Premium
Induction of protein‐tyrosine phosphatase LC‐PTP by IL‐2 in human T cells
Author(s) -
Adachi Masaaki,
Sekiya Masuo,
Ishino Masaho,
Sasaki Hiroko,
Hinoda Yuji,
Imai Kohzoh,
Yachi Akira
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80114-2
Subject(s) - protein tyrosine phosphatase , tyrosine phosphorylation , phosphorylation , tyrosine , phosphatase , microbiology and biotechnology , biology , signal transduction , protein phosphorylation , tyrosine kinase , messenger rna , receptor tyrosine kinase , gene expression , chemistry , biochemistry , protein kinase a , gene
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 l h and peaked at 6 h after IL‐2 stimulation, simultaneous with the Gl 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.