Meat and fish flesh quality

improvement with proteomic

applications
B. Picard,* F. Lefèvre,† and B. Lebret ‡§
* INRA, UMR1213 Herbivores, F-63122 Saint-Genès-Champanelle, France

† INRA, UR1037 Fish Physiology and Genomics, F-35042 Rennes, France

‡ INRA, UMR1348 Pegase, F-35590 Saint-Gilles, France

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§ Agrocampus Ouest, UMR1348 Pegase, F-35000 Rennes, France

genes and/or proteins whose expression or abundance is associated to the

Implications value of a phenotypic trait of interest, such as the quality of a product.
These genes or proteins are thus considered as biomarkers that could be
• Proteomics technologies have been used to better understand the
used to predict a given phenotype. In this review, we will focus on studies
development of complex phenotypic traits such as meat and fish
undertaken at the protein level, because proteins have the advantage to
flesh quality and identify biomarkers of these quality traits.
represent the final result of a complex gene expression system where dif-
• Many protein biomarkers of beef tenderness have been high- ferent isoforms may exist although corresponding to a single gene because
lighted and are currently under validation on different muscle and of post transcriptional modifications. Moreover, proteins are thought to
animal types. Biomarkers of fish flesh firmness, and of many sen- be the main effector of some quality variables of great interest such as
sory (tenderness) and technological (drip loss and pale, soft, and firmness. The significant interest of proteomic approaches in the field of
exudative defect) pork quality traits, have also been identified. animal and meat science to improve knowledge on biological mechanisms
• Expected outcomes are to provide control tools of meat quality determining phenotypes and identify biomarkers of traits of interest has
evaluation usable in the livestock sector and meat industries in been highlighted in recent reviews (Hollung et al., 2007; Bendixen et al.,
the near future. 2011).
In this review we will focus on the recent proteomic studies conducted
in relation with meat quality determination, evaluation, and improvement,
Key words: biomarkers, sensory quality, skeletal muscle, technological in cattle, pig, and fish species by French INRA groups. In these three mod-
quality, texture els, proteomics has been used to study specific questions according to
each production sector.
Introduction
Thanks to the sequencing of genomes, it is now possible to decode and Beef Quality: From Biomarkers to
locate many thousands of genes in a genome. This available information Phenotyping Tools
can be used for purposes of knowledge, diagnosis, or selection. The de-
Although several biochemical factors are well known and a number
velopment of tools that accompanied this progress allows for the simulta-
of quantitative trait loci (QTL) have been determined, control of the vari-
neous analysis of thousands of genes (DNA chips), transcripts (transcrip-
ability in beef tenderness remains a major challenge for the beef industry.
tomics), and proteins (proteomics; Figure 1).
Beef tenderness presents a strong and uncontrolled variability that induces
The emergence of these functional genomic technologies enables the
a consumer’s dissatisfaction and partly explains the decrease in beef con-
measurement of complex phenotypes, such as traits related to the qual-
sumption. Moreover, this quality can be assessed only after slaughter by
ity of food products. Because meat quality traits result from genetic and
mechanical measurements such as the Warner-Bratzler test or by a sensory
environment interactions, working at the gene or protein expression lev-
analysis panel. There is no technique for measuring tenderness on the liv-
el allows scientists to take both the genetic potential of animals and its
ing animal. So, the beef industry is waiting for tools to estimate the poten-
modulation by the environment into account. Thus, biomarkers of gene
tial of tenderness from the live animal or carcass (Figure 2).
expression appear more accurate than genetic markers to better under-
The strategy developed over the past 10 years has been 1) to search
stand biological processes determining phenotypes, and explain and pre-
for biomarkers of tenderness by comparing extreme groups of animals on
dict meat quality variations (te Pas et al., 2011). The principle is to identify
this criterion with genomic tools; 2) to validate the relationships between
© Picard, Lefevre, and Lebret these markers and tenderness on large numbers of animals; 3) to precisely
doi:10.2527/af.2012-0058 define the influence of management factors on the expression of these

18 Animal Frontiers
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Figure 1. Different steps of proteomic analysis.

biomarkers; 4) to further analyze the biological functions involved in the

development of tenderness; and finally 5) to use this knowledge to build
tools used by industry to estimate the quality of an animal before or after
slaughter.

Use of Genomic Tools for Identifying Biomarkers of

Tenderness: Comparative Proteomics
Over the years, several proteomic analyses were performed in specific
programs to better understand the mechanisms involved in tenderness or
to provide biomarkers that can predict it. For that, the strategy has been
to compare extreme groups of beef tenderness by proteomics (Picard et
al., 2010, 2011) and/or transcriptomics (Bernard et al., 2007). For com-
parative proteomics, the proteins of muscles from two groups (very tender
and not tender) were extracted and separated according to their isoelectric
point by two-dimensional electrophoresis. The differences in spot vol-
umes were analyzed by image analysis. Then the protein corresponding
to the significant differential spots were identified by mass spectrometry
(Figure 1). These studies established a list of biological markers of beef
tenderness. The main results obtained in the Longissimus thoracis (LT)
have demonstrated that fast glycolytic type proteins were more abundant
in animals giving the less tender meat. Among these proteins, we iden-
tified: Phosphoglucomutase (PGM), lactate dehydrogenase B (LDHB),
and Triphosphate isomerase in Charolais and Salers, the glyceraldehyde-
3-phosphate dehydrogenase (GAPDH) in the Limousin, the fast troponin
T (TnTf) isoforms in Charolais and Blond d'Aquitaine, and the β Enolase
in Limousin and Blond d'Aquitaine breeds. Additional experiments led
to similar conclusions about the positive relationships between oxidative
metabolism and tenderness (Picard et al., 2010). Similar results have been
observed for pigs. For example, D’ Alessandro et al. (2011) reported PGM
was more abundant in the muscle of pigs that produced more tender meat.
Several proteins involved in calcium metabolism were also identified as
positive markers for tenderness. For example, the amount of Parvalbu-
min peptides is considerably increased in tender muscles of Charolais and
Limousin breeds. The calcium cycle proteins seem strongly involved in
meat tenderness, in connection with the important role of calcium in meat
ageing (Ouali et al., 2006). Accordingly, Bjarnadottir et al. (2012) recently
found a relationship between Annexin 6, involved in the release of cal-

October 2012, Vol. 2, No. 4 19

 extracts on a membrane (PVDF) and hy-
bridizing the membrane with an antibody
specific for the desired protein. Dot-Blot
was used on 111 samples from LT and
ST muscles from the Charolais bovine
breed to quantify 24 proteins previously
identified as biomarkers of tenderness by
comparative proteomics (Guillemin et
al., 2012). The main results showed that
biomarkers better discriminated tender-
ness (evaluated by sensory or mechani-
cal analysis) in ST than in LT muscle.
This could be the consequence of dif-
ferent compositions of these muscles in

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characteristics such as total lipid content
(higher in LT) or collagen content which
are also involved in tenderness. Multiple
regressions highlighted PRDX6 (cis-per-
oxiredox-6), LDHB (lactate dehydroge-
nase B), Hsp70-1B, Hsp70-GRP75 (Heat
Shock Protein), and MyHC (Myosin
Heavy Chain) II (IIa + IIx) as proteins
explicative of ST tenderness (WBSF;
R2=0,86). In LT muscle, PRDX6, Hsp20,
Figure 2. The beef industry is currently in need of a tool to estimate the tenderness
Hsp70-GRP75, and αB Crystallin (CRY-
of live cattle (source: Rick Harrison). AB) were the most explicative of tenderness (R2=0.69; Guillemin et al.,
2012). These predictive equations revealed that the PRDX6 protein is the
cium, and tenderness. A set of proteins of the family of heat shock proteins main biomarker explaining the WBSF in both muscles (P=0.003). This
(Hsp) was revealed as markers of tenderness at the transcript or protein enzyme is involved in the fight against oxidative stress which is caused by
level in the different experiments. For example, Bernard et al. (2007) have free radicals of oxygen, resulting in the formation of protein aggregates
shown that gene expression of the DNAJA1 protein (protein Hsp40) was that impair tenderness (Morzel et al., 2008). Proteins of small Hsp fam-
an appropriate indicator of meat toughness of Charolais young bulls. Ac- ily (Hsp27, Hsp20, and CRY-AB) are known to prevent the formation of
cording to the hypothesis of Ouali et al. (2006), the anti-apoptosis DNA- these aggregates. Thus, the positive relationship between these Hsp and
JA1 could slow down the process of cell death during the early stages tenderness is quite concordant with the negative relationship between oxi-
of transformation of muscle into meat. Other family members were also dative stress (PRDX6) and tenderness. We confirm that Hsp is important
identified as markers of tenderness in several programs (Hsp27, Hsp20, in tenderness determination, with Hsp70 as negative markers, in contrast
αB-crystallin, Hsp70). Proteins involved in oxidative stress, such as su- to Hsp20 (Guillemin et al., 2012). Indeed, Hsp70 also sequester pro-
peroxide dismutase (SOD1) or Peroredoxin 6 (PRDX6), were found to be apoptotic factors such as BCL-2 and inhibit apoptosis (Beere and Green,
negatively related to tenderness. This is in contradiction with the data of 2001). These proteins also have chaperone functions, but not on protein
D’ Alessandro et al. (2011), which shows that SOD1 was more abundant structure. This can explain why they are negative markers of tenderness
in pork that was more tender and apparently had more protein degrada- in ST muscle, in contrast to Hsp20. Indeed, Guillemin et al. (2012) have
tion. A similar study conducted on Semitendinosus (ST) muscle showed shown that the ratio of the family of small Hsps/the family of Hsps70 ap-
differences in the identified markers according to muscle type (Guillemin peared to explain variability of beef tenderness.
et al., 2012); breed-specificities for proteomic markers of tenderness were
also reported (Chaze et al., 2009). Influence of Management Factors on the
Expression of Biomarkers of Tenderness
Validation of Biomarkers: Our objective was to determine the precise effect breeding systems
Prediction of Tenderness have on the abundance of protein biomarkers. First, a thorough analysis of
the regulation of gene expression of DNAJA1 (coding protein Hsp40) was
Comparative analyzes to identify biomarkers were conducted primar- performed to show how its expression may vary according to muscle type
ily in young bulls of different breeds. Currently, we want to validate the and animal behavior. The main results showed that the greatest abundance
relationships between markers abundance and tenderness level over large of Hsp40 was observed in the youngest animal and the most oxidative
numbers of cattle in French systems with cows, heifers, steers, bulls or muscles. No effect was detected for dietary treatment (pasture vs. maize
beef, hardy breeds, and dairy breeds. In order to simultaneously analyze based diet) or growth path (compensatory growth after a restriction pe-
different biomarkers for several muscle samples, we developed the Dot- riod). Moreover, its abundance was not modified by pre-slaughter stress
Blot technique (Guillemin et al., 2009). It consists of depositing the protein (Cassar-Malek et al., 2011).

20 Animal Frontiers
 The effect of muscle type (LT vs. ST) and animal type (bulls vs. steers) studying their relationship with tenderness could complete our knowledge
on the abundance of a list of 24 proteins was studied in Charolais cattle on tenderness and help to better explain tenderness variability.
(67 young bulls and 44 steers). We detected muscle type effect on 14 of
the 24 analyzed proteins and an animal effect on 15 of the 24 proteins. The Development of Analytical Tools
main results showed that the family of small Hsp (27, 20, αB cristallin) From these data, the goal is to develop a routine application for the
varied according to these two factors. They are more abundant in young beef sector. The principle is the opposite approach of the Dot-Blot tech-
bulls than in steers and in LT than in ST muscle. On the contrary, Hsp70/ nique. It consists in depositing the interested antibodies on the membrane
GRP75 was more abundant in steers and showed no effect of muscle type. and hybridizing with the protein extract. This technology is called "anti-
Proteins of calcium dependent proteolysis (M and μ-calpains) were more body chip". This technology is already used for muscle proteins with med-
abundant in steers with no effect of muscle type. Contractile and meta- ical applications in disease diagnostics (Sakanyan, 2005). Our challenge
bolic proteins were more variable according to muscle than animal type is to develop this technology for phenotyping bovine for tenderness. The
(Guillemin et al., 2011a). This approach is being completed for various advantages are that it is a fast, high-sensitive immunological technique
biomarkers and management factors. Altogether, this data will help pro- that enables the simultaneous quantification of several proteins in samples
vide advice on farming practices that could allow for optimal expression

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obtained by biopsy live animals or carcasses. The expected outcomes are
of tenderness biomarkers. to provide the beef sector with a tool for “paddock” use to estimate the
tenderness potential of a live animal or a meat cut. If we succeed in this
Biological Functions Governing Beef Tenderness challenge, this tool will improve the competitiveness of this industry by
From the list of 24 proteins, we used bioinformatic tools to search for allowing it to provide the consumers with controlled quality beef.
proteins interacting with other proteins identified as markers of tender-
ness (Guillemin et al., 2011b). This work highlighted cellular pathways
Pig Meat Quality: Understanding the
strongly involved in the tenderization processes: apoptosis, Hsp functions,
and oxidative stress resistance. We also demonstrated that the role of these Development and Identifying Biomarkers of
pathways on the tenderization process differs according to muscle type. Complex Phenotypic Traits
Moreover, this analysis revealed new data. For example, three proteins,
Pork is the predominant meat consumed in the world (Figure 3), ei-
never studied in tenderness, appeared to be at a crossroad of the tender-
ther as fresh meat or processed products, exhibiting a great diversity in
ness interactome: SUMO4, H2AFX, and TP53. Direct relationships with
tenderness is improbable. However, these proteins could be responsible Figure 3. Pork at Palua Tikus Market in the coastal town of Penang, Malaysia
for the balance between pathways, like apoptosis or stress response. So, (source: flickr.com/shebalso).

October 2012, Vol. 2, No. 4 21

both the type of raw material (entire parts [hams] or minced meat [sau- like small Hsp. In addition to the quantification of protein expression,
sages]) and processing techniques used (cooking or dry-curing). There- proteomics has been used recently to quantify protein phosphorylation
fore, pork quality covers technological and sensory dimensions, including changes in p.m. porcine muscle in relation with pork quality. Huang et al.
many traits like post-mortem (p.m.) pH, drip loss, color, intramuscular (2011) reported that fast pH decline muscles exhibited the greatest phos-
fat (IMF) content, tenderness, juiciness, and flavor. These pork quality phorylation level (1 hour p.m.) and the least (24 hours p.m.), whereas
traits result from interactions between genetic backgrounds, rearing and slow pH muscles showed the reverse case. Studying another important
slaughtering conditions of animals, and meat processing. Even though defect of pork, the acid meat resulting from Rendement Napole- (RN-)
many factors influencing pork quality have been identified, its variability genotype, Lametsch et al. (2011) reported greater phosphorylation levels
remains high and muscle properties underlying good eating quality are of key enzymes of glycogenolysis and glycolysis during p.m. metabolism
still unclear. Thus, like for other animal species, identifying markers of in RN- compared with wild-type pigs. This illustrates that proteomic ap-
quality traits is of significant interest in the pork industry. As a result, proaches are relevant to characterize post-translational modifications of
applications of proteomic approaches is increasing, generally based on proteins, like phosphorylation levels that could be interpreted as meta-
two-dimensional electrophoresis and mass spectrometry for protein iden- bolic fingerprints related to biological processes determining phenotypic
tification, in order to improve knowledge on biological mechanisms de- traits such as meat quality.

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termining pork quality and identifying biomarkers of phenotypes. Studies Aimed at understanding the development of pork tenderness and iden-
consider either one important quality trait (e.g., IMF, color, shear force) tifying potential markers, Laville et al. (2007) compared two contrasted
in a differential animal design for a given trait, or many traits simultane- groups for LM WBSF of cooked meat. They showed that low WBSF
ously (e.g., technological and sensory traits) using an experimental design group (i.e. tender meat) exhibited an overabundance of proteins of lipid
leading to a range of variation for these traits. Most of the work concerns metabolism, including adipocyte-fatty acid binding protein (FABP4), thus
the Longissimus (LM), but the Semimembranosus (SM, ham muscle) has suggesting greater number of intramuscular adipocytes in these muscles.
also been considered in relationships with the importance of cooked and A greater FABP4 protein level was associated with greater IMF content
dry-cured hams production. in agreement with Damon et al. (2006), and could explain the increased
tenderness. Laville et al. (2007) also reported a greater abundance of pro-
Differential Proteomic Profiles Associated to teins involved in folding and polymerization, indicating increased protein
Contrasted Levels for Quality Traits synthesis in low WBSF group.
Traits related to both technological and sensory qualities of pork [i.e.,
Associations between Proteomic Profiles and
IMF content; pale, soft, and exudative (PSE) meat defect; or shear force]
have been studied using comparative proteomics approaches to improve Variations in Technological or Sensory Traits for
biological knowledge and identify potential biomarkers. Identification of Biomarkers
The IMF content is an important component of pork quality, and is Experimental designs are aimed at associating between, or within,
highly variable among pig populations. To better understand its biological breed or rearing condition variations in pork quality and the muscle pro-
determinism and thereby help the design of genetic schemes for increas- teomic profile in order to understand underlying biological processes and
ing IMF, contrasted groups for LM IMF content (1.36 vs. 4.58%) were identify biomarkers of quality. In an experiment associating two contrast-
compared by proteomic analyses (Liu et al., 2009). The expression of ed pure breeds (local Basque, corresponding to premium quality prod-
proteins of glucose and protein metabolic processes, cell communication, ucts, and conventional Large White) reared in various production systems
metabolites binding, and the response to stimulus functional categories (conventional, alternative, or extensive), associations between biochemi-
were associated with IMF variation. Associated to transcriptomic data ob- cal, physico-chemical, and sensory traits, and transcriptomic and pro-
tained on the same animals at similar and earlier age, these results indicate teomic profiles of LM revealed biological mechanisms and metabolites,
that variability in pig IMF content might arise essentially from differences transcripts, and proteins associated to the variations of many pork traits
in early adipogenesis and adipocyte development, thereby revealing bio- (Salmi et al., 2010; Lebret and Damon, 2011; Damon et al., 2012). As an
logical processes to be considered for further studies on IMF control. example, sarcoplasmic proteome analyses revealed that protein oxidation
Pale, soft, and exudative meat, a major problem regarding pork qual- generated during meat ageing and cooking, which might impair tender-
ity, actually corresponds to various defects depending on both genetic and ness, water holding capacity, and technological properties of raw meat,
non-genetic factors, and originates from various physiological and bio- relied on proteins involved in antioxidant protection (selenium binding
chemical mechanisms. In the SM, PSE zones result in low cohesiveness protein and mitochondrial superoxide dismutase; SOD) and on iron con-
of meat that becomes unsuitable for cooked ham production, leading to taining proteins (myoglobin isoforms and serotransferrin; Promeyrat et
important problems in pork industry. Using proteomic analyses, Laville al., 2011). Proteins of antioxidant pathways were negatively associated
et al. (2005) showed a decrease in protein solubility and p.m. proteolysis with drip and cooking losses and positively associated with tenderness,
of myofibrillar proteins, and lower quantities of small Hsp (Hsp 27, CRY- whereas opposite associations were found between proteins of energy
AB) in the PSE zones compared with normal SM. The reduced protein metabolism and these traits (Sayd et al., 2009). In agreement, greater
solubility and abundance of Hsp 27 and proteins of oxidative metabolism levels of antioxidant enzymes such as SOD1 were found in tender meat
were also observed in the SM of pigs of nn genotype at the RyR1 locus from Casertana pigs compared with tougher meat from Large White pigs
(halothane gene) that leads to the genetic PSE defect, compared with NN (D’Alessandro et al., 2011). Combining proteomics and transcriptomics
pigs (Laville et al., 2009), as well as in pigs exhibiting pale vs. dark color results, these authors hypothesized that antioxidant enzymes could play a
in the SM (61.3 vs. 43.2 L* value; Sayd et al., 2006). These studies open role in protecting the proteolytic enzymes cathepsines and calpains during
the way to markers of PSE defect by quantification of chaperones proteins

22 Animal Frontiers
p.m. proteolysis, thereby enhancing meat tenderization in Casertana pigs. nutritional quality. Nevertheless, amongst sensory quality, flesh texture
In addition to studies performed on samples taken early p.m., proteome is mainly determined by biological factors such as muscle organization,
degradation during meat ageing in relation with technological and sensory protein content, and composition. In fish, the best quality is firm and co-
pork quality traits has also been investigated by proteomics approaches hesive flesh with good water holding capacity. These traits are mainly
(Lametsch et al., 2002; te Pas et al., 2009). Post-mortem proteolysis of determined by proteins’ nature and properties, so proteomic tools appear
actin and metabolic enzymes has thus been demonstrated (Lametsch et al., especially of interest to study fish flesh quality. However, very few studies
2002), providing new insights on the biochemical phenomena occurring were undertaken to identify flesh quality biomarkers, probably due to the
during meat ageing and tenderization. Altogether, these results improve small number of research teams working in that topic.
knowledge on pork quality variation and the protein targets identified can
be considered for further development of biomarkers of quality. However, Post-mortem Changes
validation of potential markers for use in various breeds or pork chains The first studies analyzed muscle proteome p.m. changes in relation
may be a difficult task. When associating LM protein abundance and pork to flesh softening. Cod muscle proteome observed in 2D-PAGE during 8
quality variations using multiple regressions analyses, Kwasiborski et al. days p.m. revealed a limited degradation compared to mammal muscles,
(2008) found that the abundance of 1 or 2 proteins could explain up to

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with 9 spots in which intensity increased and 2 spots in which intensity
85% of variability of traits like ultimate pH (muscular creatine kinase and decreased (Kjaersgard and Jessen, 2003). In this study, protein identifica-
dimericdihydrodiol dehydrogenase, 83%), drip loss (pyruvate kinase iso- tion was not reported and very little genomic data are available illustrating
form M1, 65%), or thawing loss (actin interactin protein, 85%). Never- the limitations of proteomic approaches for species in which the genome
theless, protein-trait associations displayed significant gender and breed was not sequenced. More recently, the evolution of rainbow trout muscle
differences, indicating that the identification of ‘robust’ (i.e., generic) protein was studied during 5 days p.m. by sodium dodecyl sulfate poly-
proteomic markers of pork traits for wide use in pork industries deserves acrylamide gel electrophoresis (SDS-PAGE), and gel band intensity was
further research. found to be related to flesh firmness. Proteins from both myofibrillar [i.e.,
α-actinin, actin, Myosin Light Chain (MyLC) 1 and 2, MyHC fragment]
Fish Quality: Towards a Better Understanding of and sarcoplasmic (creatine kinase, glycogen phosphorylase, triose phos-
Flesh Texture phate isomerase) fractions closely correlated with firmness (i.e., Godiksen
et al., 2009). In these cases, proteomic approaches allowed scientists to
In fish, flesh quality is dependent on environmental factors, mainly explore new targets of post-mortem proteolysis and to study the possible
water and food quality for product safety and food composition for flesh implications of the different proteolytic systems in flesh quality.

Figure 4. A rainbow trout harvest. Only 15 min of crowding stress of rainbow trout can lead to increased flesh firmness (source: flickr.com/spikefi/).

October 2012, Vol. 2, No. 4 23

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24 Animal Frontiers
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Sustainable and diversified pork chains: From science to practice, Palma de
Dr. Brigitte Picard is a meat scientist. She
Mallorca, Spain. http://www.q-porkchains.org/news/Conference/conference/
obtained a Ph.D. degree in biochemistry
programme/presentations.aspx. Accessed June 19, 2012.
in 1990 and is currently developing re-
Lefèvre, F., J. Bugeon, B. Auperin, and J. Aubin. 2008. Rearing oxygen level and search on muscle growth and cattle meat
slaughter stress effects on rainbow trout flesh quality. Aquaculture 284:81–89. quality. She is the head of an INRA team
Lefèvre F., G. Paboeuf, T.G. Pottinger, and J. Bugeon. 2010. Sélection génétique of 26 people with currently six thesis and
sur la réponse au stress et stress à l’abattage: Conséquences sur le protéome two post-doc students. She manages pro-
musculaire et lien avec la qualité de la chair chez la truite Arc-en-ciel. Pages grams on markers of beef tenderness (bio-
225–226 in Numéro spécial Viande et Produits Carnés. 13èmes Journées des logical integrative approach associating
Sciences du Muscle et Technologies des Viandes. Clermont-Ferrand, France. biochemical studies, functional genomics
Liu, J., M. Damon, N. Guitton, I. Guisle, P. Ecolan, A. Vincent, P. Cherel, and F. [proteomics] and modelling). Her compe-
Gondret. 2009. Differentially-expressed genes in pig Longissimus muscles with tences are: muscle physiology, analysis of
contrasting levels of fat, as identified by combined transcriptomic, reverse tran- proteins (electrophoresis mono and two-
scription PCR, and proteomic analyses. J. Agric. Food Chem. 57:3808–3817. dimensional, western-blot, ELISA, and immunohistochemistry), primary
Morzel, M., C. Chambon, F. Lefèvre, G. Paboeuf, and E. Laville. 2006. Modifica- cultures of muscle cells (myoblasts and satellite cells), and the proteomic
tions of trout (Oncorhynchus mykiss) muscle proteins by preslaughter activity. analysis of muscle.
J. Agric. Food Chem. 54:2997–3001. Correspondence: brigitte.picard@clermont.inra.fr
Morzel, M., C. Terlouw, C. Chambon, D. Micol, and B. Picard. 2008. Muscle pro-
Dr. Bénédicte Lebret is a meat scien-
teome and meat eating qualities of Longissimus thoracis of "Blonde d'Aquitaine"
tist. She has Ph.D. degree in biology and
young bulls: A central role of HSP27 isoforms. Meat Sci. 78:297–304.
agronomy. Her main research topics are
Ouali, A., C. H. Herrera-Mendez, G. Coulis, S. Becila, A. Boudjellal, L. Aubry, and the determination of technological and
M.A. Sentandreu. 2006. Revisiting the conversion of muscle into meat and the sensory quality of pork with a special em-
underlying mechanisms. Meat Sci. 74:44–58. phasis on production systems and geno-
Picard, B., C. Berri, L. Lefaucheur, C. Molette, T. Sayd, and C. Terlouw. 2010. type effects on these traits. Her skills are in
Skeletal muscle proteomics in livestock production. Briefings Funct. Genomics animal (pig) science, muscle biochemistry,
Proteomics 9:259–278. and meat science. She has been head of the
Picard, B., I. Cassar-Malek, N. Guillemin, and M. Bonnet. 2011. Animal systems Research Group Growth and Meat Quality
quest for novel muscle pathway biomarkers by proteomics in beef production. of INRA-UMR PEGASE (15 permanent
Pages 395–405 in Comprehensive Biotechnology. 2nd ed. V. 4. M. Moo-Young, staff; Ph.D.'s and post-docs) for 10 years.
ed. Elsevier, Amsterdam, Netherlands. She manages research programs on the
Promeyrat, A., T. Sayd, E. Laville, C. Chambon, B. Lebret, and P. Gatellier. 2011. influence of production systems on pork
Early post-mortem sarcoplasmic proteome of porcine muscle related to protein quality and on identification of biomarkers
oxidation. Food Chem. 127:1097–1104. of pork quality and is supervisor of Ph.D.
and post-doc students.
Sakanyan, V. 2005. High-throughput and multiplexed protein array technology:
Protein-DNA and protein-protein interactions. J. Chromatogr., B 815:77–95.
Dr. Florence Lefèvre is a fish flesh qual-
Salmi, B., C. Larzul, M. Damon, L. Lefaucheur, J. Mourot, E. Laville, P. Gatellier, ity scientist. She obtained her Ph.D. de-
K. Méteau, D. Laloë, and B. Lebret. 2010. Multivariate analysis to compare pig gree in food science in 1997. She works
meat quality traits according to breed and rearing system. ID442 in Proceedings in the INRA Fish Physiology and Genom-
of the 9th World Congress Genetics Applied to Livestock Production, Leipzig, ics Laboratory, more precisely in the Fish
Germany. Growth and Flesh Quality Group. She is
Sayd T., M. Morzel, C. Chambon, M. Franck, P. Figwer, C. Larzul, P. Le Roy, G. involved in research programs aimed to
Monin, P. Chérel, and E. Laville. 2006. Proteome analysis of the sarcoplasmic understand the determinants of fish flesh
fraction of pig semimembranosus muscle: implications on meat color develop- quality, especially the role of muscle struc-
ment. J. Agric. Food Chem. 54:2732–2737. ture and nature of proteins in trout muscle
Sayd T., E. Laville, S. Blinet, J. Pinguet, B. Lebret, M. San Cristobal. 2009. Use of texture.
sparse PLS method for the integration of proteomic and phenotypic data related

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