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Proteome changes underpin improved meat quality and yield of chickens (Gallus gallus) fed the probiotic Enterococcus faecium.

Zheng A, Luo J, Meng K, Li J, Zhang S, Li K, Liu G, Cai H, Bryden WL, Yao B - BMC Genomics (2014)

Bottom Line: The probiotic significantly increased meat colour, water holding capacity and pH of pectoral muscle but decreased abdominal fat content.The validity of the proteomics results was further confirmed by qPCR.This study reveals that improved meat quality of broilers fed probiotics is triggered by proteome alterations (especially the glycolytic proteins), and provides a new insight into the mechanism by which probiotics improve poultry production.

View Article: PubMed Central - PubMed

Affiliation: Key Laboratory of Feed Biotechnology of Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, P, R, China. liuguohua@caas.cn.

ABSTRACT

Background: Supplementation of broiler chicken diets with probiotics may improve carcass characteristics and meat quality. However, the underlying molecular mechanism remains unclear. In the present study, 2D-DIGE-based proteomics was employed to investigate the proteome changes associated with improved carcass traits and meat quality of Arbor Acres broilers (Gallus gallus) fed the probiotic Enterococcus faecium.

Results: The probiotic significantly increased meat colour, water holding capacity and pH of pectoral muscle but decreased abdominal fat content. These meat quality changes were related to the altered abundance of 22 proteins in the pectoral muscle following E. faecium feeding. Of these, 17 proteins have central roles in regulating meat quality due to their biological interaction network. Altered cytoskeletal and chaperon protein expression also contribute to improved water holding capacity and colour of meat, which suggests that upregulation of chaperon proteins maintains cell integrity and prevents moisture loss by enhancing folding and recovery of the membrane and cytoskeletal proteins. The down-regulation of β-enolase and pyruvate kinase muscle isozymes suggests roles in increasing the pH of meat by decreasing the production of lactic acid. The validity of the proteomics results was further confirmed by qPCR.

Conclusions: This study reveals that improved meat quality of broilers fed probiotics is triggered by proteome alterations (especially the glycolytic proteins), and provides a new insight into the mechanism by which probiotics improve poultry production.

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Related in: MedlinePlus

Biological interaction network of the proteins of differential abundance from the pectoral muscles of 42-day-old AA broilers fed dietaryE. faecium. Lines between proteins indicate evidence of association. Red indicates fusion, green indicates neighborhood, blue indicates co-occurrence, purple indicates experimental evidence, yellow indicates text-mining evidence, light blue indicates database evidence, and black indicates coexpression. MYH1, myosin, heavy chain 1; MYH3, myosin-3; MYH15, myosin heavy chain 15; SSMHC, myosin, heavy chain 7B, beta; ACTN2, α-actinin-2; TTN, structural muscle protein titin; SM1, slow myosin heavy chain 1; PGM1, phosphoglucomutase-1; LDHA, L-lactate dehydrogenase A chain; CKMT2, mitochondrial creatine kinase; FBP2, fructose-1,6-bisphosphatase 2; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; PGK, phosphoglycerate kinase; PGAM1, phosphoglycerate mutase 1; PKM2, pyruvate kinase muscle isozyme; HSP70, heat shock 70 kDa protein; and ALB, albumin.
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Fig7: Biological interaction network of the proteins of differential abundance from the pectoral muscles of 42-day-old AA broilers fed dietaryE. faecium. Lines between proteins indicate evidence of association. Red indicates fusion, green indicates neighborhood, blue indicates co-occurrence, purple indicates experimental evidence, yellow indicates text-mining evidence, light blue indicates database evidence, and black indicates coexpression. MYH1, myosin, heavy chain 1; MYH3, myosin-3; MYH15, myosin heavy chain 15; SSMHC, myosin, heavy chain 7B, beta; ACTN2, α-actinin-2; TTN, structural muscle protein titin; SM1, slow myosin heavy chain 1; PGM1, phosphoglucomutase-1; LDHA, L-lactate dehydrogenase A chain; CKMT2, mitochondrial creatine kinase; FBP2, fructose-1,6-bisphosphatase 2; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; PGK, phosphoglycerate kinase; PGAM1, phosphoglycerate mutase 1; PKM2, pyruvate kinase muscle isozyme; HSP70, heat shock 70 kDa protein; and ALB, albumin.

Mentions: Protein networks may provide insights into the biological process involving several proteins. Using the online tools of STRING 9.1, 17 proteins acted as key nodes with various relationships in biological interaction networks (BIN) (Figure 7). Eight proteins (47.1%) were related to carbohydrate and energy metabolism, seven to cytoskeleton, one to chaperone and one to transporter. The results indicate that four main clusters could be individuated in the interaction map and summarized into significant interactions with the other proteins in the map. Of these, PKM2, GAPDH, PGK, LDHA and PGAM1 were the highest degree nodes.Table 3


Proteome changes underpin improved meat quality and yield of chickens (Gallus gallus) fed the probiotic Enterococcus faecium.

Zheng A, Luo J, Meng K, Li J, Zhang S, Li K, Liu G, Cai H, Bryden WL, Yao B - BMC Genomics (2014)

Biological interaction network of the proteins of differential abundance from the pectoral muscles of 42-day-old AA broilers fed dietaryE. faecium. Lines between proteins indicate evidence of association. Red indicates fusion, green indicates neighborhood, blue indicates co-occurrence, purple indicates experimental evidence, yellow indicates text-mining evidence, light blue indicates database evidence, and black indicates coexpression. MYH1, myosin, heavy chain 1; MYH3, myosin-3; MYH15, myosin heavy chain 15; SSMHC, myosin, heavy chain 7B, beta; ACTN2, α-actinin-2; TTN, structural muscle protein titin; SM1, slow myosin heavy chain 1; PGM1, phosphoglucomutase-1; LDHA, L-lactate dehydrogenase A chain; CKMT2, mitochondrial creatine kinase; FBP2, fructose-1,6-bisphosphatase 2; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; PGK, phosphoglycerate kinase; PGAM1, phosphoglycerate mutase 1; PKM2, pyruvate kinase muscle isozyme; HSP70, heat shock 70 kDa protein; and ALB, albumin.
© Copyright Policy - open-access
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4325948&req=5

Fig7: Biological interaction network of the proteins of differential abundance from the pectoral muscles of 42-day-old AA broilers fed dietaryE. faecium. Lines between proteins indicate evidence of association. Red indicates fusion, green indicates neighborhood, blue indicates co-occurrence, purple indicates experimental evidence, yellow indicates text-mining evidence, light blue indicates database evidence, and black indicates coexpression. MYH1, myosin, heavy chain 1; MYH3, myosin-3; MYH15, myosin heavy chain 15; SSMHC, myosin, heavy chain 7B, beta; ACTN2, α-actinin-2; TTN, structural muscle protein titin; SM1, slow myosin heavy chain 1; PGM1, phosphoglucomutase-1; LDHA, L-lactate dehydrogenase A chain; CKMT2, mitochondrial creatine kinase; FBP2, fructose-1,6-bisphosphatase 2; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; PGK, phosphoglycerate kinase; PGAM1, phosphoglycerate mutase 1; PKM2, pyruvate kinase muscle isozyme; HSP70, heat shock 70 kDa protein; and ALB, albumin.
Mentions: Protein networks may provide insights into the biological process involving several proteins. Using the online tools of STRING 9.1, 17 proteins acted as key nodes with various relationships in biological interaction networks (BIN) (Figure 7). Eight proteins (47.1%) were related to carbohydrate and energy metabolism, seven to cytoskeleton, one to chaperone and one to transporter. The results indicate that four main clusters could be individuated in the interaction map and summarized into significant interactions with the other proteins in the map. Of these, PKM2, GAPDH, PGK, LDHA and PGAM1 were the highest degree nodes.Table 3

Bottom Line: The probiotic significantly increased meat colour, water holding capacity and pH of pectoral muscle but decreased abdominal fat content.The validity of the proteomics results was further confirmed by qPCR.This study reveals that improved meat quality of broilers fed probiotics is triggered by proteome alterations (especially the glycolytic proteins), and provides a new insight into the mechanism by which probiotics improve poultry production.

View Article: PubMed Central - PubMed

Affiliation: Key Laboratory of Feed Biotechnology of Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, P, R, China. liuguohua@caas.cn.

ABSTRACT

Background: Supplementation of broiler chicken diets with probiotics may improve carcass characteristics and meat quality. However, the underlying molecular mechanism remains unclear. In the present study, 2D-DIGE-based proteomics was employed to investigate the proteome changes associated with improved carcass traits and meat quality of Arbor Acres broilers (Gallus gallus) fed the probiotic Enterococcus faecium.

Results: The probiotic significantly increased meat colour, water holding capacity and pH of pectoral muscle but decreased abdominal fat content. These meat quality changes were related to the altered abundance of 22 proteins in the pectoral muscle following E. faecium feeding. Of these, 17 proteins have central roles in regulating meat quality due to their biological interaction network. Altered cytoskeletal and chaperon protein expression also contribute to improved water holding capacity and colour of meat, which suggests that upregulation of chaperon proteins maintains cell integrity and prevents moisture loss by enhancing folding and recovery of the membrane and cytoskeletal proteins. The down-regulation of β-enolase and pyruvate kinase muscle isozymes suggests roles in increasing the pH of meat by decreasing the production of lactic acid. The validity of the proteomics results was further confirmed by qPCR.

Conclusions: This study reveals that improved meat quality of broilers fed probiotics is triggered by proteome alterations (especially the glycolytic proteins), and provides a new insight into the mechanism by which probiotics improve poultry production.

Show MeSH
Related in: MedlinePlus