Abstract
Monoamine oxidases (MAOs) are FAD containing enzymes located on the outer membrane of mitochondria that catalyze the oxidative deamination of biogenic amines to aldehydes and H2O2. In view of the toxic action of these products, we have analyzed the consequence of the catalytic activity of MAOs on the induction of membrane permeability transition (MPT) in rat isolated hepatic mitochondria. This Ca2+-dependent phenomenon, characterized by the opening of a membrane pore and the consequent impairment of the mitochondrial bioenergetic function was monitored experimentally by measuring the absorbance change at 540 nm and membrane potential (DY) collapse. Inflamm. res. 50, Supplement 2 (2001) S132–S133 1023-3830/01/02S132-02 $ 1.50+0.20/0 © Birkhauser Verlag, Basel, 2001
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