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J Biol Chem, Vol. 273, Issue 9, 5253-5259, February 27, 1998
From the Minerva Center for Calcium and Bone Metabolism, Nephrology
Services, Hadassah University Hospital,
Jerusalem il-91120, Israel
Parathyroid hormone (PTH) regulates serum calcium
and phosphate levels, which, in turn, regulate PTH secretion and
mRNA levels. PTH mRNA levels are markedly increased in rats fed
low calcium diets and decreased after low phosphate diets, and this
effect is post-transcriptional. Protein-PTH mRNA binding studies,
with parathyroid cytosolic proteins, showed three protein-RNA bands. This binding was to the 3'-untranslated region (UTR) of the PTH mRNA and was dependent upon the terminal 60 nucleotides.
Parathyroid proteins from hypocalcemic rats showed increased binding,
and proteins from hypophosphatemic rats decreased binding, correlating with PTH mRNA levels. There is no parathyroid cell line; however, a
functional role was provided by an in vitro degradation
assay. Parathyroid proteins from control rats incubated with a PTH
mRNA probe led to an intact transcript for 40 min; the transcript
was intact with hypocalcemic proteins for 180 min and with
hypophosphatemic proteins only for 5 min. A PTH mRNA probe without
the 3'-UTR, or just the terminal 60 nucleotides, incubated with
hypophosphatemic proteins, showed no degradation at all, indicating
that the sequences in the 3'-UTR determine PTH mRNA degradation.
Hypocalcemia and hypophosphatemia regulate PTH gene expression
post-transcriptionally. This correlates with binding of proteins to the
PTH mRNA 3'-UTR, which determines its stability.
RNA-Protein Binding and Post-transcriptional Regulation of
Parathyroid Hormone Gene Expression by Calcium and Phosphate
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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