Love me tender: an Omics window on the bovine meat tenderness network

J Proteomics. 2012 Jul 19;75(14):4360-80. doi: 10.1016/j.jprot.2012.02.013. Epub 2012 Feb 21.


Meat tenderness prediction is a challenging task, especially in Maremmana, an Italian autochtonous and highly appreciated beef breed. In the present study we reported an integrated proteomics, phosphoproteomics and metabolomics overview of meat tenderness in longissimus dorsi from 15 male Maremmana individuals, through the discrimination of tender and tough groups via standard meat tenderness indicators (WBS, MFI(4 h), MFI(10 days), sarcomere length) and their correlation with results from Omics analyses. Results revealed that the tender meat group was characterized by higher levels of glycolytic enzymes, which were less phosphorylated and overall more active (lactate accumulation was higher in the tender group), than in tough counterparts. Additionally, we could observe a higher level of oxidative stress in the tender group. No proteomics nor phosphoproteomics result hinted at the widely accepted role of calpains and cathepsins, except for the indication of calcium homeostasis dysregulation. Nevertheless, myofibrillar degradation was monitored and related to structural protein fragmentations. Fragmentation of structural proteins and activities of glycolytic enzymes were inversely related to their phosphorylation levels, suggesting that PTMs might add further levels of complexity in the frame of meat tenderness.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle / metabolism*
  • Food Analysis / methods*
  • Male
  • Meat / analysis*
  • Meat / classification*
  • Muscle Proteins / analysis
  • Muscle Proteins / chemistry*
  • Muscle, Skeletal / metabolism*
  • Proteome / analysis
  • Proteome / chemistry*


  • Muscle Proteins
  • Proteome