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(Received for publication, March 20, 1996, and in revised form, July 16, 1996)
From the Department of Pharmacology, University of Washington,
Seattle, Washington 98195
We report here the identification of cDNAs
for three new mouse PDE1C splice variants and the
characterization of their kinetics, regulation by Ca2+,
sensitivities to inhibitors, and tissue/cellular expression patterns.
Sequence analysis indicated that these three cDNAs (PDE1C1, PDE1C4,
and PDE1C5), together with our previously reported PDE1C2 and PDE1C3,
are alternative splice products of the PDE1C gene. The
results from RNase protection analysis and in situ
hybridization indicated that the expression of the different
PDE1C splice variants is differentially regulated in a
tissue/cell-specific manner. Particularly, high levels of
PDE1C mRNAs were found in the olfactory epithelium,
testis, and several regions of mouse brain such as cerebellar granule
cells. All of these splice variants have similar kinetic properties,
showing high affinities and approximately the same relative
Vmax values for both cAMP and cGMP. However,
they responded to Ca2+ stimulation differently. In
addition, they show different sensitivities to the
calmodulin-dependent phosphodiesterase inhibitors, KS505a
and SCH51866. Substrate competition experiments suggested the presence
of only one catalytic site on these PDE1C isozymes for both
cAMP and cGMP. In summary, these findings suggest that the
PDE1C gene undergoes tissue-specific alternative
splicing that generates structurally and functionally diverse
gene products.
Volume 271, Number 41,
Issue of October 11, 1996
pp. 25699-25706
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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