Crystal-induced neutrophil activation. IX. Syk-dependent activation of class Ia phosphatidylinositol 3-kinase

Popa-Nita, Oana; Rollet-Labelle, Emmanuelle; Thibault, Nathalie; Gilbert, Caroline; Bourgoin, Sylvain G.; Naccache, Paul H.

doi:10.1189/jlb.0307174

Cited by 43 publications

(52 citation statements)

References 49 publications

(67 reference statements)

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“…A recent study from our laboratory showed that Syk mediated the MSU crystal-induced activation of class Ia PI3Ks by directly interacting with their regulatory subunit, p85 (39). This interaction was necessary to the subsequent serine/threonine phosphorylation of AKT, a major target of PI3Ks.…”

Section: The Syk-dependent Activation Of Pi3ks By Msu Crystals Dependmentioning

confidence: 99%

“…and the morphological changes in neutrophils characteristic of crystal internalization (47). Syk also mediates the activation of class Ia PI3Ks and regulates several MSU crystal-stimulated neutrophil functions such as degranulation (39). The regulation of the tyrosine phosphorylation cascade initiated by MSU crystals by the serine/threonine kinases of the PKC family (Fig.…”

Section: Syk Is a Substrate Of Pkc In Human Neutrophils Stimulated Bymentioning

confidence: 99%

“…We have recently shown that MSU crystals induce a significant degranulation of human neutrophils (39). We next monitored the potential effect of the pharmacological inhibitor of classical PKC, Gö 6976 (40), on the degranulation of the four types of neutrophil granules induced by MSU crystals.…”

Section: The Degranulation Of Human Neutrophils Induced By Msu Crystamentioning

confidence: 99%

“…We therefore examined the effect of the pharmacological inhibition of classical PKC (using Gö 6976) on the MSU crystalinduced interaction between Syk and p85 (39). Neutrophils were preincubated with Gö 6976 or with its vehicle, Me 2 SO and then stimulated with MSU crystals for the indicated periods of time.…”

Section: The Syk-dependent Activation Of Pi3ks By Msu Crystals Dependmentioning

confidence: 99%

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Crystal-Induced Neutrophil Activation: XI. Implication and Novel Roles of Classical Protein Kinase C

Popa-Nita

Proulx

Paré

et al. 2009

The Journal of Immunology

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Monosodium urate (MSU) crystals are among the most potent proinflammatory stimuli, and an innate immune inflammatory response to the crystal surface is involved in the pathology of gouty arthritis. Furthermore, MSU crystals have recently been identified as danger signals able to induce the maturation of dendritic cells. Release of the crystals into the joint cavity promotes an acute inflammation characterized by a massive infiltration of neutrophils that leads to tissue damage. Protein kinase C (PKC) represents a family of serine/threonine kinases that play central signaling roles in multiple cellular responses. This family of kinases is divided into three subfamilies based on second messenger requirements: conventional (or classical), novel, and atypical. Despite their role in signal transduction, very little is known about the involvement of the PKC family in the inflammatory reaction induced by MSU crystals. In the present study, we show that MSU crystals activate conventional PKC isoforms, and that this activation is necessary for the MSU crystal-induced degranulation and generation of a chemotactic activity in the supernatants of MSU crystal-stimulated human neutrophils. Evidence is also obtained that the tyrosine kinase Syk is a substrate of PKC and that the PKC-mediated serine phosphorylation of Syk is necessary to its interaction with the regulatory subunit of PI3K kinases (p85) and thus to the subsequent activation of these lipid kinases. These results suggest novel means of modulating neutrophil responses (through the specific regulation of PKC) during the acute phase of MSU crystal-induced inflammation.

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Section: The Syk-dependent Activation Of Pi3ks By Msu Crystals Dependmentioning

confidence: 99%

Section: Syk Is a Substrate Of Pkc In Human Neutrophils Stimulated Bymentioning

confidence: 99%

Section: The Degranulation Of Human Neutrophils Induced By Msu Crystamentioning

confidence: 99%

Section: The Syk-dependent Activation Of Pi3ks By Msu Crystals Dependmentioning

confidence: 99%

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Crystal-Induced Neutrophil Activation: XI. Implication and Novel Roles of Classical Protein Kinase C

Popa-Nita

Proulx

Paré

et al. 2009

The Journal of Immunology

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“…28 To investigate the role of this important cellular sensor, 2 selective pharmacologic inhibitors of PI3K, namely wortmannin and LY294002, were used before pulsing cells with HIV-1. No modulation of virus binding/entry was observed when using both compounds ( Figure 3F for wortmannin and data not shown for LY294002).…”

Section: Src and Syk Family Members Are Involved In The Hiv-1-mediatementioning

confidence: 99%

DCIR-mediated enhancement of HIV-1 infection requires the ITIM-associated signal transduction pathway

Lambert

Barabé

Gilbert

et al. 2011

Blood

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Dendritic cell immunoreceptor (DCIR) is IntroductionIt is known that cell-free virions do not efficiently cross genital epithelial cells. Instead HIV-1 uses primarily dendritic cells (DCs) to penetrate the mucosal epithelium. 1,2 The virus is then transferred and disseminated from this entry site to T-cell zones in secondary lymphoid organs, where it can productively infect residing CD4 ϩ T cells. The infection process causes a marked depletion of CD4 ϩ T cells, 3 progressive impairment of the immune system, as well as chronic hyperactivation of both CD4 ϩ and CD8 ϩ T cells. 4 The initial attachment step of HIV-1 to DCs may occur through several complex interactions between the virus and the target cell surface (reviewed in Clapham and McKnight 5 and in Ugolini et al 6 ) such as the association between the oligosaccharides found on the external envelope glycoprotein gp120 and the mannose receptor (CD206), langerin (CD207), or 8 This will result in virus capture and transmission to CD4 ϩ T cells in an effective trans mode 9 (ie, transfer of virions bound onto DCs and/or localized in endosomes). Another lectin receptor, that is, the dendritic cell immunoreceptor (DCIR), can behave as an HIV-1 attachment factor for HIV-1 to participate actively in trans infection of CD4 ϩ T cells. 10 DCIR also contributes to cis-infection events, that is, infection of surrounding CD4 ϩ T cells by virions produced by DCs productively infected with HIV-1. 10 DCIR is a member of a recently described family of C-type lectin receptors (CLRs), which includes DCAR, dectin-2, BDCA-2, MCL, and MINCLE. These receptors carry a single carbohydrate recognition domain (CRD) at the COOH terminal and generally lack consensus signaling motifs in their cytoplasmic region. 11 Several members of the family, however, possess a positively charged residue in their transmembrane region, via which they associate with immunoreceptor tyrosine-based activation motif (ITAM)-containing adaptor molecules, such as the Fc receptor ␥ chains. Importantly, DCIR is the only family member harboring an immunoreceptor tyrosine-based inhibitory motif (ITIM), which is involved in modulation of cellular responses. 12 DCIR is expressed on the surface of most antigen-presenting cells (ie DCs, monocytes, macrophages, and B cells), as well as on granulocytes, and it is differentially expressed depending on the DC maturation status. 13 Lipopolysaccharide, IL-4, and TNF-␣ down-regulate DCIR expression on neutrophils. 14 The ITIM domain of DCIR contains the consensus sequence S/I/V/LxYxxI/V/L, including a tyrosine residue at position 7 (ie, ITYAEV). 13 Generally, when ITIM-containing receptors are engaged, they become tyrosine-phosphorylated and then transmit signals by binding and activating Src homology-2 domain (SH2)-containing tyrosine phosphatases (eg, SHP-1 and SHP-2) and/or the SH2-containing tyrosine inositol phosphate (SHIP). 15 In the case of DCIR, one study has demonstrated that, when phosphorylated, it recruits both SHP-1 and SHP-2. 16 Nevertheless, there is still no e...

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Platelets are recruited to hepatocellular carcinoma tissues in a CX3CL1‐CX3CR1 dependent manner and induce tumour cell apoptosis

Miao

Liu

et al. 2020

Molecular Oncology

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The mechanisms and biological functions of migrating platelets in cancer remain largely unknown. Here, we analyzed platelet infiltration in hepatocellular carcinoma. We detected platelet extravasation in both mouse and human HCC tissues. CX3CL1 directly induced platelet migration, and hypoxia enhanced platelet migration by upregulating CX3CL1 expression. Knocking down CX3CL1 in HCC cells reduced platelet migration in vitro, as well as infiltration of HCC tissue in an orthotopic HCC mouse model. Components of the CX3CR1/Syk/PI3K pathway were essential for CX3CL1-induced platelet migration. Migrating platelets induced HCC cell apoptosis in vitro, as indicated by a reduced mitochondrial membrane potential and an increased percentage of apoptotic cells. In the orthotopic tumor implantation model, decreased platelet infiltration was associated with accelerated tumor growth. Taken together, our findings indicate that HCC cell-derived CX3CL1 contributes to tumor infiltration by platelets, which in turn promotes apoptosis of HCC cells.

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Crystal-induced neutrophil activation. IX. Syk-dependent activation of class Ia phosphatidylinositol 3-kinase

Cited by 43 publications

References 49 publications

Crystal-Induced Neutrophil Activation: XI. Implication and Novel Roles of Classical Protein Kinase C

Crystal-Induced Neutrophil Activation: XI. Implication and Novel Roles of Classical Protein Kinase C

DCIR-mediated enhancement of HIV-1 infection requires the ITIM-associated signal transduction pathway

Platelets are recruited to hepatocellular carcinoma tissues in a CX3CL1‐CX3CR1 dependent manner and induce tumour cell apoptosis

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