|
|
||||||||
Journal of Animal Science, Vol 69, Issue 12 4823-4835, Copyright © 1991 by American Society of Animal Science
JOURNAL ARTICLE |
M. Koohmaraie, S. D. Shackelford, N. E. Muggli-Cockett and R. T. Stone
Roman L. Hruska U.S. Meat Anim. Res. Center, U.S. Department of Agriculture, Clay Center, NE 68933.
To examine the effect of a beta-adrenergic agonist (BAA) on muscle growth, proteinase activities, and postmortem proteolysis, 16 wether lambs were randomly assigned to receive 0 or 4 ppm of L644,969 in a completely mixed high-concentrate diet for 6 wk. Weight of the biceps femoris was 18.6% heavier in treated lambs. At 0 h after slaughter, treated lambs had higher cathepsin B (35.6%), cathepsins B + L (19.1%), calpastatin (62.8%), and m-calpain (24.6%) than control lambs, but both groups had similar mu-calpain activities. In both longissimus and biceps femoris muscles, treated lambs had higher protein and RNA and lower DNA concentrations. However, total DNA was not affected, indicating that the increase in muscle mass was probably due to muscle hypertrophy rather than to hyperplasia. The pattern of postmortem proteolysis was significantly altered by BAA feeding. In treated lambs, postmortem storage had no effect on the myofibril fragmentation index and degradation of desmin and troponin-T. These results indicate that the ability of the muscle to undergo postmortem proteolysis has been dramatically reduced with BAA feeding. Similar proteolytic systems are thought to be involved in antemortem and postmortem degradation of myofibrillar proteins, so BAA-mediated protein accretion is probably due, at least in part, to reduced protein degradation. To examine whether protein synthesis was altered with BAA feeding, the level of skeletal muscle alpha-actin mRNA was quantified. Longissimus muscle alpha-actin mRNA abundance was 30% greater in BAA-fed lambs. Collectively, these results indicate that dietary administration of BAA increases muscle mass through hypertrophy and that the increase in muscle protein accretion is due to reduced degradation and possibly to increased synthesis of muscle proteins.
This article has been cited by other articles:
![]() |
R. J. Rathmann, J. M. Mehaffey, T. J. Baxa, W. T. Nichols, D. A. Yates, J. P. Hutcheson, J. C. Brooks, B. J. Johnson, and M. F. Miller Effects of duration of zilpaterol hydrochloride and days on the finishing diet on carcass cutability, composition, tenderness, and skeletal muscle gene expression in feedlot steers J Anim Sci, November 1, 2009; 87(11): 3686 - 3701. [Abstract] [Full Text] [PDF] |
||||
![]() |
G. G. Hilton, J. L. Montgomery, C. R. Krehbiel, D. A. Yates, J. P. Hutcheson, W. T. Nichols, M. N. Streeter, J. R. Blanton Jr., and M. F. Miller Effects of feeding zilpaterol hydrochloride with and without monensin and tylosin on carcass cutability and meat palatability of beef steers J Anim Sci, April 1, 2009; 87(4): 1394 - 1406. [Abstract] [Full Text] [PDF] |
||||
![]() |
G. S. Lynch and J. G. Ryall Role of {beta}-Adrenoceptor Signaling in Skeletal Muscle: Implications for Muscle Wasting and Disease Physiol Rev, April 1, 2008; 88(2): 729 - 767. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. L. Gruber, J. D. Tatum, T. E. Engle, K. J. Prusa, S. B. Laudert, A. L. Schroeder, and W. J. Platter Effects of ractopamine supplementation and postmortem aging on longissimus muscle palatability of beef steers differing in biological type J Anim Sci, January 1, 2008; 86(1): 205 - 210. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. S. Quinn, B. G. Anderson, and S. R. Plymate Muscle-specific overexpression of the type 1 IGF receptor results in myoblast-independent muscle hypertrophy via PI3K, and not calcineurin, signaling Am J Physiol Endocrinol Metab, December 1, 2007; 293(6): E1538 - E1551. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. M. Gunawan, B. T. Richert, A. P. Schinckel, A. L. Grant, and D. E. Gerrard Ractopamine induces differential gene expression in porcine skeletal muscles J Anim Sci, September 1, 2007; 85(9): 2115 - 2124. [Abstract] [Full Text] [PDF] |
||||
![]() |
G. H. Geesink, S. Kuchay, A. H. Chishti, and M. Koohmaraie {micro}-Calpain is essential for postmortem proteolysis of muscle proteins J Anim Sci, October 1, 2006; 84(10): 2834 - 2840. [Abstract] [Full Text] [PDF] |
||||
![]() |
G. H. Geesink, R. G. Taylor, and M. Koohmaraie Calpain 3/p94 is not involved in postmortem proteolysis J Anim Sci, July 1, 2005; 83(7): 1646 - 1652. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. A. Cummins, S. M. Lonergan, and E. Huff-Lonergan Short Commuunication: Effect of Dietary Protein Depletion and Repletion on Skeletal Muscle Calpastatin During Early Lactation J Dairy Sci, May 1, 2004; 87(5): 1428 - 1431. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. P. Kent, M. J. Spencer, and M. Koohmaraie Postmortem proteolysis is reduced in transgenic mice overexpressing calpastatin J Anim Sci, March 1, 2004; 82(3): 794 - 801. [Abstract] [Full Text] [PDF] |
||||
![]() |
T. G. McDaneld, D. L. Hancock, and D. E. Moody Altered mRNA abundance of ASB15 and four other genes in skeletal muscle following administration of {beta}-adrenergic receptor agonists Physiol Genomics, January 15, 2004; 16(2): 275 - 283. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |