Permeability of rat liver mitochondria to leucine, tyrosine, α-aminoisobutyric acid, and lysine

Abstract

Radioactive tracer studies show that l-leucine is rapidly taken up by isolated rat liver mitochondria. There is an initial rapid uptake of l-leucine during the first 30 sec of incubation, followed by a slower, progressive increase in l-leucine accumulation over a 10-min incubation. d-Leucinc penetrates the mitochondria rapidly but does not accumulate inside. Both the d and l isomers of tyrosine penetrate the mitochondria relatively more slowly, equilibration being achieved only after several minutes of incubation. The synthetic amino acid, α-aminoisobutyric acid, is shown to rapidly enter the mitochondria. This amino acid is not accumulated within the mitochondria. l-Lysine, a positively charged amino acid, exhibits uptake characteristics similar to those of l-leucine. An examination of the energetic requirements for these amino acid transfer processes reveals no dependence on metabolic energy or on gradients of inorganic cations, and no effects of several reagents known to block other transport mechanisms, under the conditions tested. These findings and previously reported observations are consistent with the view that the membranes of rat liver mitochondria contain a number of different mechanisms mediating uptake of various amino acids.