2003
DOI: 10.1152/ajpcell.00365.2002
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Interleukin-2 receptor-γ-dependent endocytosis depends on biotin in Jurkat cells

Abstract: . Interleukin-2 receptor-␥-dependent endocytosis depends on biotin in Jurkat cells.

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Cited by 30 publications
(29 citation statements)
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“…Note that factors other than protein folding may also affect the extracellular concentration of IL-2. Previously we have demonstrated that expression of IL-2 receptor γ correlates positively with biotin supply in Jurkat cells [44]. Increased expression of IL-2 receptor γ is associated with increased endocytosis of IL-2, decreasing the concentration of IL-2 in the culture medium.…”
Section: Discussionmentioning
confidence: 84%
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“…Note that factors other than protein folding may also affect the extracellular concentration of IL-2. Previously we have demonstrated that expression of IL-2 receptor γ correlates positively with biotin supply in Jurkat cells [44]. Increased expression of IL-2 receptor γ is associated with increased endocytosis of IL-2, decreasing the concentration of IL-2 in the culture medium.…”
Section: Discussionmentioning
confidence: 84%
“…Jurkat cells fold and secrete relatively moderate amounts of proteins, i.e., <100 pg of IL-2/(10 6 cells × h) [44]. It will be of interest to determine whether cells that secrete larger amounts of proteins (e.g., antibody-producing cells) are more susceptible to triggering UPR in response to biotin supplementation.…”
Section: Discussionmentioning
confidence: 99%
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“…Supplementation of biotin in cultured human cells modulates the expression of genes related to cell growth and immune response. [4][5][6][7] Furthermore, mRNA of hepatic glucokinase (GCK), an initial glycolytic enzyme, is increased by biotin administration in fasting or streptozotocin (STZ)-induced diabetic rats; [8][9][10][11] in contrast, the gluconeogenic enzyme, phosphoenolpyruvate carboxykinase (PCK1), mRNA inversely decreases. 12) Recently, biotinyl histones have been discovered in biotin-supplemented cultured human cells, and this novel histone modification is thought to repress or enhance classical histone modifications, such as phosphorylation, acetylation and methylation, and to bring about epigenetic alterations in chromatin.…”
mentioning
confidence: 99%
“…For example, the expression of genes encoding glucokinase, phosphoenolpyruvate carboxykinase and ornithine transcarbamylase decreases in response to biotin deficiency (5). Recently, evidence has been provided that the expression of genes encoding the cytokine interleukin-2 (IL-2) 3 and IL-2 receptor ␥ correlate with biotin status in human lymphoid cells (6).…”
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confidence: 99%