Cottingen, Federal Republic of Germany Characteristics of glutamine transport, its substrate specificity, and its pattern of competitive and non-competitive inhibition in response to amino acid analogues were determined in peripheral human lymphocytes, incubated with or without concanavalin A (Con A
Comparison between transport and degradation of leucine and glutamine by peripheral human lymphocytes exposed to concanavalin A
✍ Scribed by Brigitte Koch; Marie-Theres Schröder; Gertrud Schäfer; Peter Schauder
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 632 KB
- Volume
- 143
- Category
- Article
- ISSN
- 0021-9541
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✦ Synopsis
Cottingen, Federal Republic of Germany
Transport and pathways of leucine and glutamine degradation were evaluated in resting human peripheral lymphocytes and compared with the changes induced by concanavalin A (ConA). Cells were incubated with [l-'4C]leucine (0.1 5 mM), [U-'4C]leucine (0.15 mM), or [U-'4C]glutamine (0.4 mM) after culture with or without 2, 5, 7, or 10 (*g/ml ConA for 2, 18, or 24 hours, respectively. Initial rates of transport of leucine and glutamine were augmented 2.7-fold and threefold by the mitogen. Leucine transamination, irreversible oxidation, and catabolism beyond isovaleryl-CoA were increased by 90%, 20%, and GO%, respectively. Glutamine utilization increased threefold; accumulation of glutamate, aspartate, and ammonia increased by 700%, SO%, and loo%, respectively, and 14C0, production by about 400% in response to ConA. The results indicate that ConA stimulates to about the same extent transport of leucine and glutamine into lymphocytes. Glutamine is mainly channeled into catabolic pathways, while leucine remains largely preserved. It is suggested that these metabolic changes provide more leucine for incorporation into protein and more N-and C-atoms required for the synthesis of macromolecules and energy from glutamine.
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