Dietary ractopamine influences sarcoplasmic proteome profile of pork Longissimus thoracis

Bruno R.C. Costa-Lima; Surendranath P. Suman; Shuting Li; Carol M. Beach; Teofilo J.P. Silva; Expedito T.F. Silveira; Benjamin M. Bohrer; Dustin D. Boler

doi:10.1016/j.meatsci.2014.12.008

Dietary ractopamine influences sarcoplasmic proteome profile of pork Longissimus thoracis

Bruno R.C. Costa-Lima, Surendranath P. Suman, Shuting Li, Carol M. Beach, Teofilo J.P. Silva, Expedito T.F. Silveira, Benjamin M. Bohrer, Dustin D. Boler

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

Abstract

Dietary ractopamine improves pork leanness, whereas its effect on sarcoplasmic proteome has not been characterized. Therefore, the influence of ractopamine on sarcoplasmic proteome of post-mortem pork Longissimus thoracis muscle was examined. Longissimus thoracis samples were collected from carcasses (24. h post-mortem) of purebred Berkshire barrows (n = 9) managed in mixed-sex pens and fed finishing diets containing ractopamine (RAC; 7.4. mg/kg for 14. days followed by 10.0. mg/kg for 14. days) or without ractopamine for 28. days (CON). Sarcoplasmic proteome was analyzed using two-dimensional electrophoresis and mass spectrometry. Nine protein spots were differentially abundant between RAC and CON groups. Glyceraldehyde-3-phosphate dehydrogenase and phosphoglucomutase-1 were over-abundant in CON, whereas serum albumin, carbonic anhydrase 3, l-lactate dehydrogenase A chain, fructose-bisphosphate aldolase A, and myosin light chain 1/3 were over-abundant in RAC. These results suggest that ractopamine influences the abundance of enzymes involved in glycolytic metabolism, and the differential abundance of glycolytic enzymes could potentially influence the conversion of muscle to meat.

Original language	English
Pages (from-to)	7-12
Number of pages	6
Journal	Meat Science
Volume	103
DOIs	https://doi.org/10.1016/j.meatsci.2014.12.008
State	Published - May 1 2015

Bibliographical note

Publisher Copyright:
© 2014 Elsevier Ltd.

Funding

This work was supported by funds from the Kentucky Agricultural Experiment Station, University of Kentucky . Mass spectrometric analysis was performed at the University of Kentucky's Proteomics Core Facility, supported in part by funds from the Office of the Vice President for Research. The authors thank the Coordination for the Improvement of Higher Level Personnel (CAPES, Brazil) for providing the PDSE scholarship (BEX 0129-12-7) to Bruno Costa-Lima for completing doctoral research at the University of Kentucky.

Funders	Funder number
Coordination for the Improvement of Higher Level Personnel	BEX 0129-12-7
University of Kentucky
Kentucky Agricultural Experiment Station
Office of the Executive Vice President for Research and Partnerships, Purdue University

Keywords

Glycolysis
Longissimus thoracis
Ractopamine
Sarcoplasmic proteome

ASJC Scopus subject areas

Food Science

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10.1016/j.meatsci.2014.12.008

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title = "Dietary ractopamine influences sarcoplasmic proteome profile of pork Longissimus thoracis",

abstract = "Dietary ractopamine improves pork leanness, whereas its effect on sarcoplasmic proteome has not been characterized. Therefore, the influence of ractopamine on sarcoplasmic proteome of post-mortem pork Longissimus thoracis muscle was examined. Longissimus thoracis samples were collected from carcasses (24. h post-mortem) of purebred Berkshire barrows (n = 9) managed in mixed-sex pens and fed finishing diets containing ractopamine (RAC; 7.4. mg/kg for 14. days followed by 10.0. mg/kg for 14. days) or without ractopamine for 28. days (CON). Sarcoplasmic proteome was analyzed using two-dimensional electrophoresis and mass spectrometry. Nine protein spots were differentially abundant between RAC and CON groups. Glyceraldehyde-3-phosphate dehydrogenase and phosphoglucomutase-1 were over-abundant in CON, whereas serum albumin, carbonic anhydrase 3, l-lactate dehydrogenase A chain, fructose-bisphosphate aldolase A, and myosin light chain 1/3 were over-abundant in RAC. These results suggest that ractopamine influences the abundance of enzymes involved in glycolytic metabolism, and the differential abundance of glycolytic enzymes could potentially influence the conversion of muscle to meat.",

keywords = "Glycolysis, Longissimus thoracis, Ractopamine, Sarcoplasmic proteome",

author = "Costa-Lima, {Bruno R.C.} and Suman, {Surendranath P.} and Shuting Li and Beach, {Carol M.} and Silva, {Teofilo J.P.} and Silveira, {Expedito T.F.} and Bohrer, {Benjamin M.} and Boler, {Dustin D.}",

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doi = "10.1016/j.meatsci.2014.12.008",

language = "English",

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AU - Costa-Lima, Bruno R.C.

AU - Suman, Surendranath P.

AU - Li, Shuting

AU - Beach, Carol M.

AU - Silva, Teofilo J.P.

AU - Silveira, Expedito T.F.

AU - Bohrer, Benjamin M.

AU - Boler, Dustin D.

PY - 2015/5/1

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N2 - Dietary ractopamine improves pork leanness, whereas its effect on sarcoplasmic proteome has not been characterized. Therefore, the influence of ractopamine on sarcoplasmic proteome of post-mortem pork Longissimus thoracis muscle was examined. Longissimus thoracis samples were collected from carcasses (24. h post-mortem) of purebred Berkshire barrows (n = 9) managed in mixed-sex pens and fed finishing diets containing ractopamine (RAC; 7.4. mg/kg for 14. days followed by 10.0. mg/kg for 14. days) or without ractopamine for 28. days (CON). Sarcoplasmic proteome was analyzed using two-dimensional electrophoresis and mass spectrometry. Nine protein spots were differentially abundant between RAC and CON groups. Glyceraldehyde-3-phosphate dehydrogenase and phosphoglucomutase-1 were over-abundant in CON, whereas serum albumin, carbonic anhydrase 3, l-lactate dehydrogenase A chain, fructose-bisphosphate aldolase A, and myosin light chain 1/3 were over-abundant in RAC. These results suggest that ractopamine influences the abundance of enzymes involved in glycolytic metabolism, and the differential abundance of glycolytic enzymes could potentially influence the conversion of muscle to meat.

AB - Dietary ractopamine improves pork leanness, whereas its effect on sarcoplasmic proteome has not been characterized. Therefore, the influence of ractopamine on sarcoplasmic proteome of post-mortem pork Longissimus thoracis muscle was examined. Longissimus thoracis samples were collected from carcasses (24. h post-mortem) of purebred Berkshire barrows (n = 9) managed in mixed-sex pens and fed finishing diets containing ractopamine (RAC; 7.4. mg/kg for 14. days followed by 10.0. mg/kg for 14. days) or without ractopamine for 28. days (CON). Sarcoplasmic proteome was analyzed using two-dimensional electrophoresis and mass spectrometry. Nine protein spots were differentially abundant between RAC and CON groups. Glyceraldehyde-3-phosphate dehydrogenase and phosphoglucomutase-1 were over-abundant in CON, whereas serum albumin, carbonic anhydrase 3, l-lactate dehydrogenase A chain, fructose-bisphosphate aldolase A, and myosin light chain 1/3 were over-abundant in RAC. These results suggest that ractopamine influences the abundance of enzymes involved in glycolytic metabolism, and the differential abundance of glycolytic enzymes could potentially influence the conversion of muscle to meat.

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KW - Ractopamine

KW - Sarcoplasmic proteome

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Dietary ractopamine influences sarcoplasmic proteome profile of pork Longissimus thoracis

Abstract

Bibliographical note

Funding

Keywords

ASJC Scopus subject areas

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