http://www.jstage.jst.go.

jp/browse/jpsa
doi:+*.,+.+/jpsa.**3*--
Copyright ῌ ,*+*, Japan Poultry Science Association.

Supamit Mekchay+, ., Tawatchai Teltathum,, ., Sutkhet Nakasathien- and Petai Pongpaichan+

+
Department of Animal Science, Faculty of Agriculture, Chiang Mai University, Chiang Mai /*,**, Thailand
,
Human and Animal Biotechnology, Graduate School, Chiang Mai University, Chiang Mai /*,**, Thailand
-
Department of Agronomy, Faculty of Agriculture, Kasetsart University, Bangkok +*3**, Thailand
.
Center for Agricultural Biotechnology: AG-BIO/PERDO-CHE, Thailand

The objective of this study was to identify protein markers for tenderness trait of Thai native and commercial broiler
chicken muscles. The proteome of chicken muscle with high- and low-shear force values was analyzed by two-dimensional
gel electrophoresis and MALDI-TOF/MS technique. A total of +03 and +/2 protein spots were observed in Thai native and
commercial broiler chicken muscles, respectively. Of these proteins, five protein spots were up- and down-regulated with low
shear force values of chicken meat. Selected three protein spots were identified and showed homology with pyruvate kinase
, muscle (PKM,), phosphoglycerate mutase + (PGAM+) and triosephosphate isomerase + (TPI+) of chicken. The PKM,
and TPI+ were correlated with shear force values of chicken meats. Whereas, the PGAM+, B.0 and B+*1 trended toward
an association with shear force values. The results indicate that these enzymes of the glycolytic pathway play a major role
in the energy metabolism process of muscle and meat characteristics. These findings promote the importance of the muscle
metabolic enzymes and could be used as functional candidate genes for meat quality traits in chicken.

Key words: broiler, gene expression, muscle, proteome, Thai native chicken
J. Poult. Sci., .1: 2ῌ+,, ,*+*
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Proteomic technology is a powerful method to identify

Introduction
Meat quality of chicken is an economically important
trait. Thai native chicken has a unique taste with tough
and strong muscles. Its meat is very popular among
consumers and the market price is two to three times
higher than the commercial broiler chicken
(Wattanachant et al., ,**.). However, Thai native chick-
en has slow growth rates and contains low fat. The
chemical composition, color, texture and structure of the
Thai native and commercial broiler chicken have been
characterized before and after cooking (Wattanachant et
al., ,**., ,**/). Thai native chicken has a firmer texture
and more flavor than the commercial broiler
(Wattanachant et al., ,**.). Genetic control of meat
quality in chicken is poorly understood. Recently, the
QTLs a#ecting growth, carcass composition, metabolic
traits of chickens have been identified (Zhou et al., ,**0a,
b, ,**1). Moreover, we have reported di#erentially ex-
pressed genes in Thai native and commercial broiler chick-
en muscles (Mekchay et al., ,**0).
Received: April ,,, ,**3, Accepted: September ., ,**3
Released Online Advance Publication: December +*, ,**3
Correspondence: Dr. S. Mekchay, Department of Animal Science,
Faculty of Agriculture, Chiang Mai University, Chiang Mai /*,**,
Thailand. (E-mail: agismkch@chiangmai.ac.th)
proteins that play a major role in the mechanism for
controlling meat quality traits. The proteome of muscle
have been characterized in various livestock species such
as cattle, pigs, sheep and chicken. Proteomic analysis was
used to evaluate postmortem proteolysis changes and meat
quality of pork and beef including tenderness, drip loss,
meat color and water holding capacity (Lametsch et al.,
,**-; Sayd et al., ,**0; Jia et al., ,**1; van de Wiel and
Zhang, ,**1; Kwasiborski et al., ,**2; Morzel et al.,
,**2) as well as protein changes in dry-cured ham and
pork products (Di Luccia et al., ,**/; Picariello et al.,
,**0). A proteomic approach has also been used to
investigate the e#ects of genetic variation on di#erential
protein expression in bovine, ovine and porcine skeletal
muscle (Bouley et al., ,**/; Hamelin et al., ,**0; Hollung
et al., ,**3) as well as proteome mapping of bovine and
ovine muscles have been reported (Bouley et al., ,**.;
Hamelin et al., ,**0). Moreover, proteome of muscle
growth and development have been characterized in
chicken and pigs (Doherty et al., ,**.; Hollung et al.,
,**3). However, information on molecular markers for
meat tenderness of chickens is limited. Here, we have
reported proteome markers for tenderness trait in Thai
native chicken and commercial broiler chicken muscles.
 Mekchay et al.: Proteome of Chicken Muscles
Materials and Methods
Animals
One hundred mixed-sex Thai native chickens (namely
“Pradhuhangdum”) were obtained from the Livestock
Breeding and Research Center, Sanpatong, Chiang Mai
province, and +** mixed-sex commercial broiler chickens
were obtained from a local company. Both chicken breeds
were reared under the same conditions at the research
farm of the Department of Animal Science, Chiang Mai
University, Chiang Mai, Thailand. Pectoralis muscles
were collected from individual animals at 0 weeks for
commercial broiler and +0 weeks for Thai native chickens
(based on the same market size of chicken), respectively.
All tissue samples were kept at 2*. Among ,**
animals, / highest- and / lowest-shear force values of Thai
native chickens and / highest- and / lowest-shear force
values of commercial broiler chickens were applied to
proteomic analysis and real time PCR quantification.
Shear Force Measurement
Shear force of chicken muscle was measured using a
texture analyzer according to methods described by
Wattanachant et al. (,**.). Measured shear force of
chicken muscle was performed with three replicates for
each sample. The shear force values were expressed in
kilograms (kg).
Proteomic Analysis
The proteins of the pectoralis muscles were extracted
and cleaned with the ,-D clean up kit (Amersham Biosci-
ences, Bangkok, Thailand). The concentration of the pu-
rified protein was determined with ,-D Quant Kit
(Amersham Biosciences, Bangkok, Thailand). Proteomic
analysis was performed according to the modified method
of Kuo et al. (,**/) using two dimensional gel electropho-
resis (,-DE) and matrix-assisted laser desorption ioniza-
tion time of flight/mass spectrometry (MALDI-TOF/
MS). Briefly, +* mg of purified protein were diluted with
+,/ ml of rehydration bu#er (2M urea, .ῌ CHAPS, 0*
mM DTT, *./ῌ IPG bu#er and *.**,ῌ bromophenol
blue) and applied to the Immobiline DryStrips (pH -ῌ+*,
1 cm, Amersham Biosciences, Thailand). The strips were
rehydrated at ,* for +, h and first-dimensional iso-
electric focusing (IEF) was carried out on Ettan IPGphor
II IEF system (Amersham Biosciences, Thailand) using
-** V for +/* Vh, +,*** V for -** Vh, /,*** V for .,*** Vh
and /,*** V for /** Vh, /* mA at ,*. The strips were
incubated in equilibration bu#er for +/ min and then
applied on +/ῌ SDS polyacrylamide gel electrophoresis.
The gels were either silver or Coomassie Blue stained. The
protein spots were scanned and their intensity was
analyzed as normal volume using Dymension Revolution-
ary ,-DE software version ,.*/ a (Syngene, UK).
The protein spots of interest were excised and proteins
were subjected to in gel trypsin digestion. Peptides were
analyzed using matrix-assisted laser desorption ionization
time of flight/mass spectrometry (MALDI-TOF/MS).
Peptide mass fingerprints were compared with known
9
peptide of NCBI database using MASCOT software
(http://www.matrixscience.com).
Quantitative Real Time PCR
To validate the results of di#erential proteome of chick-
en muscles at mRNA level, real time quantitative PCR
was performed using cDNA from pectoralis muscles of
Thai native chickens and commercial broiler chickens
with high- and low-shear force values. Total RNA was
isolated from the pectoralis muscles using Trizol reagent
(Invitrogen, CA) according to the manufacturer’s proce-
dure and treated with DNase I (Promega, WI) for + h at
-1. RNA purification was performed using the RNeasy
mini Kit (Qiagen, Germany). Total RNA samples were
reverse transcribed in +* ml reaction volume containing +
mg of total RNA, +** pmol of oligo (dT)+, primers, heated
for / min at 1* and placed on ice for - min. Then +* ml
of mixture components of +x first strand bu#er, +* mM
dNTPs, +* mM DTT, +* units RNase inhibitor (Promega,
WI) and ,** units of SuperScript III reverse transcriptase
(Invitrogen, CA) were added, incubated at /* for 0*
min and finally heated to stop the reaction at 1* for +/
min and stored at ,* until analysis.
The expression levels of target genes were determined
on Chromo . RealTimePCR Detector (MJ Research
PTC-,**, Ramsey, MN). The PCRs were performed in
,* ml reaction volume containing +* ml ,x QuantiTech
SYBR Green master mix (Qiagen, Germany), , ml of
muscle cDNA sample and forward and reverse primers
(Table +) in optimal combinations of concentrations (.
mM). The target genes were amplified in duplication using
the following conditions: an initial denaturing at 3/ for
+/ min, ./ cycles of 3/ for +/ s, /0ῌ0, for -* s, 1,
for + min. The expressed target genes in muscles were
reported as relative gene expression using the comparative
threshold cycle (CT) method (,DDCT) (Livak and
Schmittgen, ,**+).
Statistical Analysis
Relative protein spot densities of ,-DE were analyzed
with paired Student’s t-test, including phenotypic values of
two extreme shear force groups of Thai native chicken and
commercial broiler chicken muscles. Moreover, correla-
tion coe$cients of protein expression levels and shear
force values were calculated. Analysis of variance was
used to compare the relative mRNA expression levels of
high- and low-shear force groups in Thai native and
commercial broiler chicken breeds. All statistical tests
were performed with SAS software release 0.*2 (SAS Inst
Inc., Cary, NC) and di#erences were considered signifi-
cant at P*.*/.
Results and Discussion
The average shear force values of Thai native chickens
(at +0 weeks of age) and commercial broiler (at 0 weeks
of age) were /.,.*.,. and ,.*.*.,. kg, respectively.
Out of ,** chickens, the / high- and / low-shear force
values of Thai native chicken muscles were 3.3.*.3- and
,.03*.+. kg (P*.*+), respectively. However, two ex-
 10 J. Poult. Sci., .1 (+)
Table +. Primers used for quantification of target genes
Genes Sequence
PKM, /ῌ-GCTGTCAGGAAGGTGCTA--ῌ
/ῌ-GATCTCAATACCCAGGTCA--ῌ
PGAM+ /ῌ-CCTGCCCTTCTGGAATGAG--ῌ
/ῌ-TGGGCTTCAGGTTCTTGTCC--ῌ
TPI+ /ῌ-CTTGCCTATGAGCCAGTTTG--ῌ
/ῌ-GTTCCTTACAGTTGCCACCA--ῌ
ACTB /ῌ-TGAACCCCAAAGCCAACAGA--ῌ
/ῌ-GAGGGCGTAGCCTTCATAG--ῌ
Fig. +. Proteome profiling of chicken pectoralis muscle.
M shows protein molecular marker LMW standards
(Amersham Biosciences, Thailand). Arrows indicate
the identified protein positions that were di#erentially
expressed between high- and low-shear force groups of
Thai native (N,-, N+*/ and N+++) or commercial
broiler chicken muscles (B.0, B+*1).
treme shear force groups of commercial broiler chicken
muscles were *./,*.*2 (low-shear force, n/) and ..+,
*..3 kg (high-shear force, n/) (P*.*+).
Proteome analysis of chicken muscle revealed a total of
+03 and +/2 protein spots in Thai native and commercial
broiler chicken muscles, respectively. Figure + shows the
proteome profiling of chicken pectoralis muscles. Table ,
shows proteins di#erentially expressed in high- and low-
shear force groups of Thai native chicken and commercial
broiler chicken muscles. Five spots were significantly up-
and down-regulated and are related to low shear force
values of chicken meat. Three protein spots (N,-, N+*/
and N+++) had decreased expression levels in low-shear
force group of Thai native chicken and two protein spots
(B.0 and B+*1) had increased expression levels in the
low-shear force group of commercial broiler chicken
muscle. The N,- and N+++ spots were correlated with
shear force values of chicken meat. Whereas, the N+*/, B
GenBank Amplicon
Tm ()
accession no. size (bp)
J**3*- /0 +.1
NM_**+*-+//0 0, +3+
NM_,*/./+ 0* +1/
L*2+0/ 0* +2.
.0 and B+*1 spots trended toward an association with
shear force values (Table ,). Of these proteins, three
protein spots (N,-, N+*/ and N+++) were selected,
identified and showed homology with pyruvate kinase ,
muscle (PKM,), phosphoglycerate mutase + (PGAM+)
and triosephosphate isomerase + (TPI+) of chicken, re-
spectively (Table ,).
All of these proteins are the glycolytic enzymes involved
in energy metabolism. PKM, catalyzes the conversion of
phosphoenolpyruvate to pyruvate in the last step of the
glycolysis pathway (Fontanesi et al., ,**2). PGAM cata-
lyzes the conversion of --phosphoglycerate into ,-phos-
phoglycerate using ,,--biphosphoglycerate as a cofactor
(Qiu et al., ,**2). Whereas, TPI+ is a glycolytic enzyme
that catalyses the conversion of dihydroxyacetone phos-
phate to glyceraldehyde---phosphate (Solem et al., ,**2).
In previous studies, the proteomes of porcine muscles
during post mortem periods were analyzed and several
proteins were found to be associated with meat quality and
meat tenderness. These proteins included actin, myosin
heavy chain, titin, myosin light chain I, myosin light II,
CapZ and coflin, troponin, desmin as well as metabolic
enzymes, like glycogen phosphorylase, creatine kinase,
phosphopyruvate hydratase, myokinase, pyruvate kinase,
dihydrolipoamide succinyltransferase and triosephosphate
isomerase + (Lametsch et al., ,**,, ,**-; Morzel et al.,
,**.; Hwang et al., ,**/). Moreover, proteome analysis
of bovine muscle during the early postmortem period
showed that metabolic enzymes of the glycolytic pathway
had changed as well as proteolytic enzymes, structural
proteins and defense proteins (Jia et al., ,**0, ,**1).
However, the PKM, and PGAM, genes were significantly
associated with growth, meat and fat deposition as well as
muscle growth and development traits in pigs (Fontanesi
et al., ,**2; Qiu et al., ,**2).
We found no significant di#erence of mRNA expression
levels of PKM,, PGAM+ and TPI+ genes in high- and
low-shear force groups of Thai native and commercial
broiler chicken breeds (Table -). However, mRNA ex-
pression levels of TPI+ gene were correlated with its
protein expression levels in Thai native (P*.*/) and
commercial broiler chickens (P*.*2). Whereas, no
relationships between mRNA expression levels of PKM,
 Mekchay et al.: Proteome of Chicken Muscles 11

Table ,. Proteins di#erentially expressed in high- and low-shear force groups of Thai native and commercial broiler
chicken muscles
Observed
accession Mowse ῌ Spot ratio r
Breeds Spot no. Protein name MW
no. score coverage (P-value) (P-value)
(kDa)/pI
Native N,- pyruvate kinase , muscle NP_33*2** ,*, .- /24./14- +4,.  *4*. *41+ *4*,
N+*/ phosphoglycerate mutase + P2.+1. 13 .3 ,243/14, +4,.  *4*. *4.3 *4+/
N+++ triosephosphate isomerase + NP_33*12, ++0 2. ,041/042 +4,2 *4*+ *40/ *4*.
Broiler B.0 unidentified    .-4//04/ *42,  *4*. *4/, *4+,
B+*1 unidentified    ,/4//241 *41-  *4*/ *4/- *4++
Spot ration: average quantity (spot intensities) in high-shear force group/average quantity in low-shear force group. A negative was
showed when the protein was over-expressed in low-shear force group. rpearson correlation coe$cients.

Table -. mRNA expression levels of PKM,, PGAM and TPI+ in

muscle of Thai native (+0 weeks of age) and commercial broiler
chickens (0 weeks of age)
Relative gene expression
Breeds Genes P-value
High-shear force Low-shear force
Native PKM, *422 *4,0 +4*1 *4.* *41*
PGAM+ *42. *4.- +4*- *4/2 *42*
TPI+ *43- *4+1 +4.1 *400 *4.1
Broiler PKM, +4+, *4-* *42+ *4+/ *4-3
PGAM+ +4+, *4+0 +40+ *40* *4.0
TPI+ +4-, *4,- ,4*0 *42+ *4*2

P*.+; * P*.*/.

Table .. Pearson correlation coe$cients of mRNA are associated with tenderness of chicken muscles. The
expression levels of target genes and their protein ex- results indicate that these enzymes of glycolytic pathway
pression levels in muscles of Thai native and com- play a major role in energy metabolism process of muscle
mercial broiler chickens and related to meat characteristics. Further study, the
single nucleotide polymorphism of the genes that encoded
gene-protein Correlation
Breeds P-value for these proteome markers will be identified and their
name coe$cient
association with meat quality traits of chicken will be
Native PKM, *4*/ *422 analyzed.
PGAM+ *4+. *403
TPI+ *41,* *4*, Acknowledgments
Broiler PKM, *4-, *4-1 This work was supported by grants from the Commis-
PGAM+ *4-* *4-3 sion on Higher Education and the Thai Research Fund
TPI+ *4/3 *4*1 (MRG/*2**11) and partially supported by the Center of

P*.+; * P*.*/ Excellence on Agricultural Biotechnology, Postgraduate
Education and Research Development O$ce, Commission
on Higher Education.
and PGAM+ genes with their protein expression levels
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