Up- and down-regulation of longissimus tenderness parallels changes in the myofibril-bound calpain 3 protein

Mohammad A Ilian; Alaa El-Din A Bekhit; Bradley Stevenson; Jim D Morton; Peter Isherwood; Roy Bickerstaffe

doi:10.1016/j.meatsci.2003.11.016

Up- and down-regulation of longissimus tenderness parallels changes in the myofibril-bound calpain 3 protein

Meat Sci. 2004 Jul;67(3):433-45. doi: 10.1016/j.meatsci.2003.11.016.

Authors

Mohammad A Ilian¹, Alaa El-Din A Bekhit, Bradley Stevenson, Jim D Morton, Peter Isherwood, Roy Bickerstaffe

Affiliation

¹ Molecular Biotechnology Group, Animal and Food Sciences Division, P.O. Box 84, Lincoln University, Canterbury, New Zealand.

PMID: 22061518
DOI: 10.1016/j.meatsci.2003.11.016

Abstract

The objective of this study was to utilize Ca(2+) and Zn(2+) treatments of meat to critically explore the possible role of calpain 3 in meat tenderisation. Calpains 1 and 2 were also examined for comparative purpose. Control animals plus animals infused with CaCl(2), ZnCl(2) or H(2)O were used (six lambs per treatment) to determine the temporal changes in muscle calpain 3 protein in the Longissimus thoracis et lumborum (LTL) during post-mortem storage. Concurrently, the temporal changes of; (1) shear force, (2) sarcomere length, (3) proteolysis of titin and nebulin and (4) calpains 1 and 2 proteins were also determined. Infusing LTL with Ca(2+) or Zn(2+) caused significant up- and down-regulation of LTL tenderisation, respectively, compared to water infusion and the control animals. Furthermore, the rate of breakdown of calpain 3, the rate of proteolysis of titin and nebulin and the rate of meat tenderisation during post-mortem storage of LTL in the various treatments were highly correlated. These studies suggest that calpain 3, like calpain 1, may be involved in the tenderisation of meat through limited proteolysis of specific muscle structural proteins such as titin and nebulin.