Abstract
The distribution and intracellular translocation of AFB 1 in various subcellular fractions was investigated in isolated hepatocytes by pulse-chase experiments. After labeling the hepatocytes with [ 3H]-AFB 1 (14.5 nM) for 15 min, the highest concentration of [ 3H]-AFB 1 was found in the cytosolic fraction where 66% was bound noncovalently and 1.5% covalently. The lowest concentration of [ 3H]-AFB 1 was found in the nuclear fraction; 36% and 4.9% were bound noncovalently and covalently respectively. When the [ 3H]-AFB 1 loaded cells were chased with unlabeled AFB 1 (1 μM), the radioactivity of [ 3H]-AFB 1 in the cell lysate and cytosolic fraction decreased in time with an apparant rate of elimination ( t1 2 ) of 93 min and 66 min, respectively. The levels of covalently bound AFB 1 increased with time and reached a maximum at 60 min in nuclei (270%), and at 120 min in mitochondria (220%) and cytosol (430%) as compared to the zero time. Only in the microsomal fraction was there no significant increase with time in covalently bound AFB 1. These results suggest that the toxin after activation by the microsomal mixed function oxidases was either detoxified or transported to other cellular organelles where covalent binding of macromolecules occurred.
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