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Titolo:
INHIBITION OF AMINE OXIDASE ACTIVITY BY DERIVATIVES THAT RECOGNIZE IMIDAZOLINE I-2 SITES
Autore:
CARPENE C; COLLON P; REMAURY A; CORDI A; HUDSON A; NUTT D; LAFONTAN M;
Indirizzi:
CHU RANGUEIL,INST LOUIS BUGNARD,INSERM,U317,BAT L3 F-31054 TOULOUSE FRANCE INST RECH SERVIER F-92150 SURESNES FRANCE SCH MED SCI BRISTOL,PSYCHOPHARMACOL UNIT BRISTOL AVON ENGLAND
Titolo Testata:
The Journal of pharmacology and experimental therapeutics
fascicolo: 2, volume: 272, anno: 1995,
pagine: 681 - 688
SICI:
0022-3565(1995)272:2<681:IOAOAB>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
IDAZOXAN-BINDING-SITES; GUANIDINIUM-RECEPTIVE SITES; RABBIT CEREBRAL-CORTEX; H-3 IDAZOXAN; MONOAMINE-OXIDASE; PHARMACOLOGICAL CHARACTERIZATION; ALPHA-2-ADRENERGIC RECEPTOR; I-RECEPTORS; ADRENOCEPTOR; LIVER;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
C. Carpene et al., "INHIBITION OF AMINE OXIDASE ACTIVITY BY DERIVATIVES THAT RECOGNIZE IMIDAZOLINE I-2 SITES", The Journal of pharmacology and experimental therapeutics, 272(2), 1995, pp. 681-688

Abstract

Nonadrenergic imidazoline binding sites (imidazoline I-2 sites) have been described to be colocated with monoamine oxidase (MAO) in the mitochondrial fraction of various cell types. In the present work, the authors considered whether this colocation could be associated with a functional interplay. in rat liver membranes, [H-3]-idazoxan binding to I-2 receptors was competed for by naphazoline and idazoxan, which alsoshared a high affinity for alpha-2 adrenoceptors (alpha-2 ARs). The chemicals 2-n-heptylimidazoline (S 15430), 1-methyl-5-n-heptylimidazole(S 15674), 2-benzofuran-2-yl-imidazoline (RX 801077) and 2-(1,3-benzodioxanyl)-2-imidazoline (RX 821029) exhibited higher affinity for I-2 receptors than for alpha-2 ARs. The most selective agent was S 15430 with a 150-fold higher affinity for liver I-2 receptors than for adipocyte alpha-2 ARs. Moreover, [H-3]-idazoxan binding was also competed for by several MAO inhibitors (MAOI) that are not imidazoline or guanidinium derivatives such as tranylcypromine, harmaline, clorgiline and pargyline. Rat liver MAO activity was not only inhibited by MAOIs but also by some imidazoline derivatives: cirazoline, naphazoline, S 15674, RX 801077 and RX 821029. Idazoxan had no effect on MAO activity; it neither inhibited MAO nor prevented the inhibition induced by other imidazolines or MAOIs. This suggested that the ligand recognition site of I-2 receptors was distinct from the MAOI target site. Furthermore, some imidazolines inhibited the activity of bovine plasma amine oxidase, an enzyme that does not possess the same cofactor as MAO and is insensitive to harmaline or pargyline. Taken together, these data indicate that 1) some imidazolines, such as S 15430 or RX 801077, are more selective for I-2 sites than idazoxan or cirazoline; 2) agents that recognize I-2 sites do not necessarily belong to the family of imidazoline orguanidinium derivatives; 3) the inhibition of amine oxidase activity represents a novel biological effect of I-2-site ligands, although it appears that the site of action of imidazolines involved in MAO inhibition may be distinct from that of classic MAOIs.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 16:01:17