Activation of Lyn is a common element of the stimulation of human neutrophils by soluble and particulate agonists

Gaudry, Muriel; Gilbert, Caroline; Barabé, Frédéric; Pe, Poubelle; Naccache, Paul H.

doi:10.1182/blood.v86.9.3567.bloodjournal8693567

Cited by 64 publications

(22 citation statements)

References 66 publications

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“…Activation of plasma membrane heterotrimeric G proteins, of protein kinase C (PKC), and of Src family kinases is among a variety of the known crystal-induced upstream signals potentially able to promote rapid acti-vation of ERK-1/ERK-2 (1,13,(23)(24)(25)(26)50). Significantly, hydroxyapatite crystal-induced and triclinic CPPD crystal-induced ERK-1/ERK-2 activation mediates crystal-induced mitogenesis in foreskin fibroblasts (30).…”

Section: Discussionmentioning

confidence: 99%

“…Inflammatory crystals, like growth factors, activate multiple transduction pathways, including heterotrimeric and ras superfamily G proteins, phospholipases A 2 , C, and D, the Src family tyrosine kinases, and NADPH oxidase (1,(23)(24)(25)(26)(27)(28)(29). MAPK activation has been documented in certain cell types in the context of crystal-induced signal transduction, and a role demonstrated for certain cell functions.…”

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confidence: 99%

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Extracellular signal–regulated kinase 1/extracellular signal–regulated kinase 2 mitogen-activated protein kinase signaling and activation of activator protein 1 and nuclear factor κB transcription factors play central roles in interleukin-8 expression stimulated by monosodium urate monohydrate and calcium pyrophosphate crystals in monocytic cells

Liu

O’Connell

Johnson

et al. 2000

Arthritis & Rheumatism

110

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Objective. Monosodium urate monohydrate (MSU) and calcium pyrophosphate dihydrate (CPPD) crystals cause acute gout and pseudogout, respectively. Because acute gout and pseudogout appear to be dependent on interleukin-8 (IL-8)-induced neutrophil in-gress, this study was undertaken to define and compare how MSU and CPPD crystals stimulate IL-8 messenger RNA (mRNA) expression in mononuclear phagocytes. Methods. MSU and CPPD crystal-induced mitogen-activated protein kinase (MAPK) signal trans-duction and IL-8 transcriptional activation were studied in human monocytic cells, using the THP-1 cell line. Results. MSU and CPPD crystals (0.5 mg/ml) induced activation of c-Jun N-terminal kinase, extracel-lular signal-regulated kinase 1 (ERK-1)/ERK-2, and p38 MAPK pathways in THP-1 cells. Activation of the ERK-1/ERK-2 pathway was essential for MSU and CPPD crystal-induced IL-8 mRNA expression, whereas the p38 pathway played a greater role in IL-8 mRNA expression in response to CPPD crystals in comparison with MSU crystals. Both crystals induced the binding of nuclear factor B (NF-B), including the NF-B complex c-Rel/RelA, and activator protein 1 (AP-1, including N-terminal phosphorylated c-Jun) to the IL-8 promoter. Both crystals induced transcriptional activation of the IL-8 promoter, which was dependent on activation of c-Rel/RelA and AP-1. Activation of the NF-IL-6 transcription factor played a lesser role. Finally, crystal-induced IL-8 promoter activation was mediated by activation of the ERK-1/ERK-2 pathway, as demonstrated by transfection of dominant-negative raf-1. Conclusion. These results indicate that ERK-1/ ERK-2 signaling and transcriptional activation through AP-1 and NF-B are essential for the induction of IL-8 expression in mononuclear phagocytes in response to CPPD and MSU crystals.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Extracellular signal–regulated kinase 1/extracellular signal–regulated kinase 2 mitogen-activated protein kinase signaling and activation of activator protein 1 and nuclear factor κB transcription factors play central roles in interleukin-8 expression stimulated by monosodium urate monohydrate and calcium pyrophosphate crystals in monocytic cells

Liu

O’Connell

Johnson

et al. 2000

Arthritis & Rheumatism

110

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“…We highlight here several of the most reported ones. Src family kinase member Lyn is activated in human neutrophils by MSU crystals (62). Using the human monocytic cell line THP-1, Liu et al (21) reported that MSU stimulation led to the activation of c-Src, Lyn, Hck, and Fyn, as well as serine ⁄ threonine kinase p70s6k.…”

Section: Other Kinasesmentioning

confidence: 99%

Monosodium urate crystals in inflammation and immunity

Shi¹,

Mucsi²,

Ng³

2009

Immunological Reviews

131

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Uric acid crystals [monosodium urate (MSU)] have emerged as an important factor for both gouty arthritis and immune regulation. This simple crystalline structure appears to activate innate host defense mechanisms in multiple ways and triggers robust inflammation and immune activation. The recognition mechanisms of MSU following its phase change from soluble uric acid are diverse, involving both protein receptors and non-specific plasma membrane attachment. Upon contact with host cells, MSU induces a set of membrane events that trigger Syk and PI3K activation, phagocytosis, and cytokine production. Having entered the cell, MSU further triggers NALP3 inflammasome activation and induces the production of IL-1 beta, likely inducing a full spectrum of inflammation. This review describes the recognition mechanisms and activation pathways involved in MSU-mediated inflammation and adjuvanticity and hypothesizes that direct membrane binding by solid surfaces, such as MSU, may function as a generic mechanism in tissue responses to particulate and crystalline structures.

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“…The non-receptor tyrosine kinases Fgr [36], Hck [37], Syk [38], and Lyn [39] have been shown to be activated by fMLP. Vanadate has also been shown to activate Btk, Hck, and Syk [40].…”

Section: Discussionmentioning

confidence: 99%

Tyrosine kinase-regulated small GTPase translocation and the activation of phospholipase D in HL60 granulocytes

Houle

Naccache

Bourgoin

1999

Journal of Leukocyte Biology

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We focus on the mechanisms of regulation of phospholipase D (PLD) activity. Three agonists known to stimulate PLD activity, fMet-LeuPhe (fMLP), phorbol 12-myristate 13-acetate (PMA) and V 4؉ -OOH, induced a differential translocation of ADP-ribosylation factor (ARF), RhoA, and protein kinase C␣ (PKC␣), all cofactors for PLD activation. Whereas fMLP recruited all three proteins to membranes, V 4؉ -OOH only elicited RhoA translocation and PMA induced ARF and PKC␣ translocation. Three tyrosine kinases inhibitors, ST-638, methyl 2,5-dihydroxycinnamate, and genistein reduced fMLP-stimulated PLD activity by up to 80%. Furthermore, tyrosine kinase inhibitors reduced the fMLP-induced increase of GTP␥S-stimulated PLD activity in membranes and recruitment of ARF, RhoA, and PKC␣ to the membrane fraction. The data suggest that a tyrosine phosphorylation event is located upstream of the translocation of ARF, RhoA, and PKC␣ in the signaling pathway leading to PLD activation by fMLP. RO 31-8220, a specific inhibitor of PKC, reduced PMA-induced PLD activity by 80% in intact HL60 granulocytes but enhanced fMLP-stimulated PLD activity by 60%. Although PMA alone had no effect on RhoA recruitment to the membrane fraction, in the presence of RO 31-8220 the levels of membrane-bound RhoA were increased. The levels of membrane-bound ARF and PKC␣ were unaffected by RO 31-8220 during PMA stimulation. In contrast, fMLP-induced recruitment of ARF and RhoA was insensitive to RO 31-8220 but PKC␣ translocation was increased. We propose that RhoA translocation may be regulated by PKC in an ATPindependent manner. Furthermore, increased fMLP-induced PKC␣ translocation in the presence of RO 31-8220 may partially account for the synergistic activation of PLD observed when both fMLP and RO 31-8220 are used together in intact HL60 cells.

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Activation of Lyn is a common element of the stimulation of human neutrophils by soluble and particulate agonists

Cited by 64 publications

References 66 publications

Monosodium urate crystals in inflammation and immunity

Tyrosine kinase-regulated small GTPase translocation and the activation of phospholipase D in HL60 granulocytes

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