|Updike, M. Scott|
|Liu, Ge - George|
|Baldwin, Ransom - Randy|
Submitted to: Livestock Science
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 11/30/2013
Publication Date: 12/16/2013
Citation: Zhao, C., Zan, L., Wang, Y., Updike, M., Liu, G., Bequette, B.J., Baldwin, R.L., Song, J. 2013. Functional proteomic and interactome analysis of proteins associated with beef tenderness in angus cattle. Livestock Science. 161:201-209. Interpretive Summary: Beef is a source of high-quality protein for the human population, and beef tenderness has a significant influence on beef palatability, consumer expectation, and industry profitability. To further characterize factors affecting beef tenderness, functional proteomics and bioinformatics interactome analysis were performed on longissimus dorsi (LD) muscle of Angus cattle. Eight proteins were identified from this study which had meaningful interactions with the level of tenderness of the beef. These proteins are involved with carbohydrate metabolism, as well as protein breakdown and response to stress. Because tenderness is such an important part of beef sales, the results of this study provide important information for the development of new methods to ensure beef tenderness in production systems.
Technical Abstract: Beef is a source of high quality protein for the human population, and beef tenderness has significant influence on beef palatability, consumer expectation and industry profitability. To further elucidate the factors affecting beef tenderness, functional proteomics and bioinformatics interactome analysis were performed on longissimus dorsi (LD) tissue from Angus cattle. Proteins were analyzed by SDS-PAGE and linearly regressed against Warner-Bratzler shear forces (WBSF). Seventeen electrophoretic bands were revealed to be correlated with beef tenderness. Two of the bands with the most significant correlations were selected and submitted to LCMS/MS for analysis. Eight proteins, beta-enolase (ENOB), L-lactate dehydrogenase A chain (LDHA), glyceraldehyde-3-phosphate dehydrogenase (G3P), carbonic anhydrase 3 (CAH3), phosphoglycerate mutase 2 (PGAM2), peroxiredoxin-6 (PRDX6), myosin heavy chain 1 (MYH1) and myosin heavy chain 7 (MYH7), were identified from these two bands. Interactions of these 8 protein markers were constructed using Cytoscape and further functional annotation analysis showed these proteins of the interactome were enriched in metabolic pathways, such as carbohydrate metabolic and catabolic processes, apoptosis, peptidase activity and response to stress. The results of this study provide a novel insight into the interaction of proteins functionally correlated with beef tenderness.