A comparison of post‐receptor signal transduction events in Jurkat cells transfected with either IL‐8R1 or IL‐8R2 Chemokine mediated activation of p42/p44 MAP‐kinase (ERK‐2)

Jones, Simon A.; Moser, Bernhard; Thelen, Marcus

doi:10.1016/0014-5793(95)00397-r

Cited by 105 publications

(16 citation statements)

References 38 publications

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“…Therefore, we investigated whether SDF-1 causes protracted activation of other intracellular signal transduction pathways. Previous studies demonstrated that the MAP kinase kinase cascade leading to the activation of ERK-2 is regulated independently of protein kinase B 28, and chemokines were shown to stimulate ERK-2 activity in Jurkat cells 12. Using the same panel of chemokines, we compared the activation of ERK-2 in T cells.…”

Section: Resultsmentioning

confidence: 99%

“…Signal transduction by chemokine receptors leads to the activation of G proteins and phospholipase C and the elevation of cytosolic free calcium 2. We and others have shown that stimulation of chemokine receptors results in the transient activation of the mitogen-activated protein (MAP) kinase extracellular signal–regulated kinase (ERK)-2 121314. Activation of ERK-2 is Ras dependent, and prolonged activation causes its nuclear translocation and activation of transcription 15.…”

Section: Introductionmentioning

confidence: 99%

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Signal Transduction by Cxc Chemokine Receptor 4

Tilton

Oberlin

et al. 2000

The Journal of Experimental Medicine

197

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We report that stromal cell–derived factor (SDF)-1 has the remarkable capacity to induce sustained signaling through CXC chemokine receptor 4 (CXCR4). In contrast to other chemokines, such as monocyte chemotactic protein 1 (CC chemokine receptor 2 [CCR2]), macrophage inflammatory protein 1β (CCR5), liver and activation-regulated chemokine (LARC [CCR6]), Epstein-Barr virus–induced molecule 1 ligand chemokine (ELC [CCR7]), and IP10 (CXCR3), SDF-1 stimulates the prolonged activation of protein kinase B and extracellular signal–regulated kinase (ERK)-2. Activation of protein kinase B is reversed by displacement of SDF-1 from CXCR4 or inhibition of phosphatidylinositol 3-kinase. Although increasing concentrations of SDF-1 enhance CXCR4 internalization, kinase activation is prolonged. In addition, restimulation yields >60% of initial protein kinase B activity, indicating that the remaining receptors are not desensitized. Furthermore, activation is prolonged by inhibiting SDF-1 degradation. The sustained activation of cell survival and mitogenic pathways may account for the unique role of SDF-1 and CXCR4 in embryogenesis and lymphopoiesis.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Signal Transduction by Cxc Chemokine Receptor 4

Tilton

Oberlin

et al. 2000

The Journal of Experimental Medicine

197

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“…The functional role of this ELR motif is to confer angiogenic activity to the ELR-containing chemokine (424) and this motif is important for ligand-receptor binding interactions on neutrophils (425, 426). Ligand binding to CXCR1 and CXCR2 causes degranulation, intracellular calcium mobilization, and phosphorylation of MAP-kinase (427). …”

Section: The Chemokinesmentioning

confidence: 99%

Cytokines and Chemokines inMycobacterium tuberculosisInfection

et al. 2016

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Chemokines and cytokines are critical for initiating and coordinating the organized and sequential recruitment and activation of cells into Mycobacterium tuberculosis -infected lungs. Correct mononuclear cellular recruitment and localization are essential to ensure control of bacterial growth without the development of diffuse and damaging granulocytic inflammation. An important block to our understanding of TB pathogenesis lies in dissecting the critical aspects of the cytokine/chemokine interplay in light of the conditional role these molecules play throughout infection and disease development. Much of the data highlighted in this review appears at first glance to be contradictory, but it is the balance between the cytokines and chemokines that is critical, and the “goldilocks” (not too much and not too little) phenomenon is paramount in any discussion of the role of these molecules in TB. Determination of how the key chemokines/cytokines and their receptors are balanced and how the loss of that balance can promote disease is vital to understanding TB pathogenesis and to identifying novel therapies for effective eradication of this disease.

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“…2 A). Although ERK activation can be induced by homeostatic CXCL12 in B lymphocytes [40] and CXCL8 in T cell lines [41], this may differ in the case of primary Th1 lymphocytes because signaling pathways vary in terms of the cell type, ligands, receptors and kinetics involved. Additionally, the diverse chemokine receptor profiles expressed by different T cell subpopulations, such as antigen-experienced resting T lymphocytes and naïve or recently activated T lymphocytes [32], most likely influence signaling pathways differently.…”

Section: Discussionmentioning

confidence: 99%

Migration of Th1 Lymphocytes Is Regulated by CD152 (CTLA-4)-Mediated Signaling via PI3 Kinase-Dependent Akt Activation

Knieke¹,

Lingel²,

Chamaon³

et al. 2012

PLoS ONE

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Efficient adaptive immune responses require the localization of T lymphocytes in secondary lymphoid organs and inflamed tissues. To achieve correct localization of T lymphocytes, the migration of these cells is initiated and directed by adhesion molecules and chemokines. It has recently been shown that the inhibitory surface molecule CD152 (CTLA-4) initiates Th cell migration, but the molecular mechanism underlying this effect remains to be elucidated. Using CD4 T lymphocytes derived from OVA-specific TCR transgenic CD152-deficient and CD152-competent mice, we demonstrate that chemokine-triggered signal transduction is differentially regulated by CD152 via phosphoinositide 3-kinase (PI3K)-dependent activation of protein kinase B (PKB/Akt). In the presence of CD152 signaling, the chemoattractant CCL4 selectively induces the full activation of Akt via phosphorylation at threonine 308 and serine 473 in pro-inflammatory Th lymphocytes expressing the cognate chemokine receptor CCR5. Akt signals lead to cytoskeleton rearrangements, which are indispensable for migration. Therefore, this novel Akt-modulating function of CD152 signals affecting T cell migration demonstrates that boosting CD152 or its down-stream signal transduction could aid therapies aimed at sensitizing T lymphocytes for optimal migration, thus contributing to a precise and effective immune response.

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A comparison of post‐receptor signal transduction events in Jurkat cells transfected with either IL‐8R1 or IL‐8R2 Chemokine mediated activation of p42/p44 MAP‐kinase (ERK‐2)

Cited by 105 publications

References 38 publications

Signal Transduction by Cxc Chemokine Receptor 4

Signal Transduction by Cxc Chemokine Receptor 4

Cytokines and Chemokines inMycobacterium tuberculosisInfection

Migration of Th1 Lymphocytes Is Regulated by CD152 (CTLA-4)-Mediated Signaling via PI3 Kinase-Dependent Akt Activation

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