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Characterization of the isoenzymes of cyclic nucleotide phosphodiesterase in human platelets and the effects of E4021.

Abstract：

:In extracts of human platelets, three isoenzymes of cyclic nucleotide phosphodiesterase (PDE), namely, PDE2, PDE3, and PDE5, were identified; activities of PDE1 and PDE4 were not detected. In human platelets, the cGMP-hydrolytic activity was about six times higher than the cAMP-hydrolytic activity, and PDE5 and PDE3 are the major phosphodiesterase isoenzymes that hydrolyze cGMP and cAMP, respectively. PDE5 exhibited organ-specific expression in humans, and platelets were among the tissues richest in PDE5. A novel inhibitor of PDE5, sodium 1-[6-chloro-4-(3,4-methylenedioxybenzyl)aminoquinazolin-2-yl ] piperidine-4-carboxylate sesquihydrate (E4021), was a potent and highly selective inhibitor of human platelet PDE5. However, E4021 (up to 10 microM) did not inhibit 9,11-epithio-11,12-methano-thromboxane A2-induced platelet aggregation, in vitro. E4021 plus SIN-1 (3-morpholino-sydnonimine), at concentrations that had little effect individually, inhibited aggregation. These results suggest the unique distribution of phosphodiesterase isoenzymes in human platelets and the PDE5 inhibitors might be useful as a new class of antiplatelet drugs.

journal_name

Cell Signal

journal_title

Cellular signalling

authors

Ito M,Nishikawa M,Fujioka M,Miyahara M,Isaka N,Shiku H,Nakano T

doi

10.1016/s0898-6568(96)00112-x

subject

Has Abstract

pub_date

1996-12-01 00:00:00

pages

575-81

issue

8

eissn

0898-6568

issn

1873-3913

pii

S0898-6568(96)00112-X

journal_volume

8

pub_type

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