J. Anim Sci.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


J. Anim Sci. 1989. 67:3313-3321.
© 1989 American Society of Animal Science

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Forsberg, N. E.
Right arrow Articles by Wehr, N. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Forsberg, N. E.
Right arrow Articles by Wehr, N. B.

Effects of Cimaterol on Rabbit Growth and Myofibrillar Protein Degradation and on Calcium-Dependent Proteinase and Calpastatin Activities in Skeletal Muscle1,2,3,

N. E. Forsberg4,6,, M. A. Ilian4, A. Ali-Bar5, P. R. Cheeke4 and N. B. Wehr4

Oregon State University, Corvallis 97331-6702

Abstract

The objectives of this study were to examine effects of a beta-adrenergic agonist (cimaterol) on growth and muscle development in rabbits and to examine cimaterol's effects on myofibrillar protein degradation (MPD) and on activities of several proteolytic enzymes including the calcium-dependent proteinases (CDP). Twelve New Zealand White rabbits were assigned to either control diets or to diets containing cimaterol for 35 d, after which they were killed and effects on performance and tissue weight gains were determined. Urine was collected from d 21 through 28 from each rabbit for assessment of N{tau}-methylhistidine (NMH) excretion. Cimaterol increased rates of gain, efficiency of gain and skeletal muscle weights. Enhancement in muscle weight was associated with an increase in total DNA and with a reduction in NMH. Cimaterol did not affect activities of cathepsin B, cathepsin D or neutral serine proteinase, but it reduced activities of the millimolar and micromolar forms of the CDP by 58 and 57%, respectively, and it reduced activity of the inhibitor of the CDP (calpastatin) by 52%. Cimaterol-dependent myofibrillar protein accretion was likely mediated, at least in part, by a reduction in MPD. The change in MPD was associated with a reduction in muscle CDP activities. Cimaterol-dependent muscle hypertrophy therefore may involve changes in calcium-dependent proteolysis of myofibrillar proteins. The significance of the effects of cimaterol on calpastatin activity is not known.


Footnotes

1 Published as paper number 8738 of the Oregon Agric. Exp. Sta.

2 The authors acknowledge the generous assistance of M. Koohmaraie in development of assays for calcium-dependent proteinases and calpastatin. The authors also thank Helen Chesbrough for typing the manuscript. Cimaterol was a gift of American Cyanamid Co., Princeton, NJ.

3 Supported in part by USDA grant 88-37265-3796.

4 Dept. of Anim. Sci., Oregon State Univ.

5 Faculty of Agric., Sana'a Univ., Sana'a, Yemen Arab Republic.

6 Reprint requests.




This article has been cited by other articles:


Home page
Physiol. Rev.Home page
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]


Home page
J ANIM SCIHome page
D. E. Goll, G. Neti, S. W. Mares, and V. F. Thompson
Myofibrillar protein turnover: The proteasome and the calpains
J Anim Sci, April 1, 2008; 86(14_suppl): E19 - E35.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1989 by the American Society of Animal Science.