The proteome of chicken skeletal muscle: Changes in soluble protein expression during growth in a layer strain

被引:100
作者
Doherty, MK
McLean, L
Hayter, JR
Pratt, JM
Robertson, DHL
El-Shafei, A
Gaskell, SJ
Beynon, RJ [1 ]
机构
[1] Univ Liverpool, Prot Funct Grp, Dept Vet Preclin Sci, Liverpool L69 7ZJ, Merseyside, England
[2] Univ Manchester, Michael Barber Ctr Mass Spectrometry, Dept Chem, Manchester M60 1QD, Lancs, England
关键词
chicken; Gallus gallus; matrix assisted laser desorption/ionization-time of flight; pectoralis muscle; skeletal muscle; two-dimensional gel electrophoresis;
D O I
10.1002/pmic.200300716
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The whole animal, and the pectoralis muscle in particular, grows at a greatly enhanced rate in chickens selected for meat production (broilers) when compared to those selected for egg production (layers). As part of an ongoing study to analyse muscle protein dynamics under conditions of rapid growth, we have embarked upon a preliminary characterisation of the proteome of layer chicken pectoralis muscle, at specified time-points from 1 to 27 days after hatching. Soluble extracts of muscle homogenates were separated by two-dimensional (2-D) gel electrophoresis and selected spots were analysed by in-gel tryptic digestion and matrix assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry. Of 90 spots, 51 gave mass spectra that matched to existing chicken proteins present in on-line databases, 12 matched equivalent proteins from non-avian species and 11 yielded good quality spectra but were unable to be matched against existing databases. For many of these proteins, growth over 27 days elicited dramatic changes in relative expression levels. Chicken skeletal muscle offers an excellent system for developmental proteomics.
引用
收藏
页码:2082 / 2093
页数:12
相关论文
共 50 条
[31]  
SAKODA S, 1988, J BIOL CHEM, V263, P16899
[32]   MUSCLE GROWTH AND PROTEIN-DEGRADATION DURING EARLY DEVELOPMENT IN CHICKS OF FAST AND SLOW GROWING STRAINS [J].
SAUNDERSON, CL ;
LESLIE, S .
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-PHYSIOLOGY, 1988, 89 (03) :333-337
[33]   Expression and conservation of apolipoprotein AIT in an avian species [J].
Steinmetz, A ;
Hermann, M ;
Nimpf, J ;
Aebersold, R ;
Ducret, A ;
Weinberg, RB ;
Schneider, WJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (17) :10543-10549
[34]   Evolving functions of apolipoprotein AIV: From birds to mammals [J].
Steinmetz, A ;
Schneider, WJ .
TRENDS IN CARDIOVASCULAR MEDICINE, 1999, 9 (06) :153-157
[35]  
STEVENS L, 1991, GENETICS EVOLUTION D, V1
[36]  
Stolz M, 1998, J CELL SCI, V111, P1207
[37]   Relative contribution of variation within the APOC3/A4/A5 gene cluster in determining plasma triglycerides [J].
Talmud, PJ ;
Hawe, E ;
Martin, S ;
Olivier, M ;
Miller, GJ ;
Rubin, EM ;
Pennacchio, LA ;
Humphries, SE .
HUMAN MOLECULAR GENETICS, 2002, 11 (24) :3039-3046
[38]   CHICKEN ALPHA-ENOLASE BUT NOT BETA-ENOLASE HAS A SRC-DEPENDENT TYROSINE-PHOSPHORYLATION SITE - CDNA CLONING AND NUCLEOTIDE-SEQUENCE ANALYSIS [J].
TANAKA, M ;
MAEDA, K ;
NAKASHIMA, K .
JOURNAL OF BIOCHEMISTRY, 1995, 117 (03) :554-559
[39]   SWITCHING IN LEVELS OF TRANSLATABLE MESSENGER-RNAS FOR ENOLASE ISOZYMES DURING DEVELOPMENT OF CHICKEN SKELETAL-MUSCLE [J].
TANAKA, M ;
SUGISAKI, K ;
NAKASHIMA, K .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1985, 133 (03) :868-872
[40]  
Tarugi P, 1996, J LIPID RES, V37, P493