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Volume 272, Number 14, Issue of April 4, 1997 pp. 9161-9165
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Cytoplasmic Protein mRNA Interaction Mediates cGMP-modulated Translational Control of the Asialoglycoprotein Receptor

(Received for publication, December 19, 1996, and in revised form, January 29, 1997)

From the Department of Medicine, Marion Bessin Liver Research Center, Albert Einstein College of Medicine, New York, New York 10461

Expression of the asialoglycoprotein receptor by the human hepatocellular carcinoma cell line HuH-7 in response to intracellular cGMP concentrations was previously shown to be regulated at the translational level. In a cell-free system, initiation of asialoglycoprotein receptor mRNA translation was dependent on the presence of the 7-methylguanylate cap site and was independent of 8-bromo-cGMP levels in which the cells were grown prior to RNA isolation. Stable transfection of COS-7 cells with deletion constructs of the asialoglycoprotein receptor H2b subunit localized the cGMP-responsive cis-acting element to the mRNA 5-untranslated region (UTR). Addition of biotin (an activator of guanylate cyclase) induced the expression of -galactosidase present as a chimeric plasmid containing the H2b 187-nucleotide 5-UTR. An RNA gel retardation assay identified a 37-nucleotide cognate sequence within this 187-nucleotide region. Titration of the 5-UTR with a cytosolic fraction isolated from HuH-7 grown in the presence or absence of 8-bromo-cGMP or biotin provided direct evidence for an RNA-binding protein responsive to intracellular levels of cGMP. Based on these findings, it seems reasonable to propose that reduction of intracellular levels of cGMP by biotin deprivation results in a negative trans-acting factor associating with the 5-UTR of asialoglycoprotein receptor mRNAs, thereby inhibiting translation.

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