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)

In vivo and in vitro productions of interleukin-2 (IL-2), IL-2 receptor (IL-2R) and gamma-interferon (gamma-IFN) in 64 multi-transfused thalassemic patients and 20 healthy children were studied. The results were: 1) Increased serum concentrations of IL-2 and IL-2R, and decreased serum concentration of gamma-IFN were found in thalassemic patients when compared to controls. 2) In in vitro study, productions of IL-2, IL-2R and gamma-IFN were much lower in thalassemic patients than in controls. The possible mechanisms for the altered lymphokine productions are discussed.
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PMID:In vivo and in vitro productions of interleukin-2, interleukin-2 receptor and gamma-interferon in multitransfused thalassemic patients. 162 46

Interleukin-2 (IL-2) stimulates the proliferation of activated antigen-specific T cells through its interaction with high affinity receptors. This event is largely regulated by the inducible expression of the alpha-chain (CD25) which, in combination with the beta-chain and possibly additional chains, forms the high affinity IL-2 receptor (IL-2R) complex. From a concanavalin A (Con A)-activated ovine T-cell complementary DNA (cDNA) library we have isolated two cDNA clones which together constitute a 2650 base pair (bp) messenger RNA (mRNA) species encoding the ovine IL-2R alpha chain. The nucleotide sequence has high homology with analogous cDNA from other species and predicts a mature protein of 254 amino acids. In addition to the predominate 2.6 kilobase (kb) ovine IL-2R alpha chain mRNA species. Northern blot analysis of activated T-cell RNA revealed two larger mRNA species. The ovine IL-2R alpha chain cDNA was transfected into CHO cells and low affinity binding of human recombinant IL-2 demonstrated. Polyclonal antisera generated against the transfected cells cross-reacted with Con A-activated ovine lymphocytes. In addition these antisera were used to immunoprecipitate a unique 50,000 MW protein from the transfected cells. It is likely that this protein represents the expressed ovine IL-2R alpha chain cDNA which is heavily glycosylated as distinct from the 30,869 MW primary translation product. Southern blot analysis of ovine genomic DNA suggests that the ovine IL-2R alpha chain is encoded by a single copy gene.
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PMID:Molecular cloning, expression and characterization of the ovine IL-2R alpha chain. 162 87

Interleukin-2-dependent pathways of lymphocyte activation were investigated in canine peripheral blood lymphocytes (PBL) following stimulation with T-cell mitogens including phytohemagglutinin, phorbol ester (TPA), calcium ionophore (ionomycin), and human recombinant interleukin-2 (hrIL-2). The ability of the stimulated cells to produce interleukin-2 (IL-2) was determined using murine indicator cell lines. IL-2 receptor expression by mitogen-stimulated canine PBL was confirmed by the binding of hrIL-2 with high affinity, and with characteristics comparable to those of the human and murine IL-2 receptor. Examination of serum and PBL from two dogs that were treated with hrIL-2 and human recombinant tumor necrosis factor for systemic mast cell tumors showed that in one dog, IL-2 could be measured in the serum. Concurrently, the in vitro mitogenic response of this dog's PBL to hrIL-2 occurred earlier, possibly reflecting an increase in the relative number of IL-2-responsive cells within the PBL population.
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PMID:Immunophysiological studies of interleukin-2 and canine lymphocytes. 163 72

Stimulation of the interleukin-2 (IL-2) receptor results in phosphorylation and activation of cytosolic Raf-1 serine/threonine kinase. Herein, we report that enzymatically active Raf-1 is physically associated with the IL-2 receptor beta chain (p75) in T-cell blasts. Following stimulation with IL-2, Raf-1 dissociates from the IL-2 receptor complex and translocates to the cytosol. Genistein, a protein tyrosine kinase inhibitor, prevents the dissociation of enzymatically active Raf-1 from the ligand-stimulated IL-2 receptor complex. These data favor a model of IL-2 receptor activation in which an IL-2-activated protein tyrosine kinase phosphorylates the IL-2 receptor and/or receptor-bound Raf-1. Following tyrosine phosphorylation, enzymatically active Raf-1 dissociates from the IL-2 receptor and translocates into the cytosol.
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PMID:Interleukin-2 (IL-2) induces tyrosine kinase-dependent translocation of active raf-1 from the IL-2 receptor into the cytosol. 163 73

In ten chronic uremic patients on regular hemodialysis treatment in vitro experiments revealed that stimulation of opioid receptors with morphine did not significantly change the mitogen-induced proliferative response of peripheral blood lymphocytes and interleukin-2 (IL-2) receptor expression on PHA-stimulated lymphocytes, while it appreciably decreased surface transferrin (Trf) receptor expression on PHA-stimulated lymphocytes. However, metenkephalin inhibited mitogen-induced proliferation and surface Trf receptor expression on uremic lymphocytes without affecting IL-2 receptor expression on PHA-stimulated cells. In ten healthy subjects opioid receptor agonists did not significantly affect mitogen-induced proliferation of lymphocytes, except for the inhibitory effect of 10(-8) M morphine in relation to lymphocytes stimulated with an optimal pokeweed mitogen (PWM) concentration. At the same time, opioid receptor agonists depressed surface IL-2 and Trf receptor expression on PHA-stimulated normal lymphocytes. In most of our experiments naloxone itself, a non-selective competitive opioid receptor antagonist, decreased mitogen-induced lymphocyte proliferation and IL-2 and Trf receptor expression on PHA-stimulated lymphocytes. Moreover, most frequently naloxone did not reverse inhibitory effects of opioid receptor agonists on lymphocytes. The results seem to indicate that opioid receptor stimulation by high metenkephalin concentrations, which are observed in the uremic blood plasma, may share the responsibility for immunodeficiency in chronic uremic patients. Next, in the presence of opioid receptor agonists directions of changes in the mitogen-induced proliferative response may not follow the alterations of IL-2 and Trf receptor expression on both uremic and normal lymphocytes. Finally the results also suggest that naloxone may possibly exert effects which are independent of its action on opioid receptors on lymphocytes.
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PMID:Modification of some lymphocyte functions in vitro by opioid receptor agonists and antagonist in chronic uremic patients and healthy subjects. 166 19

Northern blot analysis and a highly sensitive methodology for mRNA phenotyping, polymerase chain reaction (PCR), were used to explore the basis for the synergism between CD3/alpha beta T cell receptor (TCR) and the CD2 antigen-derived signals in promoting proliferation of T cells. Northern blotting of RNA isolated from highly purified normal human T cells revealed that crosslinking of anti-TCR-1 (a mAb directed at a framework determinant of the TCR) and OKT11 (a mAb directed at the SRBC-binding epitope of the CD2 antigen) induced the expression of the interleukin-2 gene and the gene for IL-2 receptor alpha, mRNA phenotyping by PCR revealed that crosslinkage of TCR with the CD2 antigen, and not independent crosslinking of TCR or the CD2 antigen, results in the induction of IL-2, IL-2 receptors alpha and beta, and IL-4-specific transcripts. Highly purified CD4+ T cells, as well as CD8+ T cells proliferated by crosslinking TCR with CD2 antigen. Moreover, crosslinkage of TCR with the CD2 antigen and not of either antigen with the CD4 antigen (on the surface of CD4+ T cells) or the CD8 antigen (on the surface of CD8+ T cells) resulted in marked proliferation. Our demonstration that the CD2 antigen-derived signal(s) contribute to the expression of growth promoting genes elicited via the TCR, and that the CD2 antigen is more efficient compared with the CD4 or CD8 antigen in evoking T cell proliferation, suggests that autoimmunity as well as alloimmunity might be regulated by targeting the CD2 antigen.
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PMID:The molecular basis for the synergism between the CD3/alpha beta T cell receptor and the CD2 antigen-derived signals in promoting T-cell proliferation. 167 15

It has been recently shown that severe depression is characterized by immune dysfunctions such as blunted mitogen-induced blast transformation, which is linked to interleukin-2 (IL-2) mechanisms, and to autoimmune responses. In order to explore one of the putative pathophysiological mechanisms underlying both factors, we have measured the predexamethasone and postdexamethasone serum dipeptidyl-peptidase IV (DPP IV) activity in depressed inpatients and normal controls. This enzyme is an important mediator of IL-2-related blast proliferation, and it may play a role in autoimmunity. We found significantly lower DPP IV levels in major depressives as compared with healthy controls, and melancholics exhibited significantly lower enzyme activity than minor depressives. There was a significant negative correlation between serum DPP IV activity and the severity of illness. However, we were unable to detect any significant relationships between DPP IV on the one hand, and mitogen-induced blast transformation, soluble IL-2 receptor accumulation in PHA culture supernatant, total number of leukocytes and lymphocytes, T lymphocytes, CD4+ and CD25+ cells, on the other. Men exhibited significantly higher serum DPP IV levels than women.
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PMID:Decreased serum dipeptidyl peptidase IV activity in major depression. 168 47

The phenotypic and functional nature of the lymphocytes that have been activated against autologous tumor cells and expanded in Interleukin-2 (IL-2) was studied in the context of their suitability for use in adoptive immunotherapy for cancer. While long-term co-cultures between autologous lymphocytes and tumor cells in the presence of exogenous IL-2 occasionally induced CD8+ cytolytic T cells, a substantial majority of such co-cultures generated predominantly CD4+ non-cytolytic or poorly cytolytic effector cells. In addition, these CD4+ non-cytolytic effector populations, and a number of CD4+ T cell clones derived from them, behaved like functional T suppressor (Ts) cells by elaborating a factor(s) that had profound negative effect(s) on activation of fresh T cells (inhibition of IL-2 synthesis, inhibition of IL-2 receptor [IL-2]-alpha expression, and inhibition of proliferation). Accordingly, infusion of these non-cytolytic populations capable of exhibiting such regulatory properties may have a substantial negative effect on host response toward cancer.
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PMID:Suppressor function of lymphocytes activated in in vitro co-culture against autologous tumor cells and expanded in interleukin-2. 168 55

IL-2 receptor positive T-cells from leukocyte-infiltrated pancreatic islets of diabetes prone or acutely diabetic NOD mice were propagated in vitro by culture in interleukin-2 containing medium. Of 13 lines obtained after limiting dilution all were positive for the T-cell marker Thy-1 and for CD8. Considerable heterogeneity in T-cell receptor usage was noted. Seven lines expressed T-cell receptors using V beta 8, one line was positive for V beta 5 and two lines expressed a non V beta 5, non V beta 8 receptor. Finally, two further lines lacked T-cell receptors. None of the cell lines were cytotoxic to islet cells although 10 lines showed non MHC restricted lysis of one or more tumour cells including rat insulinoma cells. We conclude that IL-2 receptor positive CD8+ T-lymphocytes from NOD islets are heterogenous with respect to V beta T-cell receptor usage. The majority of these cells are not cytotoxic to islet cells.
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PMID:Analysis of IL-2 receptor positive CD8(+)-T-lymphocytes grown from islets of NOD mice. 168 10

Recent data suggest that basophils express receptors for a variety of lymphokines. In this study we present the biochemical characterization of the interleukin-2 (IL-2) receptor on the basophil surface membrane. Highly enriched populations (purity: 92% to 99%) of blood basophils were obtained from chronic granulocytic leukemia (CGL) patients (n = 3) by negative selection using monoclonal antibodies (MoAbs) and complement. CGL basophils were found to bind CD25 MoAbs (n = 4) directed against different epitopes of the 55- to 60-Kd subunit of the IL-2 receptor (= Tac peptide). Immunoprecipitation experiments with lysates of purified CGL basophils and CD25 MoAbs showed a protein with a molecular weight of 60 Kd, equivalent to the Tac peptide on human T blasts. Quantitative binding studies and Scatchard plot analysis using radiolabeled recombinant human (rh) IL-2 indicated the presence of 12,000 +/- 4,700 low affinity IL-2 binding sites (kd = 66 nmol/L) per purified CGL basophil. Northern blot analysis with enriched CGL basophils showed two messenger RNA bands of 3.5 and 1.5 kilobases hybridizing to radiolabeled Tac cDNA. Immunoprecipitation of the Tac peptide from enriched basophils metabolically labeled with 35S-methionine showed active synthesis of the IL-2 receptor. Our results show that human blood basophils synthesize and express receptors for IL-2.
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PMID:Human blood basophils synthesize interleukin-2 binding sites. 169 35


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