Champanelle, France
*
†E-mail: picard@clermont.inra.fr
Get access

Abstract

Some proteins have been revealed as biomarkers for beef tenderness by previous studies. These markers could be used in immunological tests to predict beef tenderness, in living animals as well as in carcasses. It is well known that rearing practices modify the amounts of mRNA and proteins. Therefore, the reliability of protein tests could be affected by livestock and biological effects such as production systems, breed, muscle and animal type. This study analysed the effects of animal and muscle type on 24 proteins. The animals studied were 67 young bulls and 44 steers of the Charolais breed, and muscles were Longissimus thoracis and Semitendinosus. Protein amounts were determined by Dot blot, an immunological technique. Results showed that expressions of 20 proteins were influenced by animal and/or muscle type. These results could lead to modifications and adaptations of prediction tests according to rearing practice, bovine breed and beef cut.

Keywords

beefprotein biomarkermeat tendernessprotein abundanceDot blot
Type
Full Paper
Information
animal , Volume 5 , Issue 6 , June 2011 , pp. 885 - 894
Copyright
Copyright © The Animal Consortium 2011

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.)

References

Bernard, C, Cassar-Malek, I, LeCunff, M, Dubroeucq, H, Renand, G, Hocquette, JF 2007. New indicators of beef sensory quality revealed by expression of specific genes. Journal of Agricultural and Food Chemistry 55, 5229–5237.CrossRefGoogle ScholarPubMed
Bouley, J 2004. Analyse protéomique du muscle squelettique bovin. PhD thesis, Université de Clermont-Ferrand 2, Clermont-Ferrand, France.Google Scholar
Bouley, J, Chambon, C, Picard, B 2004. Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry. Proteomics 4, 1811–1824.CrossRefGoogle ScholarPubMed
Bradford, MM 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein–dye binding. Analytical Biochemistry 72, 248–254.CrossRefGoogle ScholarPubMed
Brandstetter, AM, Picard, B, Geay, Y 1998. Muscle fibre characteristics in four muscles of growing male cattle II. Effect of castration and feeding level. Livestock Production Science 53, 25–36.CrossRefGoogle Scholar
Brandstetter, AM, Sauerwein, H, Veerkamp, JH, Geay, Y, Hocquette, JF 2002. Effects of muscle type, castration, age and growth rate on H-FABP expression in bovine skeletal muscle. Livestock Production Science 75, 199–208.CrossRefGoogle Scholar
Cassar-Malek, I, Picard, B, Bernard, C, Hocquette, JF 2008. Application of gene expression studies in livestock production systems: a European perspective. Australian Journal of Experimental Agriculture 48, 701–710.CrossRefGoogle Scholar
Cassar-Malek, I, Jurie, C, Bernard, C, Barnola, I, Micol, D, Hocquette, JF 2009. Pasture-feeding of Charolais steers influences skeletal muscle metabolism and gene expression. Journal of Physiology and Pharmacology 60, 83–90.Google ScholarPubMed
Cassar-Malek, I, Guillemin, N, Hocquette, JF, Micol, D, Bauchart, D, Picard, B 2010. Expression of DNAJA1 in bovine muscles according to developmental age and management factors. Animal (in press).Google Scholar
Choi, YM, Kim, BC 2009. Muscle fiber characteristics, myofibrillar protein isoforms, and meat quality. Livestock Science 122, 105–118.CrossRefGoogle Scholar
Clark, KA, McElhinny, AS, Beckerle, MC, Gregorio, CC 2002. Striated muscle cytoarchitecture: an intricate web of form and function. Annual Review of Cell and Developmental Biology 18, 637–706.CrossRefGoogle ScholarPubMed
Dransfield, E, Martin, JF, Bauchart, D, Abouelkaram, S, Lepetit, J, Culioli, J, Jurie, C, Picard, B 2003. Meat quality and composition of three muscles from French cull cows and young bulls. Animal Science 76, 387–399.CrossRefGoogle Scholar
Fink, AL 1999. Chaperone-mediated protein folding. Physiological Reviews 79, 425–449.CrossRefGoogle ScholarPubMed
Fritsche, S, Steinhart, H 1998. Differences in natural steroid hormone patterns of beef from bulls and steers. Journal of Animal Science 76, 1621–1625.CrossRefGoogle ScholarPubMed
Geay, Y, Bauchart, D, Hocquette, JF, Culioli, J 2001. Effect of nutritional factors on biochemical, structural and metabolic characteristics of muscles in ruminants, consequences on dietetic value and sensorial qualities of meat. Reproduction Nutrition Development 41, 1–26 (Erratum 41, 377).CrossRefGoogle ScholarPubMed
Gilbert, R, Cohen, JA, Pardo, S, Basu, A, Fischman, DA 1999. Identification of the A-band localization domain of myosin binding proteins C and H (MyBP-C, MyBP-H) in skeletal muscle. Journal of Cell Science 112, 69–79.CrossRefGoogle Scholar
Golenhofen, N, Perng, MD, Quinlan, RA, Drenckhahn, D 2004. Comparison of the small heat shock proteins alpha B-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle. Histochemistry and Cell Biology 122, 415–425.CrossRefGoogle Scholar
Guillemin, N 2010. Marqueurs protéiques de la tendreté de la viande bovine: étude prédictive et fonctionnelle. Université Blaise Pascal, Clermont-Ferrand, France.Google Scholar
Guillemin, N, Meunier, B, Jurie, C, Cassar-Malek, I, Hocquette, JF, Levéziel, H, Picard, B 2009a. Validation of a Dot-blot quantitative technique for large-scale analysis of beef tenderness biomarkers. Journal of Physiology and Pharmacology 60, 91–97.Google ScholarPubMed
Guillemin, N, Cassar-Malek, I, Hocquette, JF, Jurie, C, Micol, D, Listrat, A, Levéziel, H, Renand, G, Picard, B 2009b. La maîtrise de la tendreté de la viande bovine: identification de marqueurs biologiques. INRA Productions Animales 22, 331–344.CrossRefGoogle Scholar
Guillemin, N, Jurie, C, Renand, G, Hocquette, JF, Micol, D, Lepetit, J, Levéziel, H, Picard, B 2010. Tenderness phenotypic and proteomic markers. Journal of Animal Science (in press).Google Scholar
Herrmann, H, Bar, H, Kreplak, L, Strelkov, SV, Aebi, U 2007. Intermediate filaments: from cell architecture to nanomechanics. Nature Reviews Molecular Cell Biology 8, 562–573.CrossRefGoogle ScholarPubMed
Hocquette, JF, Lehnert, SA, Barendse, W, Cassar-Malek, I, Picard, B 2007. Recent advances in cattle functional genomics and their application to beef quality. Animal 1, 159–173.CrossRefGoogle ScholarPubMed
Jia, X, Hollung, K, Therkildsen, M, Hildrum, KI, Bendixen, E 2006. Proteome analysis of early post-mortem changes in two bovine muscle types: M. longissimus dorsi and M. semitendinosis. Proteomics 6, 936–944.CrossRefGoogle ScholarPubMed
Jia, X, Veiseth-Kent, E, Grove, H, Kuziora, P, Aass, L, Hildrum, KI, Hollung, K 2009. Peroxiredoxin-6 – a potential protein marker for meat tenderness in bovine M. Longissimus thoracis muscle. Journal of Animal Science 87, 2391–2399.CrossRefGoogle ScholarPubMed
Junn, E, Taniguchi, H, Jeong, BS, Zhao, X, Ichijo, H, Mouradian, MM 2005. Interaction of DJ-1 with Daxx inhibits apoptosis signal-regulating kinase 1 activity and cell death. Proceedings of the National Academy of Sciences of the United States of America 102, 9691–9696.CrossRefGoogle ScholarPubMed
Jurie, C, Robelin, J, Picard, B, Renand, G, Geay, Y 1995. Inter-animal variation in the biological characteristics of muscle tissue in male Limousin cattle. Meat Science 39, 415–425.CrossRefGoogle ScholarPubMed
Jurie, C, Picard, B, Hocquette, JF, Dransfield, E, Micol, D, Listrat, A 2007. Muscle and meat quality characteristics of Holstein and Salers cull cows. Meat Science 77, 459–466.CrossRefGoogle ScholarPubMed
Kaul, SC, Deocaris, CC, Wadhwa, R 2007. Three faces of mortalin: a housekeeper, guardian and killer. Experimental Gerontology 42, 263–274.CrossRefGoogle ScholarPubMed
Kiang, JG, Tsokos, GC 1998. Heat shock protein 70 kDa: molecular biology, biochemistry, and physiology. Pharmacology & Therapeutics 80, 183–201.CrossRefGoogle ScholarPubMed
Kubo, E, Hasanova, N, Tanaka, Y, Fatma, N, Takamura, Y, Singh, DP, Akagi, Y 2010. Protein expression profiling of lens epithelial cells from Prdx6-depleted mice and their vulnerability to UV radiation exposure. American Journal of Physiology – Cell Physiology 298, C342–C354.CrossRefGoogle ScholarPubMed
Lametsch, R, Karlsson, A, Rosenvold, K, Andersen, HJ, Roepstorff, P, Bendixen, E 2003. Postmortem proteome changes of porcine muscle related to tenderness. Journal of Agricultural and Food Chemistry 51, 6992–6997.CrossRefGoogle ScholarPubMed
Laufen, T, Mayer, MP, Beisel, C, Klostermeier, D, Mogk, A, Reinstein, J, Bukau, B 1999. Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones. Proceedings of the National Academy of Sciences of the United States of America 96, 5452–5457.CrossRefGoogle ScholarPubMed
Lee, CE, McArdle, A, Griffiths, RD 2007. The role of hormones, cytokines and heat shock proteins during age-related muscle loss. Clinical Nutrition 26, 524–534.CrossRefGoogle ScholarPubMed
Lefaucheur, L 2010. A second look into fibre typing – relation to meat quality. Meat Science 84, 257–270.CrossRefGoogle ScholarPubMed
Moradas-Ferreira, P, Costa, V, Piper, P, Mager, W 1996. The molecular defences against reactive oxygen species in yeast. Molecular Microbiology 19, 651–658.CrossRefGoogle ScholarPubMed
Morris, CA, Cullen, NG, Hickey, SM, Dobbie, PM, Veenvliet, BA, Manley, TR, Pitchford, WS, Kruk, ZA, Bottema, CD, Wilson, T 2006. Genotypic effects of calpain 1 and calpastatin on the tenderness of cooked M. longissimus dorsi steaks from Jersey × Limousin, Angus and Hereford-cross cattle. Animal Genetics 37, 411–414.CrossRefGoogle ScholarPubMed
Paulin, D, Li, ZL 2004. Desmin: a major intermediate filament protein essential for the structural integrity and function of muscle. Experimental Cell Research 301, 1–7.CrossRefGoogle Scholar
Picard, B, Barboiron, C, Duris, MP, Gagniere, H, Jurie, C, Geay, Y 1999. Electrophoretic separation of bovine muscle myosin heavy chain isoforms. Meat Science 53, 1–7.CrossRefGoogle ScholarPubMed
Picard, B, Berri, C, Lefaucheur, L, Molette, C, Sayd, T, Terlouw, C 2010. Skeletal muscle proteomics in livestock production. Briefings in Functional Genomics 9, 259–278.CrossRefGoogle ScholarPubMed
Picard, B, Jurie, C, Bauchart, D, Dransfield, E, Ouali, A, Martin, JF, Jailler, R, Lepetit, J, Culioli, J 2007. Caractéristiques des muscles et de la viande des principales races bovines allaitantes du Massif Central. Sciences des Aliments 27, 168–180.CrossRefGoogle Scholar
Schreurs, NM, Garcia, F, Jurie, C, Agabriel, J, Micol, D, Bauchart, D, Listrat, A, Picard, B 2008. Meta-analysis of the effect of animal maturity on muscle characteristics in different muscles, breeds, and sexes of cattle. Journal of Animal Science 86, 2872–2887.CrossRefGoogle ScholarPubMed
Sun, Y, MacRae, TH 2005. Small heat shock proteins: molecular structure and chaperone function. Cellular and Molecular Life Sciences 62, 2460–2476.CrossRefGoogle ScholarPubMed
Totland, GK, Kryvi, H 1991. Distribution patterns of muscle fibre types in major muscles of the bull (Bos taurus). Anatomy and Embryology 184, 441–450.CrossRefGoogle ScholarPubMed
Veysset, P, Bebin, D, Lherm, M 2005. Adaptation to Agenda 2000 (CAP reform) and optimisation of the farming system of French suckler cattle farms in the Charolais area: a model-based study. Agricultural Systems 83, 179–202.CrossRefGoogle Scholar
Vicart, P, Caron, A, Guicheney, P, Li, ZL, Prevost, MC, Faure, A, Chateau, D, Chapon, F, Tome, F, Dupret, JM, Paulin, D, Fardeau, M 1998. A missense mutation in the alpha B-crystallin chaperone gene causes a desmin-related myopathy. Nature Genetics 20, 92–95.CrossRefGoogle Scholar
Voss, MR, Stallone, JN, Li, M, Cornelussen, RNM, Knuefermann, P, Knowlton, AA 2003. Gender differences in the expression of heat shock proteins: the effect of estrogen. American Journal of Physiology – Heart and Circulatory Physiology 285, H687–H692.CrossRefGoogle Scholar
Wang, X, Phelan, SA, Forsman-Semb, K, Taylor, EF, Petros, C, Brown, A, Lerner, CP, Paigen, B 2003. Mice with targeted mutation of peroxiredoxin 6 develop normally but are susceptible to oxidative stress. Journal of Biological Chemistry 278, 25179–25190.CrossRefGoogle ScholarPubMed