Open AccessInterleukin 2 receptor gene expression in normal human T lymphocytes.
Author(s) -
Warren J. Leonard,
Martin Krönke,
Nancy J. Peffer,
Joel M. Depper,
Warner C. Greene
Publication year - 1985
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.82.18.6281
Subject(s) - interleukin 21 receptor , receptor , 5 ht5a receptor , biology , microbiology and biotechnology , gene expression , receptor expression , protease activated receptor 2 , interleukin 4 receptor , messenger rna , interleukin 12 receptor, beta 1 subunit , interleukin 5 receptor alpha subunit , liver receptor homolog 1 , interleukin 1 receptor, type ii , nuclear receptor co repressor 1 , interleukin 6 receptor , interleukin 1 receptor, type i , cell surface receptor , gene , interleukin , nuclear receptor , transcription factor , cytokine , interleukin 5 , biochemistry , g alpha subunit , immunology , protein subunit
We have used cDNAs for the human interleukin 2 (IL-2) receptor to study IL-2 receptor gene expression in normal activated T cells. Resting T cells do not contain detectable IL-2 receptor mRNA. Within 1 hr after stimulation with phytohemagglutinin (PHA), a large, presumably nuclear precursor RNA species is seen, which then gradually disappears. Mature IL-2 receptor mRNA forms appear within 8 hr after stimulation, reach peak levels between 8 and 24 hr, and then decline. Thus, in PHA-activated lymphocytes the rise and fall in IL-2 receptor mRNA levels precede by more than 24 hr the peak and decline of IL-2 receptor protein expression occurring at the cell surface. 4 beta-Phorbol 12-myristate 13-acetate (PMA) also stimulates IL-2 receptor mRNA and protein expression by T cells. Combinations of optimal concentrations of PHA and PMA produce an additive effect on IL-2 receptor mRNA levels, suggesting that PHA and PMA may induce IL-2 receptor gene expression through different, complementary mechanisms. Nuclease S1-protection assays indicate that IL-2 receptor mRNAs may differ in length due to the use of three different polyadenylylation signals. Further, these assays demonstrate the presence of transcripts that lack a 216-base segment within the protein-coding region and thus do not encode a functional IL-2 receptor. Nuclear transcription assays indicate that the increase in IL-2 receptor mRNA is reflected at the level of transcription. Thus, IL-2 receptor gene regulation controls IL-2 receptor expression at the cell surface and is intimately linked to the control of T-cell proliferation.