Hostname: page-component-cd9895bd7-dk4vv Total loading time: 0 Render date: 2024-12-18T15:57:55.779Z Has data issue: false hasContentIssue false
  • English
  • Français

Proteome dynamics during contractile and metabolic differentiation of bovine foetal muscle

Published online by Cambridge University Press:  01 July 2009

T. Chaze ,
B. Meunier ,
C. Chambon ,
C. Jurie  and
B. Picard
T. Chaze
Affiliation:
INRA, UR1213, Unité de Recherches sur les Herbivores, Equipe Croissance et Métabolisme du Muscle, F-63122 Saint-Genès Champanelle, France
B. Meunier
Affiliation:
INRA, UR1213, Unité de Recherches sur les Herbivores, Equipe Croissance et Métabolisme du Muscle, F-63122 Saint-Genès Champanelle, France
C. Chambon
Affiliation:
INRA, UR370 QuaPA, Plateforme Protéome du Centre INRA de Clermont-Theix-Lyon, Theix, F-63122 Saint-Genès-Champanelle, France
C. Jurie
Affiliation:
INRA, UR1213, Unité de Recherches sur les Herbivores, Equipe Croissance et Métabolisme du Muscle, F-63122 Saint-Genès Champanelle, France
B. Picard*
Affiliation:
INRA, UR1213, Unité de Recherches sur les Herbivores, Equipe Croissance et Métabolisme du Muscle, F-63122 Saint-Genès Champanelle, France
*
†E-mail: [email protected]
Get access

Abstract

Contractile and metabolic properties of bovine muscles play an important role in meat sensorial quality, particularly tenderness. Earlier studies based on Myosin heavy chain isoforms analyses and measurements of glycolytic and oxidative enzyme activities have demonstrated that the third trimester of foetal life in bovine is characterized by contractile and metabolic differentiation. In order to complete this data and to obtain a precise view of this phase and its regulation, we performed a proteomic analysis of Semitendinosus muscle from Charolais foetuses analysed at three stages of the third trimester of gestation (180, 210 and 260 days). The results complete the knowledge of important changes in the profiles of proteins from metabolic and contractile pathways. They provide new insights about proteins such as Aldehyde dehydrogenase family, Enolase, Dihydrolipoyl dehydrogenase, Troponin T or Myosin light chains isoforms. These data have agronomical applications not only for the management of beef sensorial quality but also in medical context, as bovine myogenesis appears very similar to human one.

Keywords

Bos tauruscontractile and metabolic differentiationin vivomyogenesisproteomics
Type
Full Paper
Information
animal , Volume 3 , Issue 7 , July 2009 , pp. 980 - 1000
Copyright
Copyright © The Animal Consortium 2009

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

Ansay, M 1974. Biochemical development of fetal muscle in the cow. III. Enzymes and differentiation. Annales de Biologie Animale, Biochimie, Biophysique 14, 105–116 (in French).CrossRefGoogle ScholarPubMed
Bouley, J, Chambon, C, Picard, B 2003. Proteome analysis applied to the study of muscle development and sensorial qualities of bovine meat. Sciences des Aliments 23, 75–78.CrossRefGoogle 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
Bouley, J, Meunier, B, Chambon, C, De Smet, S, Hocquette, JF, Picard, B 2005. Proteomic analysis of bovine skeletal muscle hypertrophy. Proteomics 5, 490–500.CrossRefGoogle ScholarPubMed
Briand, M, Talmant, A, Briand, Y, Monin, G, Durand, R 1981. Metabolic types of muscle in the sheep: I. Myosin ATPase, gloycolytic, and mitochondrial enzyme activities. European Journal of Applied Physiology 46, 347–358.Google Scholar
Caraux, G, Pinloche, S 2005. PermutMatrix: a graphical environment to arrange gene expression profiles in optimal linear order. Bioinformatics 21, 1280–1281.Google Scholar
Chaze, T, Meunier, B, Chambon, C, Jurie, C, Picard, B 2008. In vivo proteome dynamics during early bovine myogenesis. Proteomics 8, 4236–4248.CrossRefGoogle ScholarPubMed
Cho, M, Hughes, SM, Karsch-Mizrachi, I, Travis, M, Leinwand, LA, Blau, HM 1994. Fast myosin heavy chains expressed in secondary mammalian muscle fibers at the time of their inception. Journal of Cell Science 107, 2361–2371.CrossRefGoogle ScholarPubMed
Fougerousse, F, Edom-Vovard, F, Merkulova, T, Ott, M-O, Durand, M, Butler-Browne, G, Keller, A 2001. The muscle-specific enolase is an early marker of human myogenesis. Journal of Muscle Research and Cell Motility 22, 535–544.CrossRefGoogle ScholarPubMed
Gagnière, H, Picard, B, Geay, Y 1999. Contractile differentiation of foetal cattle muscles: intermuscular variability. Reproduction Nutrition Development 39, 637–655.CrossRefGoogle ScholarPubMed
Geay, Y, Bauchart, D, Hocquette, JF, Culioli, J 2001. Erratum: Effect of nutritional factors on biochemical, structural and metabolic characteristics of muscles in ruminants, consequences on dietetic value and sensorial qualities of meat (vol. 41, pp. 1–26, 2001). Reproduction Nutrition Development 41, 377.CrossRefGoogle Scholar
Huang, Q-Q, Chen, A, Jin, J-P 1999. Genomic sequence and structural organization of mouse slow skeletal muscle troponin T gene. Gene 229, 1–10.CrossRefGoogle ScholarPubMed
Iancu-Rubin, C, Atweh, GF 2004. The role of stathmin in the regulation of the cell cycle. Journal of Cellular Biochemistry 93, 242–250.Google Scholar
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
Maccatrozzo, L, Caliaro, F, Toniolo, L, Patruno, M, Reggiani, C, Mascarello, F 2007. The sarcomeric myosin heavy chain gene family in the dog: Analysis of isoform diversity and comparison with other mammalian species. Genomics 89, 224–236.CrossRefGoogle ScholarPubMed
Maier, A, McEwan, JC, Dodds, KG, Fischman, DA, Fitzsimons, RB, Harris, AJ 1992. Myosin heavy chain composition of single fibres and their origins and distribution in developing fascicles of sheep tibialis cranialis muscles. Journal of Muscle Research and Cell Motility 13, 551–572.CrossRefGoogle ScholarPubMed
Markiewicz, E, Ledran, M, Hutchison, CJ 2005. Remodelling of the nuclear lamina and nucleoskeleton is required for skeletal muscle differentiation in vitro. Journal of Cell Science 118, 409–420.CrossRefGoogle ScholarPubMed
Meunier, B, Dumas, E, Piec, I, Bechet, D, Hebraud, M, Hocquette, JF 2007. Assessment of hierarchical clustering methodologies for proteomic data mining. Journal of Proteome Research 6, 358–366.CrossRefGoogle ScholarPubMed
Muroya, S, Nakajima, I, Chikuni, K 2003. Amino acid sequences of multiple fast and slow troponin T isoforms expressed in adult bovine skeletal muscles. Journal of Animal Science 81, 1185–1192.Google Scholar
Nougués, J 1972. Study of changes in the number of muscular fibers during postnatal muscle growth in rabbits. Comptes rendus des Séances de la Société de Biologie et de ses Filiales 166, 165–172 (in French).Google Scholar
Pernelle, J-J, Righetti, PG, Wahrmann, JP, Herve, B 1990. Human skeletal muscle myosin light chains analyzed by immobilized pH gradients during ontogenesis: identification of new phosphorylatable isoforms of light chain 2. Electrophoresis 11, 325–332.Google Scholar
Picard, B, Barboiron, C, Duris, MP, Gagnière, H, Jurie, C, Geay, Y 1999. Electrophoretic separation of bovine muscle myosin heavy chain isoforms. Meat Science 53, 1–7.Google Scholar
Picard, B, Lefaucheur, L, Berri, C, Duclos, MJ 2002. Muscle fibre ontogenesis in farm animal species. Reproduction Nutrition Development 42, 415–431.CrossRefGoogle ScholarPubMed
Picard, B, Jurie, C, Cassar-Malek, I, Hocquette, JF, Lefaucher, L, Berri, C, Duclos, MJ, Alami-Duarte, H, Rescan, PY 2003. Myofibre typing and ontogenesis in farm animal species. Productions Animales 16, 117–123 (in French).Google Scholar
Picard, B, Jurie, C, Duris, MP, Renand, G 2006. Consequences of selection for higher growth rate on muscle fibre development in cattle. Livestock Science 102, 107–120.CrossRefGoogle Scholar
Picard, B, Barboiron, C, Chadeyron, D, Jurie, C 2007. Une technique d’électrophorèse appliquée à la séparation des isoformes de chaînes lourdes de myosines du muscle squelettique de bovin. Cahier des Techniques INRA 62, 17–24.Google Scholar
Rahman-Roblick, R, Johannes Roblick, U, Hellman, U, Conrotto, P, Liu, T, Becker, S, Hirschberg, D, Jornvall, H, Auer, G, Wiman, KG 2007. p53 targets identified by protein expression profiling. Proceedings of the National Academy of Sciences of the United States of America 104, 5401–5406.Google Scholar
Robelin, J, Lacourt, A, Béchet, D, Ferrara, M, Briand, Y, Geay, Y 1991. Muscle differentiation in the bovine fetus: a histological and histochemical approach. Growth, Development and Aging 55, 151–160.Google ScholarPubMed
Shrager, JB, Desjardins, PR, Burkman, JM, Konig, SK, Stewart, DR, Su, L, Shah, MC, Bricklin, E, Tewari, M, Hoffman, R, Rickels, MR, Jullian, EH, Rubinstein, NA, Stedman, HH 2000. Human skeletal myosin heavy chain genes are tightly linked in the order embryonic-IIa-IId/x-IIb-perinatal-extraocular. Journal of Muscle Research and Cell Motility 21, 345–355.CrossRefGoogle Scholar
Sophos, NA, Vasiliou, V 2003. Aldehyde dehydrogenase gene superfamily: the 2002 update. Chemico-Biological Interactions 143–144, 5–22.CrossRefGoogle ScholarPubMed
Stephens, FB, Constantin-Teodosiu, D, Greenhaff, PL 2007. New insights concerning the role of carnitine in the regulation of fuel metabolism in skeletal muscle. The Journal of Physiology 581, 431–444.Google Scholar
Talmadge, RJ, Roy, RR 1993. Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms. Journal of Applied Physiology 75, 2337–2340.CrossRefGoogle ScholarPubMed
Tsitsilonis, OE, Stoeva, S, Echner, H, Balafas, A, Margomenou, L, Katsoulas, HL, Troy, DJ, Voelter, W, Papamichail, M, Lymberi, P 2002. A skeletal muscle troponin T specific ELISA based on the use of an antibody against the soluble troponin T (16–31) fragment. Journal of Immunological Methods 268, 141–148.Google Scholar
Vasiliou, V, Pappa, A, Petersen, DR 2000. Role of aldehyde dehydrogenases in endogenous and xenobiotic metabolism. Chemico-Biological Interactions 129, 1–19.Google Scholar
Vaz, FM, Fouchier, SW, Ofman, R, Sommer, M, Wanders, RJA 2000. Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis. Journal of Biological Chemistry 275, 7390–7394.Google Scholar
Wei, N, Deng, XW 2003. THE COP9 SIGNALOSOME. Annual Review of Cell and Developmental Biology 19, 261–286.CrossRefGoogle ScholarPubMed
Wigmore, PM, Stickland, NC 1983. Muscle development in large and small pig fetuses. Journal of Anatomy 137, 235–245.Google ScholarPubMed