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Effect of monoamine oxidase inhibitors on qualitative alterations in enzymatic properties of mitochondrial monoamine oxidases
Authors:M H Abdel Samed  Z I Akopyan  I V Veryovkina  A A Kulygina  V Z Gorkin
Affiliation:2. Division of Pediatric Pulmonology, Allergy & Sleep Medicine, Department of Pediatrics, Indiana University School of Medicine, Riley Hospital for Children at Indiana University Health, Indianapolis, Indiana;3. Allergy Partners, Columbus, Indiana;4. Department of Biostatistics, School of Public Health, Indiana University School of Medicine, Indianapolis, Indiana;1. Department of Clinical Pharmacology, Medical University of Vienna, Waehringer Guertel 18-20, 1090 Vienna, Austria;2. Department of Obstetrics and Gynecology, Medical University of Vienna, Waehringer Guertel 18-20, 1090 Vienna, Austria;3. Department of Biotechnology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria;4. Institute of Immunology, Center for Pathophysiology, Infectiology and Immunology Medical University of Vienna, Waehringer Guertel 18-20, 1090 Vienna, Austria;5. Department of Biomedical Sciences, Veterinary Research Tower, Cornell University, Ithaca, NY 14853-6401, USA;6. Department of Internal Medicine I, Division of Hematology, Medical University of Vienna, Waehringer Guertel 18-20, 1090 Vienna, Austria
Abstract:Preincubation of highly purified ox liver MAO with specific MAOI pargyline, iproniazid or tranylcypromine prevents qualitative alteration (“transformation”) in enzymatic properties of MAO after treatment of the enzyme with oxidized oleic acid (OOA). Pretreatment with pargyline or tranylcypromine of highly purified rat liver MAO prevents qualitative alteration in its enzymatic properties after incubation with Cu2+ in aerobic conditions. Pretreatment of rats with iproniazid prevents appearance in liver mitochondria of histamine-, putrescine- and l-lysine-deaminating activity after parenteral administration of OOA into the rats. It is possible that MAOI may find new fields of application based on their property to prevent qualitative alteration in enzymatic properties of monoamine oxidases in some pathological states (e.g. those accompanied by accumulation of lipid peroxides in tissues).
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