Repression of rat kidney L-arginine:glycine amidinotransferase synthesis by creatine at a pretranslational level

D. M. McGuire, Myron D Gross, J. F. Van Pilsum, H. C. Towle

Research output: Contribution to journalArticlepeer-review

64 Scopus citations

Abstract

The first committed reaction in the biosynthesis of creatine is catalyzed by the enzyme L-arginine:glycine amidinotransferase, commonly called transamidinase. Creatine, the end product of the biosynthetic pathway, is known to alter the levels of kidney transamidinase activity. Rats fed a diet containing 0.3% creatine had 26% of the kidney transamidinase activity of the rats fed a creatine-free diet. This reduction in transamidinase activity was correlated with a decrease in transamidinase protein in the creatine-fed rats. The relative synthetic rates and mRNA functional activities of transamidinase were measured in control and creatine-fed rats. The relative synthetic rate of transamidinase in creatine-fed rats was 21% of that found in the control animals. The functional transamidinase mRNA in creatine-fed rats was correspondingly reduced to 37% of the amount in the control animals. Thus, creatine affects transamidinase activity by altering its rate of synthesis at a pretranslational step and represents an example of end-product repression in a higher eukaryote.

Original languageEnglish (US)
Pages (from-to)12034-12038
Number of pages5
JournalJournal of Biological Chemistry
Volume259
Issue number19
StatePublished - Jan 1 1984

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