Abstract
The effects of aminoglycosides, 3', 4'-dideoxykanamycin B (DKB), gentamicin, and amikacin, on rat kidney cortical lysosomes were investigated. The binding of 3H-DKB to the lysosomal fraction was significantly larger than that to any other subcellular fraction examined. In the presence of 10-2M aminoglycosides, about 70% of the N-acetyl-β-D-glucosaminidase was released. However, the release of this enzyme fell below the control level at 10-5M DKB. In the case of acid phosphatase, the release increased gradually with aminoglycosides concentration. The higher the concentration of aminoglycosides became, the greater was the fluidity of the lysosomal membrane. These results suggest that aminoglycoside binds to the lysosomal membrane and increases the membrane fluidity, leading to the release of N-acetyl-β-D-glucosaminidase and acid phosphatase from the lysosomes.
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