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Mitochondrial Physiology Unit, Department of Biology, Tufts University, Medford, Massachusetts 02155
Using rat liver mitochondria we determined that the primary biochemical target for inhibition of mitochondrial bioenergetic function by rhodamine 123 (Rh123) was FoF1-ATPase and that the amount of Rh123 associated with mitochondria is proportional to the mitochondrial membrane potential. Inhibition of coupled respiration by Rh123 in mitochondria isolated from CX-1, a Rh123-sensitive carcinoma cell type, and CV-1, a Rh123-insensitive normal epithelial cell type, was linearly related to the amount of Rh123 added (µg/mg protein) with CX-1 mitochondria exhibiting 2-fold greater inhibition compared to CV-1 mitochondria at any given amount of dye. The inhibition pattern for mitochondria isolated from MIP101, a Rh123-insensitive carcinoma cell type, was nonlinear, exhibiting greater sensitivity than CV-1 mitochondria at very low amounts of Rh123 but becoming less sensitive than either CV-1 or CX-1 at higher amounts. Rh123 inhibited FoF1-ATPase activity to a similar extent and in a concentration-dependent manner in both CV-1 and CX-1 mitochondria, but a different and complex pattern of inhibition was apparent for MIP101 mitochondria. Moreover, mitochondria from the 2 carcinoma cell types, CX-1 and MIP101, had higher membrane potentials (163 ± 7 and 158 ± 8 mV, respectively) than did mitochondria from the normal epithelial cell type, CV-1 (104 ± 9 mV). It was concluded that differences in both mitochondrial membrane potential and sensitivity of FoF1-ATPase contribute to the selective cytotoxicity exhibited by Rh123 for certain cell types in vitro.
1 Submitted in partial fulfillment of the requirements for the Ph.D. in Biology at Tufts University.
2 To whom requests for reprints should be addressed, at Mitochondrial Physiology Unit, Department of Biology, Tufts University, Medford, Massachusetts 02155.
Received 7/28/86. Revised 4/27/87. Accepted 5/15/87.
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