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J. Biol. Chem., Vol. 269, Issue 28, 18271-18274, Jul, 1994
C Sette, E Vicini and M Conti
Several mRNAs coding for a cAMP-specific phosphodiesterase (ratPDE3/IVd)
with divergent 5' regions have been detected in mammalian cells. To
determine the physiological significance of these differences, the
expression of these mRNAs and the properties of the corresponding proteins
were investigated. At least three mRNA species derived from the ratPDE3/IVd
gene (ratPDE3.1, ratPDE3.2, and ratPDE3.3 mRNAs) are present in Sertoli and
thyroid cells and in brain. Expression of ratPDE3.1 and ratPDE3.2 but not
ratPDE3.3 mRNAs was dependent on hormone stimulation. The ratPDE3.2 and
ratPDE3.3 mRNA variants were translated into polypeptides with
immunochemical and biochemical properties identical to the native cAMP
phosphodiesterases (PDEs) found in the Sertoli cell and thyroid FRTL-5
cells. Incubation of the recombinant PDEs with the catalytic subunit of the
cAMP- dependent protein kinase in a cell-free system caused the
phosphorylation and activation of the ratPDE3.3 protein variant. Under the
same experimental conditions, ratPDE3.1 and ratPDE3.2 protein variants were
neither phosphorylated nor activated by the cAMP- dependent protein kinase.
Similar results were obtained by stimulating cells expressing the three
recombinant PDE variants with dibutyryl cAMP. These findings demonstrate
that the ratPDE3/IVd gene codes for PDE forms subject to different
regulations.
The ratPDE3/IVd phosphodiesterase gene codes for multiple proteins differentially activated by cAMP-dependent protein kinase [published erratum appears in J Biol Chem 1994 Aug 12;269(32):20806]
Department of Gynecology and Obstetrics, Stanford University, Medical Center, California 94305-5317.
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