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J Biol Chem, Vol. 275, Issue 17, 12963-12969, April 28, 2000

Structural Determinants for Post-transcriptional Stabilization of Lactate Dehydrogenase A mRNA by the Protein Kinase C Signal Pathway*

Sabine Short, Di Tian, Marc L. Short, and Richard A. JungmannDagger

From the Department of Cellular and Molecular Biology and Cancer Center, Northwestern University Medical School, Chicago, Illinois 60611-3008

Activation of protein kinase C (PKC) and protein kinase A (PKA) in rat C6 glioma cells increases the half-life of short-lived lactate dehydrogenase (LDH)-A mRNA about 5- and 8-fold, respectively. PKA and PKC act synergistically and prolong LDH-A mRNA half-life more than 21-fold. Similar effects were observed after transfection and transcription of a globin/lactate dehydrogenase minigene consisting of a beta -globin expression vector in which the 3'-untranslated region (UTR) of beta -globin had been replaced with the LDH-A 3'-UTR. Synergism was only obtained by transcription of minigenes containing the entire 3'-UTR and did not occur when truncated 3'-UTR fragments were analyzed. Additional mutational analyses showed that a 20-nucleotide region, named PKC-stabilizing region (PCSR), is responsible for mediating the stabilizing effect of PKC. Previous studies (Tian, D., Huang, D., Short, S., Short, M. L., and Jungmann, R. A. (1998) J. Biol. Chem. 273, 24861-24866) have demonstrated the existence of a cAMP-stabilizing region in LDH-A 3'-UTR. Sequence analysis of PCSR identified a 13-nucleotide AU-rich region that is common to both cAMP-stabilizing region and PCSR. These studies identify a specific PKC-responsive stabilizing element and indicate that interaction of PKA and PKC results in a potentiating effect on LDH-A mRNA stabilization.

* This work was supported by Grant GM53115 from the National Institutes of Health and Neuroscience Training Grant T32NS07140 (to D. T.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dept. of Cell and Molecular Biology, Northwestern University Medical School, 303 E. Chicago Ave., Chicago, IL 60611. Tel.: 312-908-5275; Fax: 312-503-7107; E-mail: rjungman@nwu.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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