Abstract
Monoamine oxidase is an enzyme that breaks down biological amines, such as norepinephrine and serotonin and renders them inert for producing vasoconstriction. The purpose of this study was to characterize monoamine oxidase activity in skeletal muscle arteries and to determine if estrogen contributes to sex‐related differences in monoamine oxidase activity. Five male and 20 female F344 rats were anesthetized. Twelve females were ovariectomized and a subset of six received an estrogen pellet (17β‐estradiol (4μg/day)). In all animals, the white gastrocnemius 1A arteriole (WG1A) was removed. The arterioles were homogenized in enzyme buffer. Luminometric and spectrophotometric assays were used to quantify monoamine oxidase activity and total protein content of the vessel, respectively. Relative luminescence units (RLU) were proportionate to monoamine oxidase activity. Monoamine oxidase activity in the WG1A was 29.85±18.71 RLU·μg−1 protein for males, but only 11.42±5.13 RLU·μg−1 protein in females (p<0.05). Estrogen replacement had no effect on monoamine oxidase activity (Ovariectomized: 16.63±10.64 RLU·μg−1 protein; Ovariectomized+estrogen: 16.93±10.38 RLU·μg−1 protein). These results suggest that there are sex‐related differences in monoamine oxidase activity, but, estrogen does not appear to be the hormone that influences sex‐related differences in monoamine oxidase activity.
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