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      1,25-dihydroxycholecalciferol 이 Sol 8 세포내 calpain계 mRNA 및 단백질 발현에 미치는 영향

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      https://www.riss.kr/link?id=A102674607

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      다국어 초록 (Multilingual 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 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.
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      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.

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