Postmortem proteolysis is reduced in transgenic mice overexpressing calpastatin1,2

M. P. Kent, M. J. Spencer, M. Koohmaraie
2004 Journal of Animal Science  
Postmortem proteolysis is reduced in transgenic mice overexpressing calpastatin 2004. 82:794-801. J Anim Sci ABSTRACT: Using both in vitro and in vivo approaches, numerous studies have provided evidence that -calpain is responsible for postmortem proteolysis. This paper reports the effect of overexpression of calpastatin on postmortem proteolysis in transgenic mice. Transgenic mice (n = 8) with a human calpastatin gene, whose expression was driven by the human skeletal muscle actin promoter,
more » ... actin promoter, were killed along with control nontransgenic littermates (n = 5). Hind limbs were removed and stored at 4°C, and muscle samples were dissected at 0, 1, 3, and 7 d postmortem and analyzed individually. At time 0, active human calpastatin was expressed in transgenic murine skeletal muscle at a level 370-fold greater (P < 0.001) than calpastatin in control mice. Although the native isoform of this protein was degraded with storage, at 7 d postmortem, approximately 78% of at-death activity remained, indicating that degraded calpastatin retains activity. Calpain (and m-) expression was unaffected (P > 0.05) by the
doi:10.1093/ansci/82.3.794 pmid:15032436 fatcat:z6onuefnl5csbis4mq5hvgf7ca