Journal of Applied Physiology, Vol 69, Issue 3 843-848, Copyright © 1990 by American Physiological Society

ARTICLES

Cytochrome c mRNA and alpha-actin mRNA in muscles of rats fed beta-GPA

M. M. Lai and F. W. Booth
Department of Physiology and Cell Biology, University of Texas Medical School, Houston 77225.

A diet of 1% beta-guanidinopropionic acid (beta-GPA) fed to rats for weeks results in decreased muscle adenosine triphosphate and creatine phosphate concentrations (J. Biol. Chem. 249: 1060-1063, 1974), increased activities of selected mitochondrial enzymes (Biochem. J. 232: 125-131, 1985), and atrophied type IIb fibers (Lab. Invest. 33: 151-158, 1975). The hypothesis of the present study was that chronic beta-GPA feeding would increase cytochrome c mRNA in muscle and would decrease alpha-skeletal actin mRNA in type IIb muscle. Data collected supported, in part, the hypothesis. After 22 days of a 1% beta-GPA diet, cytochrome c mRNA was increased 60-67% in muscles with inherently low cytochrome c mRNA but was not altered in muscles with higher cytochrome c mRNA levels. alpha-Skeletal actin mRNA was unchanged in muscles with low and high cytochrome c mRNA after 22 days of 1% beta-GPA. After 66 days of beta-GPA feeding, both cytochrome c mRNA and alpha-skeletal actin mRNA were decreased 18 and 26%, respectively, per unit of total RNA, in white quadriceps muscle. At the same time muscles composed of predominantly type II fibers atrophied 22%, whereas type I muscle size was unaltered. These data suggest that high-energy phosphate levels could play some role in adaptive changes in muscle composition.

This article has been cited by other articles:

				J. Stoppani, A. L. Hildebrandt, K. Sakamoto, D. Cameron-Smith, L. J. Goodyear, and P. D. Neufer AMP-activated protein kinase activates transcription of the UCP3 and HKII genes in rat skeletal muscle Am J Physiol Endocrinol Metab, December 1, 2002; 283(6): E1239 - E1248. [Abstract] [Full Text] [PDF]

				P. E. Durante, K. J. Mustard, S.-H. Park, W. W. Winder, and D. G. Hardie Effects of endurance training on activity and expression of AMP-activated protein kinase isoforms in rat muscles Am J Physiol Endocrinol Metab, July 1, 2002; 283(1): E178 - E186. [Abstract] [Full Text] [PDF]

				D. A. Hood Plasticity in Skeletal, Cardiac, and Smooth Muscle: Invited Review: Contractile activity-induced mitochondrial biogenesis in skeletal muscle J Appl Physiol, March 1, 2001; 90(3): 1137 - 1157. [Abstract] [Full Text] [PDF]

				M. Wyss and R. Kaddurah-Daouk Creatine and Creatinine Metabolism Physiol Rev, July 1, 2000; 80(3): 1107 - 1213. [Abstract] [Full Text] [PDF]

				Z. Yan and F. W. Booth Cytochrome c promoter activity in soleus and white vastus lateralis muscles in rats J Appl Physiol, September 1, 1998; 85(3): 973 - 978. [Abstract] [Full Text] [PDF]

				J. W. E. Rush, P. C. Tullson, and R. L. Terjung Molecular and kinetic alterations of muscle AMP deaminase during chronic creatine depletion Am J Physiol Cell Physiol, February 1, 1998; 274(2): C465 - C471. [Abstract] [Full Text] [PDF]