## Abstract Two transport systems for neutral amino acids have been characterised in LLC‐PK~1~ cells. The first, which transport alanine in a sodium‐dependent manner, also mediates alanine exchange and is preferentially inhibited by serine, cysteine, and α‐amino‐n‐butyric acid. This system resemble
Cystine and dibasic amino acid uptake by opossum kidney cells
✍ Scribed by Beatrice States; Stanton Segal
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 866 KB
- Volume
- 143
- Category
- Article
- ISSN
- 0021-9541
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✦ Synopsis
Abstract
The characteristics of the uptake of L‐cystine by the continuous opossum kidney cell line, OK, were examined. Uptake of cystine is rapid and, in contrast to other continuous cultured cell lines, these cells retain the cystine/dibasic amino acid transport system which is found in vivo and in freshly isolated kidney tissue. Confluent monolayers of cells also fail to show the presence of the cystine/glutamate transport system present in LLC‐PK~1~ cells, fibroblasts, and cultured hepatocytes. Uptake of cystine occurs via a high‐affinity saturable process which is independent of medium sodium concentration. The predominant site of cystine transport is across the apical cell membrane. The intracellular concentration of GSH far exceeds that of cysteine with a ratio greater than 100:1 for GSH:cysteine. Incubation of cells for 5 minutes with a physiological level of labelled cystine resulted in the labelling of 66% and 5% of the total intracellular cysteine and glutathione, respectively. The ability of these cells to reflect the shared cystine/dibasic amino acid transport system makes them a suitable model for investigation of the cystine carrier which is altered in human cystinuria.
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