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Am J Physiol Cell Physiol 270: C76-C85, 1996;
0363-6143/96 $5.00
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AJP - Cell Physiology, Vol 270, Issue 1 C76-C85, Copyright © 1996 by American Physiological Society

ARTICLES

Creatine analogue beta-guanidinopropionic acid alters skeletal muscle AMP deaminase activity

P. C. Tullson, K. W. Rundell, R. L. Sabina and R. L. Terjung
Department of Physiology, State University of New York Health Science Center at Syracuse 13210, USA.

Dietary supplementation of the creatine analogue beta-guanidinopropionic acid (beta-GPA) decreases in vitro skeletal muscle AMP deaminase (AMP-D) activity in rats. Downregulation of AMP-D activity was progressive and greater in fast-twitch muscles (70-80%) than in the slow-twitch soleus muscle (approximately 50%). The loss in AMP-D activity had little effect on inosine 5'-monophosphate accumulation in mixed-fiber muscle with intense tetanic contractions. In contrast, inosine 5'-monophosphate formation was evident earlier in fast-twitch red and white fiber sections of creatine-depleted animals during intense twitch contractions, indicating that fast-twitch muscle of beta-GPA-treated rats buffers decreases in the ATP/ADPfree ratio via deamination, even though AMP-D activity is less. Isoforms of skeletal muscle AMP-D mRNAs in mixed-fiber muscle were not altered by feeding beta-GPA for up to 9 wk. Creatine depletion did not alter total immunoreactivity; however, a redistribution of AMP-D immunoreactivity from primarily an approximately 80-kDa form toward lower apparent molecular mass species (approximately 60 and approximately 56 kDa) was observed. Posttranslational changes in AMP-D appear related to changes in activity.


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