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Molecular Pharmacology, Vol 18, 468-475, Copyright © 1980 by the American Society for Pharmacology and Experimental Therapeutics
1 Department of Tissue Culture, Norsk Hydro’s Institute for Cancer Research, The Norwegian Radium Hospital, Montebello,
Oslo 3, Norway
More than 60 different amines have been tested for their effect on protein degradation and protein synthesis in isolated rat hepatocytes. Unsubstituted monoamines and amino alcohols were generally lysosomotropic, as shown by their ability to inhibit protein degradation and to induce lysosomal swelling (vacuolation). In a nutrient-free medium these amines also inhibited protein synthesis, apparently by limiting the supply of degradation-derived amino acids and energy substrates. Some diamines were lysosomotropic; others were not. Most of the diamines inhibited protein synthesis and did so independently of whether they affected protein degradation or not. Polyamines, amino acids, and quaternary ammonium compounds were not lysosomotropic. All of the typically lysosomotropic amines inhibited protein degradation to the same extent (corresponding to approx. 75% of the overall degradation), and their maximal effects were nonadditive. This may indicate a complete and selective blockade of the lysosomal pathway of protein degradation, making these compounds useful tools in the study of intracellular protein metabolism.
Submitted on May 12, 1980
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