Document Detail


Combined effect of epinephrine and exercise on calpain/calpastatin and cathepsin B and L activity in porcine longissimus muscle.
MedLine Citation:
PMID:  10492449     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The objective of the study was to improve the understanding of the relationship between the effect of epinephrine plus exercise and meat tenderness. The calpain, calpastatin, and cathepsin B + L activities and postmortem proteolysis in porcine longissimus muscle were studied. The muscle glycogen stores were depleted in five pigs by s.c. injection of epinephrine (.3 mg/kg) at 15 h antemortem and exercise on a treadmill (5 min, 3.8 km/h) immediately before slaughter. Antemortem injection of epinephrine and treadmill exercise resulted in higher ultimate pH (6.32 vs 5.66 in control) and decreased (P < .05) thaw loss, cooking loss, and shear force values. The muscle energy depletion treatment increased (P < .05) the muscle mu-calpain activity measured 42 min postmortem, and at 24 h mu-calpain activity was still approximately 50% greater in the high ultimate pH group. Also, as the ratio of mu-calpain to calpastatin increased (P < .01), the overall proteolytic potential of the calpain system were greater. These observations suggest that the muscle energy level may influence the activity of the calpain system in the living animal. The high ultimate pH group showed lower (P < .001) cathepsin B + L activity in the myofibrillar and the soluble fractions after 8 d of storage, suggesting that the increased ultimate pH increased the stability of the lysosomal membrane and thereby reduced the release of cathepsins from the lysosomes during storage. The SDS-PAGE showed increased (P < .001) degradation of a 39-kDa band in the epinephrine and exercise-treated samples. Degradation products at 30, 31, and 32 kDa were labeled by troponin-T antibody in western blot. An appearing 24-kDa band was identified as a troponin-I degradation product in western blot. The proteolytic degradation pattern of myofibrillar proteins during storage differed in control and treated samples, supporting the hypothesis that calpain-mediated proteolysis was affected after treatment, resulting in meat with high ultimate pH.
Authors:
P Ertbjerg; P Henckel; A Karlsson; L M Larsen; A J Møller
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of animal science     Volume:  77     ISSN:  0021-8812     ISO Abbreviation:  J. Anim. Sci.     Publication Date:  1999 Sep 
Date Detail:
Created Date:  1999-10-05     Completed Date:  1999-10-05     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8003002     Medline TA:  J Anim Sci     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  2428-36     Citation Subset:  IM; S    
Affiliation:
Department of Dairy and Food Science, Royal Veterinary and Agricultural University, Frederiksberg C, Denmark. peer@kvl.dk
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MeSH Terms
Descriptor/Qualifier:
Animals
Calcium-Binding Proteins / metabolism*
Calpain / metabolism*
Cathepsin B / metabolism*
Cathepsin L
Cathepsins / metabolism*
Cysteine Endopeptidases
Electrophoresis, Polyacrylamide Gel
Endopeptidases*
Energy Metabolism
Epinephrine / pharmacology*
Female
Glycogen / metabolism
Meat / standards
Muscle, Skeletal / drug effects,  metabolism*
Physical Conditioning, Animal*
Swine / metabolism*
Chemical
Reg. No./Substance:
0/Calcium-Binding Proteins; 51-43-4/Epinephrine; 79079-11-1/calpastatin; 9005-79-2/Glycogen; EC 3.4.-/Cathepsins; EC 3.4.-/Endopeptidases; EC 3.4.22.-/Calpain; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.22.1/Cathepsin B; EC 3.4.22.15/Cathepsin L

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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