Tenderness has been identified as the single most important palatability factor affecting
consumer satisfaction of beef meat. A couple of recent methods to activate calpain-induced
tenderization has been the oral supplementation of vitamin D3 or its m...
Tenderness has been identified as the single most important palatability factor affecting
consumer satisfaction of beef meat. A couple of recent methods to activate calpain-induced
tenderization has been the oral supplementation of vitamin D3 or its metabolites. To improve
understanding of the regulation of calpain protease system in muscle, the effects of
1,25-Dihydroxy colecalciferol (1,25-(OH)2 D3) on calpain protease enzymes were studied using
Sol 8 cell line. In criteria of cell number and proliferation, a concentration of 100 nM
1,25-(OH)2 D3 most inhibited the myogenic differentiation of Sol 8 cells. 1,25-(OH)2 D3
increased mRNA gene expressions of u-calpain while that of m-calpain and calpastatin showed
(p < 0.05) the opposite expression pattern. The amount of u-calapin and m-calpain protein were
the highest (p < 0.01) at 4h and 2h incubation with 1,25-(OH)2 D3, respectively, whereas
calapstatin level was significantly decreased. There was no changes in calcium uptake into inner
cells by 100 nM 1,25-(OH)2 D3 in spite of significant (p < 0.05) up-regulation in vitamin D
receptor gene expression. The results indicated that the calpain protease system of Sol 8 cell
was greatly influenced by 1,25-(OH)2 D3 without alteration of calcium concentration of inner
cell. Therefore, the role of vitamin D receptor remains to be further elucidated later.