Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P14784 (IL-2 receptor)
 3,849 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The unique feature of the Ly-5 system is that it is a major cell surface glycoprotein, representing up to 10% of the total cell surface complement, confined to the hematopoietic cells as a family of isoforms generated by alternative splicing of a single Ly-5 gene. The cytoplasmic domain of Ly-5 has protein tyrosine phosphatase activity suggesting that Ly-5 is involved in signal transduction. We used Ly-5 anti-sense oligodeoxyribonucleotides (oligo) and Ly-5 monoclonal antibody (mAb) to study the functional role of Ly-5 in the concanavalin A mitogenesis response by spleen cells, as well as in the generation of lymphokine-activated killer cells and the proliferative response by spleen cells induced by recombinant human interleukin-2 (rhIL-2). Our results indicate that the Ly-5 mAb could enhance these activities whereas the anti-sense oligo was inhibitory. These data clearly suggest that Ly-5 is involved in the IL-2 and IL-2 receptor responsive circuit.
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PMID:A function of Ly-5 (CD-45) in the generation of lymphokine-activated killer cells defined by Ly-5 anti-sense oligodeoxyribonucleotides and Ly-5 monoclonal antibody. 778 93

Engagement of interleukin-2 (IL-2) mediates the heterodimeridation of the common beta chain (beta(c)) and common gamma chain (gamma(c)) of the IL-2 receptor (IL-2R). This is sufficient and necessary for receptor activation and signal transduction. It is generally held that the IL-2R is activated by the trans-activity of the protein tyrosine kinases (PTKs) Jak1 and Jak3 associated with beta(c) and gamma(c) respectively. Transduction of proliferative signals requires Jak3 activity. A Jak3 independent signalling pathway involving p56(lck), generating anti-apoptotic signals, can be observed and requires the PROX domain of gamma(c). p56(lck) can be activated by dephosphorylation of an inhibitory carboxyl terminal phosphorylated tyrosine residue (Y505). We propose that this is mediated by a PROX domain associated protein tyrosine phosphatase (PTP). Activation of p56(lck) alone is insufficient for transduction of proliferative signals and thus works in concert with Jak3 mediated receptor activation. This indicates that both gamma(c) domains are vital for signal transduction.
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PMID:Activation of the interleukin 2 receptor: a possible role for tyrosine phosphatases. 1088 65

CD4(+) T cells express IL-2 receptor complexes to the same level as CD8(+) T cells when the two T cell populations were stimulated simultaneously. However, the activation of downstream signaling molecules, such as Jaks, was increased in CD8(+) T cells. Although equivalent amounts of CD45, which acts as a Jak phosphatase, was expressed on the two T cell populations, those on the CD8(+) T cells have less protein tyrosine phosphatase activity than those on the CD4(+) T cells. Furthermore, we find that different CD45 isoforms dominate in the two populations; CD45RO on proliferating CD4(+) T cells and CD45RBC on proliferating CD8(+) T cells. In addition, NIH3T3 cells expressing the CD45RBC transgene had more phosphorylated Jak1 and grew faster than those with the CD45RO transgene. Thus, the expression of specific CD45 isoforms on T cells correlates with their proliferative response to IL-2, suggesting that controlling cells expressing specific CD45 isoforms could correct excessive or insufficient immune responses.
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PMID:Expression of CD45 isoforms correlates with differential proliferative responses of peripheral CD4+ and CD8+ T cells. 2009 41