Abstract
Amino acid transport was studied in freshly isolated adult rat hepatocytes using non-metabolizable alpha-amino-1-[14C] isobutyric acid and 1-aminocyclopentane-1-[14C] carboxylic acid. In the presence of sodium, hepatocytes concentrated alpha-aminoisobutyric acid; this concentrative component of the transport had properties similar to transport system A. The sodium-independent transport of aminocyclopentane carboxylic acid had properties similar to transport system L (facilitated diffusion). Glucagon stimulated the influx of alpha-aminoisobutyric acid into hepatocytes. The glucagon effect (a) occurred rapidly, but its full expression required two hours of exposure of the cells to hormone; (b) involved new protein (and possibly RNA) synthesis; and (c) occurred at low concentrations of glucagon (50% effect with 0.4 nm). Glucagon stimulated only system A. Cyclic AMP also stimulated the transport of alpha-aminoisobutyric acid. Freshly isolated hepatocytes appear conveniently suited to the investigation of various aspects of the regulation of liver amino acid transport in normal and pathophysiological states.
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