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J. Biol. Chem., Vol. 275, Issue 40, 31469-31479, October 6, 2000
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From the Discovery Research Laboratory, Tanabe Seiyaku Co. Ltd.,
2-50, Kawagishi-2-chome, Toda, Saitama 335-8505, Japan
cDNAs encoding a novel phosphodiesterase,
phosphodiesterase 11A (PDE11A), were isolated by a combination of
reverse transcriptase-polymerase chain reaction using degenerate
oligonucleotide primers and rapid amplification of cDNA ends.
Their catalytic domain was identical to that of PDE11A1 (490 amino acids) reported during the course of this study. However, the
cDNAs we isolated had N termini distinct from PDE11A1, indicating
two novel N-terminal variants of PDE11A. PDE11A3 cDNA encoded a
684-amino acid protein including one complete and one incomplete GAF
domain in the N-terminal region. PDE11A4 was composed of 934 amino
acids including two complete GAF domains and shared 630 C-terminal
amino acids with PDE11A3 but had a distinct N terminus containing the
putative phosphorylation sites for cAMP- and cGMP-dependent
protein kinases. PDE11A3 transcripts were specifically expressed in
testis, whereas PDE11A4 transcripts were particularly abundant in
prostate. Recombinant PDE11A4 expressed in COS-7 cells hydrolyzed cAMP
and cGMP with Km values of 3.0 and 1.4 µM, respectively, and the Vmax
value with cAMP was almost twice that with cGMP. Although PDE11A3
showed the same Km values as PDE11A4, the relative
Vmax values of PDE11A3 were approximately one-sixth of those of PDE11A4. PDE11A4, but not PDE11A3, was
phosphorylated by both cAMP- and cGMP-dependent protein
kinases in vitro. Thus, the PDE11A gene undergoes
tissue-specific alternative splicing that generates structurally and
functionally distinct gene products.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AB036704 and AB038041.
Isolation and Characterization of Two Novel Phosphodiesterase
PDE11A Variants Showing Unique Structure and Tissue-specific
Expression*
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 81-48-433-8069;
Fax: 81-48-433-8159; E-mail: k-omori@tanabe.co.jp.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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