Abstract

The rate of uptake of hypoxanthine in S49 cells was only about 2–5% of the rate of hypoxanthine transport observed in many other types of mammalian cells, and of the rate of uridine transport in this and other cell types. Part of the slow entry of hypoxanthine seems to be due to non-mediated permeation, but the remainder is saturable, strongly inhibited by uridine, nitrobenzylthioinosine and dipyridamole and not detectable in a nucleoside-transport-deficient mutant of S49 cells (AE1). The inhibition of hypoxanthine transport in S49 cells by nitrobenzylthioinosine resembles the inhibition of nucleoside transport in these and other mammalian cells, whereas it contrasts with the resistance of hypoxanthine transport to nitrobenzylthioinosine in all types of mammalian cells that have been investigated. We conclude that S49 cells lack the hypoxanthine transport system common to other types of cells and that hypoxanthine entry into these cells is mediated, although very inefficiently, by the nucleoside transporter. In contrast, adenine transport in S49 and AE1 cells was comparable to that in other types of cells.

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