Studies of free and protein-bound β-flavaspidic acid (cas 114-42-1)-N-methylglucaminate in isolated rat hepatocytes and mitochondria☆

Add time:08/24/2019    Source:sciencedirect.com

β-Flavaspidic acid-N-methylglucaminate (FLAV), the water-soluble derivative of flavaspidic acid, was absorbed from medium by isolated hepatocytes at a concentration-dependent rate. At a medium concentration of 5 mM, FLAV was absorbed at a steady state rate of 1.2 nmoles/mg of protein/min. Oxygen consumption by the cells was increased erratical ly by 0.18 nmoles/mg of protein/ min, a quantity not considered sufficient to support microsomal oxidation of the compound. When added to mitochondrial suspensions, FLAV at concentrations ranging from 80 nM to 8 μM uncoupled oxidative phosphorylation and caused a linear stimulation of ADP-independent respiration. FLAV binds readily to bovine serum albumin (BSA) and to the fatty acid-binding protein (FABP) in the cytosol. When bound to these proteins in molar ratios of 0.66 and 3.3, respectively, or to a partially purified cytosolic FABP protein (12.7 nmoles/μg of protein), FLAV failed to uncouple oxidative phosphorylation. These data suggest that, at a medium concentration of 5 mM, FLAV does not alter the mitochondrial oxidative activity of isolated hepatocytes. Thus, results from studies in isolated hepatocytes utilizing FLAV reflect the displacement of fatty acids from FABP and are not due to a secondary metabolic effect of the compound at the level of oxidative phosphorylation.

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