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J. Biochem, 1990, Vol. 107, No. 6 817-820
© 1990 Japanese Biochemical Society

research-article

Uptake of 3H-Labeled 1-Aminooxy-3-Aminopropane by Baby Hamster Kidney Cells1

Tapani Hyvönen*,2, Alex R. Khomutov**, Radii M. Khomutov**, Seppo Lapinjoki*** and Terho O. Eloranta*

*Departments of Biochemistry
**Institute of Molecular Biology, the U.S.S.R. Academy of Sciences Vavilov Street 32, Moscow, 117 984 U.S.S.R
***Pharmaceutical Chemistry, University of Kuopio P.O. Box 6, SF-70211 Kuopio, Finland

2 To whom correspondence should be addressed.

The uptake, catabolism, and release of 3H-labeled 1-aminooxy-3-aminopropane, a new putrescine analog shown to be a potent polyamine antimetabolite, into and from baby hamster kidney cells (BHK21/C13) were studied. The results show that [3H] -1-aminooxy-3-aminopropane (APA) is not concentrated in the cell, does not compete with polyamines for transport and reveals no difference in uptake between polyamine-depleted and control cells. After a 12-h culture, 60% of APA was recovered intact in the culture media. At this time point, only 30% of the intracellular radioactivity was intact APA, showing that the drug is catabolized in the cells. This intracellular ratio persisted throughout the 4-day culture period. The metabolites of APA were not characterized further. The results indicate that the drug is not recognized as a polyamine by the cells and does not replace or interfere with the polyamines in cellular functions. Thus, its potent affinity to ornithine decarbox-ylase and spermidine synthase is likely to be due to close structural similarity with the intermediates formed in these reactions. This has implications for the mechanisms involved.

1 This work was supported by the National Council for Natural Sciences, Finland.


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