Abstract:
:The PDE4 catalytic machinery comprises, in part, two divalent cations in a binuclear motif. Here we report that PDE4A4 expressed in Sf9 cells exhibits a biphasic Mg(2+) dose-response (EC(50) of 0.15 and >10 mM) in catalyzing cAMP hydrolysis. In vitro phosphorylation of PDE4A4 by the PKA-catalytic subunit increases the enzyme's sensitivity to Mg(2+), leading to 4-fold increased cAMP hydrolysis without affecting its K(m). The phosphorylation also increases the potencies of (R)- and (S)-rolipram without affecting CDP-840 and SB-207499. The results support that modulating the cofactor binding affinity of PDE4 represents a mechanism for regulating its activity.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Laliberté F,Liu S,Gorseth E,Bobechko B,Bartlett A,Lario P,Gresser MJ,Huang Zdoi
10.1016/s0014-5793(02)02259-7keywords:
subject
Has Abstractpub_date
2002-02-13 00:00:00pages
205-8issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302022597journal_volume
512pub_type
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