Tyrosine phosphorylation has been implicated in interleukin 2 (IL-2)-induced growth signaling and the phosphorylation levels are regulated by the balance of tyrosine kinase and tyrosine phosphatase activities. Here, we demonstrate the rapid activation of a leukocyte tyrosine phosphatase LC-PTP (HePTP) gene expression by IL-2 in an IL-2 dependent human T cell ILT-Mat. Accumulation of LC-PTP mRNA appeared at 1 h and peaked at 6 h after IL-2 stimulation, simultaneous with the G1 to early S phase, and the induction of LC-PTP mRNA did not require protein synthesis. LC-PTP protein increased approximately 6-fold at 8 h after IL-2 stimulation. Nuclear run-on assays showed that the induction of LC-PTP mRNA expression is mostly due to transcriptional activation. These data suggest that LC-PTP is an early response gene and its protein seems to be a crucial molecule which regulates the tyrosine phosphorylation level during T cell proliferation.
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Adachi et al. (1994) studied this question.
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