Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-3-15
pubmed:abstractText
Nonadrenergic imidazoline binding sites (imidazoline I2 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, [3H]-idazoxan binding to I2 receptors was competed for by naphazoline and idazoxan, which also shared 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 I2 receptors than for alpha-2 ARs. The most selective agent was S 15430 with a 150-fold higher affinity for liver I2 receptors than for adipocyte alpha-2 ARs. Moreover, [3H]-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 I2 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.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-3565
pubmed:author
pubmed:issnType
Print
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
681-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Inhibition of amine oxidase activity by derivatives that recognize imidazoline I2 sites.
pubmed:affiliation
Institut National de la Santé et de la Recherche Médicale (INSERM U 317), Institut Louis Bugnard, Université Paul Sabatier, Toulouse, France.
pubmed:publicationType
Journal Article