Involvement of Calpain 3 in Postmortem Talin 2 Degradation Influencing Meat Quality

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  • 肉質に影響するタリン2の死後分解におけるカルパイン3の関与
  • ニクシツ ニ エイキョウ スル タリンツー ノ シゴ ブンカイ ニ オケル カルパインスリー ノ カンヨ

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Abstract

The present experiment was conducted to determine which calpain isoforms contribute to the postmortem degradation of the costamere protein talin 2. The chicken pectoralis major (PM) and biceps femoris (BF) muscles gizzard (G) and heart (H) were stored for 4 days at 4℃. Talin 2 in PM and BF were degraded during early postmortem time, but that in G and H were not degraded. While, desmin in PM was degraded faster than the others. The ratio of calpain 1 mRNA level to calpastatin was seemed to correspond to the postmortem degradation of desmin. The ratio of calpain 2 to calpastatin and the ratio of calpain 3 to ribosomal protein large P1 were seemed to correspond to the postmortem degradation of talin 2. Desmin in the isolated myofibrils of the skeletal muscles was degraded with 5 mM Ca2+ and not degraded with leupeptin, the ubiquitous calpain inhibitor. However, talin 2 was degraded with 5 mM Ca2+ and leupeptin. Desmin and talin 2 in the heart were not influenced by 5 mM Ca2+. Furthermore talin 2 was degraded with 1 μM Ca2+ at 4℃, but desmin was not. Therefore, we propose that talin 2 is degraded by calpain 3 during postmortem storage.

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