The development of proteomic biomarkers for meat tenderness remains an important challenge. The present study used Longissimus thoracis (LT) and Semitendinosus (ST) muscles of young bulls of three continental breeds (Aberdeen Angus, Blond d'Aquitaine and Limousin) to i) identify cellular pathways robustly related with meat tenderness, using potential protein biomarkers and ii) describe biochemical mechanisms underlying muscle to meat conversion. Correlation networks reveal robust correlations, i.e. present for at least two breeds, between potential meat tenderness biomarkers. For the two muscles of the three breeds, DJ-1 and Peroxiredoxin 6 were consistently correlated with Hsp20 and μ-calpain, respectively. For the three breeds, μ-calpain was related to Hsp70-8 in the LT muscle. Various correlations were muscle specific. For the three breeds, DJ-1 was correlated with Hsp27 for the ST, and with ENO3 and LDH-B for the LT muscle. Overall, in the LT, more correlations were found between proteins related to the glycolytic pathway and in the ST, with the small Hsps (Hsp20, 27 and αB-crystallin). Hsp70-Grp75 appeared involved in several relevant biological pathways. At the scientific level, results give insights in biological functions involved in meat tenderness. Further studies are needed to confirm the possible use of these biomarkers in the meat industry to improve assurance of good meat qualities.