Abstract
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 D<sub>3</sub> 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)<sub>2</sub> D<sub>3</sub>) 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)<sub>2</sub> D<sub>3</sub> most inhibited the myogenic differentiation of Sol 8 cells. 1,25-(OH)<sub>2</sub> D<sub>3</sub> 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)<sub>2</sub> D<sub>3</sub>, respectively, whereas calapstatin level was significantly decreased. There was no changes in calcium uptake into inner cells by 100 nM 1,25-(OH)<sub>2</sub> D<sub>3</sub> 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)<sub>2</sub> D<sub>3</sub> without alteration of calcium concentration of inner cell. Therefore, the role of vitamin D receptor remains to be further elucidated later.
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