Inhibition of T-cell antigen receptor-mediated transmembrane signaling by protein kinase C activation.

Abraham, Robert T.; Ho, S N; Barna, Thomas J.; Rusovick, K M; McKean, D J

doi:10.1128/mcb.8.12.5448

Cited by 39 publications

(26 citation statements)

References 16 publications

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“…While in both a murine T lymphoma line (9) and in neutrophils (7, 36) phosphorylation and down-regulation of receptors by PKC has been implicated, this observation cannot explain the effect of PMA on receptor-independent changes in [Ca 2ϩ ] i . Similarly, a reduction in IP 3 generated due to a PKCdependent phosphorylation of phospholipase C (9) fails to explain the observed reduction in release of Ca 2ϩ from internal stores following thapsigargin treatment (Fig.…”

Section: Discussionmentioning

confidence: 64%

“…It has been proposed that the decreased magnitude of agonist-stimulated changes in [Ca 2ϩ ] i after PMA pretreatment is due to a PKC-dependent phosphorylation and inactivation of phospholipase C (9). Such a phosphorylation would result in decreased production of IP 3 with a corresponding reduction in the amount of Ca 2ϩ released from the intracellular storage depot.…”

Section: Effects Of Phorbol Ester On Agonist-induced Changes Inmentioning

confidence: 99%

“…First is a PKC-mediated phosphorylation of the ␥ subunit of the TCR⅐CD3 complex and subsequent down-regulation of this complex at the surface of the cell (7,8). Second is the PKC-dependent phosphorylation of phospholipase C, with a consequent reduction in phospholipase C activity and IP 3 generation (9). Third is the phosphorylation of the plasma membrane Ca 2ϩ /ATPase, leading to its activation and a facilitation of efflux of Ca 2ϩ (10).…”

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confidence: 99%

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A Role for Protein Kinase CβI in the Regulation of Ca2+ Entry in Jurkat T Cells

Haverstick¹,

Dicus²,

Resnick³

et al. 1997

Journal of Biological Chemistry

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T cell activation leading to cytokine production and cellular proliferation involves a regulated increase and subsequent decrease in the intracellular concentration of Ca 2؉ ([Ca 2؉ ] i ). While much is understood about agonist-induced increases in [Ca 2؉ ] i , less is known about down-regulation of this pathway. Understanding the mechanism of this down-regulation is critical to the prevention of cell death that can be the consequence of a sustained elevation in [Ca 2؉ ] i . Protein kinase C (PKC), activated by the diacylglycerol produced as a consequence of T cell receptor engagement, has long been presumed to be involved in this down-regulation, although the precise mechanism is not wholly clear. In this report we demonstrate that activation of PKC by phorbol esters slightly decreases the rate of Ca 2؉ efflux from the cytosol of Jurkat T cells following stimulation through the T cell receptor or stimulation in a receptorindependent manner by thapsigargin. On the other hand, phorbol ester treatment dramatically reduces the rate of Ca 2؉ influx following stimulation. Phorbol ester treatment is without an effect on Ca 2؉ influx in a different T cell line, HSB. Down-regulation of PKC␤I expression by 18-h phorbol ester treatment is associated with a loss of the response to acute phorbol ester treatment in Jurkat cells, suggesting that PKC␤I may be the isozyme responsible for the effects on Ca 2؉ influx. Electroporation of an anti-PKC␤I antibody, but not antibodies against PKC␣ or PKC␥, led to an increase in the rate of Ca 2؉ influx following stimulation. Taken together, these data suggest that PKC␤I may be a component of the down-regulation of increases in [Ca 2؉ ] i associated with Jurkat T cell activation.Activation of T lymphocytes via stimulation through the T cell receptor for antigen (TCR) 1 leading to proliferation, cytokine production, or effector function requires a regulated increase and subsequent decrease in the intracellular concentration of Ca 2ϩ ([Ca 2ϩ ] i ). The biochemical events associated with activation of T lymphocytes and leading to Ca 2ϩ entry have been extensively studied (1). Engagement of the TCR leads to the activation of phospholipase C, which subsequently cleaves phosphatidylinositol bisphosphate into inositol 1,4,5-trisphosphate (IP 3 ) and diacylglycerol (DAG). IP 3 , binding to an intracellular receptor, induces the release of Ca 2ϩ from an intracellular storage depot (2). In a receptor-independent manner, the Ca 2ϩ /ATPase inhibitor thapsigargin (3) causes an uncompensated leak of Ca 2ϩ from this internal storage pool. In T lymphocytes, as well as in most electrically nonexcitable cells, this depletion of the intracellular storage pool induces the opening of the plasma membrane Ca 2ϩ entry pathway and permits influx of extracellular Ca 2ϩ (1). Previously, we have provided evidence that the pathway between release of intracellular Ca 2ϩ and influx of extracellular Ca 2ϩ is mediated by Ca 2ϩ -activated calmodulin (4), which permits Ca 2ϩ entry carried by a current we have called I T...

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Section: Discussionmentioning

confidence: 64%

Section: Effects Of Phorbol Ester On Agonist-induced Changes Inmentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

A Role for Protein Kinase CβI in the Regulation of Ca2+ Entry in Jurkat T Cells

Haverstick¹,

Dicus²,

Resnick³

et al. 1997

Journal of Biological Chemistry

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“…The activity of protein b a s e C is associated with the transport of this enzyme from the cytosol to the plasma membrane [24]. Abraham et al showed, however, that IL 1 does not induce this process [25]. Thus, a difference in the biology of protein kinase C in these two clones is unlikely.…”

Section: Discussionmentioning

confidence: 95%

Internalization of interleukin 1 (IL 1) correlates with IL 1‐induced IL 2 receptor expression and IL 2 secretion of EL4 thymoma cells

et al. 1989

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Center, HeidelbergThe cytokine interleukin 1 (IL 1) plays an important role in the induction of IL 2 secretion and high-affinity IL 2 receptor (IL 2R) expression by T cells. The events that follow binding of IL 1 to IL lR, however, are still unknown. In this study we describe two variants of the murine thymoma EL4 (5D3 and D6/76) that express comparable numbers of cell surface IL 1 receptors and bind IL 1 with the same affinity, but show distinct IL 1-dependent IL 2 secretion and IL 2R expression. In the presence of the tumor promoter phorbol 12-myristate 13-acetate IL 1 augments IL 2 secretion and IL 2R expression of EL4 5D3 but not of EL4 D6/76 cells. Comparison of the internalization of IL 1 by both clones revealed that EL4 D6/76 was unable to transport cell surface-bound IL 1 to the cytoplasm. These findings suggest that internalization of receptor-bound IL 1 is required for the action of this cytokine.

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“…They act through high-affinity receptors but little is known of their post-receptor mechanisms. ILl causes no change in phosphoinositide breakdown, intracellular Ca 2+ or protein kinase C translocation in a T lymphoma line [3], although it does apparently increase breakdown of phosphatidylcholine (without affecting phosphatidylinositol) in Jurkat cells [4]. ILl does not change cAMP levels in fibroblasts and chondrocytes [5].…”

Section: Introductionmentioning

confidence: 99%

Interleukin 1 and tumour necrosis factor increase phosphorylation of fibroblast proteins

Kaur

Saklatvala

1988

FEBS Letters

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Interleukin 1 (ILl) or turnout necrosis factor (TNF) stimulated phosphorylation of a triad of 27 kDa phosphoproteins (pl 6.0, 5.7 and 5.5) in human dermal fibroblasts. The change was dependent on the dose of cytokine in the range 0.1-20 ng, was detectable between 3 and 5 rain after stimulation and was maximal by I0 rain. The proteins were found in the cytosol after subeellular fractionation. The 32p was removed from them by alkali, indicating the presence of phosphoserine and/or phosphothreonine. The results suggest that early changes in serine/threonine protein kinase activity may be involved in responses of fibroblasts to IL 1 and TNF.Interleukin-1; Tumor necrosis factor; Protein phosphorylation; (Fibroblast)

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Inhibition of T-cell antigen receptor-mediated transmembrane signaling by protein kinase C activation.

Cited by 39 publications

References 16 publications

A Role for Protein Kinase CβI in the Regulation of Ca2+ Entry in Jurkat T Cells

A Role for Protein Kinase CβI in the Regulation of Ca2+ Entry in Jurkat T Cells

Internalization of interleukin 1 (IL 1) correlates with IL 1‐induced IL 2 receptor expression and IL 2 secretion of EL4 thymoma cells

Interleukin 1 and tumour necrosis factor increase phosphorylation of fibroblast proteins

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