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J Biol Chem, Vol. 274, Issue 26, 18438-18445, June 25, 1999
From the Discovery Research Laboratory, cDNA encoding a novel phosphodiesterase (PDE)
was isolated from a human fetal lung cDNA library and designated
PDE10A. The deduced amino acid sequence contains 779 amino acids,
including a putative cGMP binding sequence in the amino-terminal
portion of the molecule and a catalytic domain that is 16-47%
identical in amino acid sequence to those of other PDE families.
Recombinant PDE10A transfected and expressed in COS-7 cells hydrolyzed
cAMP and cGMP with Km values of 0.26 and 7.2 µM, respectively, and Vmax with
cGMP was almost twice that with cAMP. Of the PDE inhibitors tested,
dipyridamole was most effective, with IC50 values of 1.2 and 0.45 µM for inhibition of cAMP and cGMP hydrolysis, respectively. cGMP inhibited hydrolysis of cAMP, and cAMP inhibited cGMP hydrolysis with IC50 values of 14 and 0.39 µM, respectively. Thus, PDE10A exhibited properties of a
cAMP PDE and a cAMP-inhibited cGMP PDE. PDE10A transcripts were
particularly abundant in the putamen and caudate nucleus regions of
brain and in thyroid and testis, and in much lower amounts in other
tissues. The PDE10A gene was located on chromosome 6q26 by fluorescent
in situ hybridization analysis. PDE10A represents a new
member of the PDE superfamily, exhibiting unique kinetic properties and
inhibitor sensitivity.
Cloning and Characterization of a Novel Human Phosphodiesterase
That Hydrolyzes Both cAMP and cGMP (PDE10A)
,, and Laboratory of Biological Chemistry,
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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