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Relationship Between Imidazoline 2 Sites and Monoamine Oxidase
Author(s) -
PATERSON LM,
TYACKE RJ,
NUTT DJ,
HUDSON AL
Publication year - 2003
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1304.045
Subject(s) - imidazoline receptor , monoamine oxidase , allosteric regulation , chemistry , binding site , enzyme , monoamine neurotransmitter , ligand (biochemistry) , stereochemistry , non competitive inhibition , membrane , biochemistry , biophysics , pharmacology , biology , receptor , serotonin
A bstract : I 2 site‐selective compounds are known to interact with and inhibit monoamine oxidase (MAO), but it remains unclear as to whether this interaction occurs through an allosteric or competitive interaction. This study used the new selective, irreversible I 2 ligand BU99006, to clarify the relationship between MAO and the I 2 binding sites (I 2 ‐BS). Results demonstrate that irreversible binding of BU99006 to rat brain membranes does not inhibit the enzyme or interfere with its interaction with other imidazoline enzyme inhibitors. This finding suggests that the I 2 sites that react with BU99006 are not those implicated in MAO inhibition and points to the existence of at least two distinct I 2 binding proteins.