| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
ANIMAL PRODUCTS |
,3
* CCL Research, Veghel, The Netherlands NL-5462;
and
Department of Pharmacology, University of Illinois College of Medicine, Chicago, IL 60612-3725; and
and
USDA, ARS, Roman L. Hruska US Meat Animal Research Center, Clay Center, NE 68933-0166
3 Corresponding author: koohmaraie{at}email.marc.usda.gov
The objective of this investigation was to test the hypothesis that -calpain is largely responsible for postmortem proteolysis of muscle proteins. To accomplish this objective, we compared proteolysis of known muscle proteins in muscles of wild type and µ-calpain knockout mice during postmortem storage.Knockout mice (n = 6) were killed along with control mice (n = 6). Hind limbs were removed and stored at4°C. Muscles were dissected at 0, 1, and 3d postmortem and subsequently analyzed for degradation of nebulin, dystrophin, metavinculin, vinculin, desmin, and tropo-nin T. In a separate experiment, hind limb muscles from knockout (n = 4) and control mice (n = 4) were analyzed at 0, 1, and 3 d postmortem using casein zy-mography to confirm that µ-calpain activity was knocked out in muscle and to determine whether or not m-calpain is activated in murine postmortem muscle. Cumulatively, the results of the first experiment indicated that postmortem proteolysis was largely inhibited in µ-calpain knockout mice. The results of the second experiment established the absence of µ-calpain in the muscle tissue of knockout mice and confirmed the results of an earlier study that m-calpain is active in postmortem murine muscle. The results of the current study show that even in a species in which m-calpain is activated to some extent postmortem, µ-calpain is largely responsible for postmortem proteolysis. This observation excludes a major role for any of the other members of the calpain family or any other proteolytic system in postmortem proteolysis of muscle proteins. Therefore, understanding the regulation of µ-calpain in postmortem muscle should be the focus of further research on postmortem proteolysis and tenderization of meat.
Key Words: µ-calpain • meat tenderization • postmortem • proteolysis
This article has been cited by other articles:
|
|
 |
|
  J. Berard, M. Kreuzer, and G. Bee Effect of litter size and birth weight on growth, carcass and pork quality, and their relationship to postmortem proteolysis J Anim Sci, September 1, 2008; 86(9): 2357 - 2368. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. P. Camou, S. W. Mares, J. A. Marchello, R. Vazquez, M. Taylor, V. F. Thompson, and D. E. Goll Isolation and characterization of {micro}-calpain, m-calpain, and calpastatin from postmortem muscle. I. Initial steps J Anim Sci, December 1, 2007; 85(12): 3400 - 3414. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. P. Camou, J. A. Marchello, V. F. Thompson, S. W. Mares, and D. E. Goll Effect of postmortem storage on activity of {micro}- and m-calpain in five bovine muscles J Anim Sci, October 1, 2007; 85(10): 2670 - 2681. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
