| Literature DB >> 8135854 |
N Meskini1, G Némoz, I Okyayuz-Baklouti, M Lagarde, A F Prigent.
Abstract
The cyclic nucleotide phosphodiesterase (PDE) inhibitory profile of four related xanthine derivatives: pentoxifylline (BL 191), propentofylline (HWA 285), torbafylline (HWA 448) and albifylline (HWA 138), pharmacologically active on the peripheral and/or cerebral microcirculation was established using the four main PDE isoforms present in rat heart cytosol. HPLC on a Mono Q ion-exchange column resolved four separate cyclic nucleotide PDE activities: a calmodulin-activated fraction (PDE I), a cGMP-stimulated fraction (PDE II), a cAMP-specific rolipram-sensitive fraction (PDE IV) and a cGMP-inhibited fraction (PDE III). Among the four compounds studies, only torbafylline and pentoxifylline inhibited more efficiently the calcium plus calmodulin-stimulated than the basal activity of PDE I. The four xanthine derivatives inhibited more potently the cGMP-stimulated than the basal activity of the cGMP-stimulatable PDE II, propentofylline being the most inhibitory (IC50: 20 microM). Except for propentofylline, which exhibited a marked selectivity toward the rolipram-sensitive PDE versus the cGMP-inhibited PDE III, the other xanthines modestly (IC50 in the 10(-4) M range) inhibited both cAMP-specific isoforms with similar potency. Propentofylline proved to be the best inhibitor whatever the considered isoform whereas torbafylline exhibited the weakest inhibitory potency with, however, some selectivity for PDE I.Entities:
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Year: 1994 PMID: 8135854 DOI: 10.1016/0006-2952(94)90477-4
Source DB: PubMed Journal: Biochem Pharmacol ISSN: 0006-2952 Impact factor: 5.858