Oct 1, 1990

Uptake and metabolism of dipeptides by human red blood cells

The Biochemical Journal
H LochsS A Adibi


A function of the abundant cytoplasmic peptidases in red blood cells could be hydrolysis of oligopeptides circulating in plasma. To investigate whether human red blood cells actively transport dipeptides for this purpose, these cells were incubated with 14C-labelled glycylproline, glycylsarcosine, glycine, proline and alanine. There was uptake of each dipeptide, as indicated by their recovery as dipeptides in the cell cytoplasm. However, after a brief time (1-2 min) uptake of dipeptides abruptly ceased, while that of amino acids continued. As a result, after 30 min red blood cell uptake of amino acids was 5-13-fold greater than that of any dipeptide. Investigation of intracellular contents after 1 min of incubation revealed different metabolism for different dipeptides. The composition of intracellular radioactivity was 19-71% as intact dipeptides, 0-20% as free amino acids and 8-77% as neither dipeptides nor constituent amino acids. Investigation of the mechanism of dipeptide uptake by red blood cells showed: (1) a lack of hydrolysis by the plasma membrane, (2) no non-specific binding to the plasma membrane, and (3) a lack of saturation over a wide range of concentrations (0.05-50 mM). The data suggest that the mechanism of up...Continue Reading

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Mentioned in this Paper

Metabolic Process, Cellular
Amino Acids, I.V. solution additive
Peptide Hydrolases
Red blood cells, blood product

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