Premium
The Density of Monoamine Oxidase B Sites Is Not Altered in the Postmortem Brain of Alcoholics
Author(s) -
Maeztu Ana I.,
Ballesteros Javier,
Callado Luis F.,
Gutiérrez Miguel,
Meana J. Javier
Publication year - 1997
Publication title -
alcoholism: clinical and experimental research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.267
H-Index - 153
eISSN - 1530-0277
pISSN - 0145-6008
DOI - 10.1111/j.1530-0277.1997.tb04479.x
Subject(s) - monoamine oxidase , monoamine oxidase b , ethanol , enzyme , chemistry , in vitro , monoamine oxidase a , potency , medicine , endocrinology , biochemistry , biology
The status of the enzyme monoamine oxidase B (MAO‐B) was directly evaluated in the postmortem brain from 20 alcoholics and 23 matched controls. The density of MAO‐B sites was quantified by the specific binding of the selective inhibitor [ 3 H]Ro 19‐6327 (lazabemide) (8 nM) to cortical membranes. A positive correlation between age at death and MAO‐B density was observed in the total sample ( r = 0.37, p = 0.015). The density of MAO‐B in alcoholics (B max = 1,263 ± 131 fmol/mg of protein) was not different form that in control (B max = 1,131 ± 96 fmol/mg of protein). Ethanol in vitro inhibited [ 3 H]Ro 19‐6327 binding, with similar potency in membranes form alcoholics ( K i = 280 ± 13 mM) and controls ( K i = 338 ± 84 mM). The present results in brain tissue contrast with previous reports of decreased MAO‐B enzymatic activity in platelets of alcoholics, but strongly agree with recent genetic studies on MAO‐B status in alcoholism.