Key result
Monoamine oxidase was localized in the endoplasmic reticulum, nuclear envelope, and mitochondrial outer compartment of guinea pig and rat tissues using BSPT and tryptamine.
This study demonstrates the ultrastructural localization of MAO in various tissues, including myocardium, using a novel tetrazolium salt.
Localization in rodent myocardium warrants clinical caution; extends ultrastructural MAO mapping but leaves open human translation.
The ultrastructural localization of monoamine oxidase (MAO) is demonstrated with tryptamine and a new nonosmiophilic tetrazolium salt, 2-(2'-benzothiazolyl)-5-styryl-3-(4'-phthalhydrazidyl) tetrazolium chloride (BSPT), which is reduced to an osmiophilic formazan. Under the cytochemical conditions for conducting osmication, the styryl group is not osmicated. MAO is localized in guinea pig myocardial, renal and hepatic tissues and rat myocardium. Enzymatic activity is demonstrated in endoplasmic reticulum, nuclear envelope and mitochondrial outer compartment, specifically in the outer membrane. Sensitivity to formaldehyde fixation and specific MAO inhibitors indicates that the enzymatic activity is due to MAO and possibly other amine oxidases.
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Shannon et al. (1974) studied this question. BSPT and tryptamine was evaluated on Ultrastructural localization of monoamine oxidase (MAO). Monoamine oxidase was localized in the endoplasmic reticulum, nuclear envelope, and mitochondrial outer compartment of guinea pig and rat tissues using BSPT and tryptamine.
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