Involvement of BLT1 Endocytosis and Yes Kinase Activation in Leukotriene B4-Induced Neutrophil Degranulation

Gaudreault, Éric; Thompson, C. S.; Staňková, Jana; Rola‐Pleszczynski, Marek

doi:10.4049/jimmunol.174.6.3617

Cited by 50 publications

(37 citation statements)

References 61 publications

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“…Degranulation of PLB-985 cells has been studied in a fragmentary way. Primary granule exocytosis was reported in DMF-and DMSO-differentiated cells by analyzing the release of b-glucuronidase or b-hexosaminidase after stimulation with fMLF or LTB 4, respectively (Gaudreault et al, 2005;Kaldi et al, 2003). Pedruzzi et al (2002) described the functional degranulation of specific granules and secretory vesicles in DMF-induced PLB-985 cells, by analysing the fMLFinduced increase in cell-surface expression of CD11b and CD35.…”

Section: Article In Pressmentioning

confidence: 98%

Characterisation of degranulation and phagocytic capacity of a human neutrophilic cellular model, PLB-985 cells☆

et al. 2010

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Section: Article In Pressmentioning

confidence: 98%

Characterisation of degranulation and phagocytic capacity of a human neutrophilic cellular model, PLB-985 cells☆

et al. 2010

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“…A number of signaling pathways, including those containing p38 MAPK, PI3K, and nonreceptor tyrosine kinases, regulate exocytosis in human neutrophils (17,37,55,58). To evaluate the role of these and other kinases in clathrin-mediated endocytosis, neutrophils were pretreated with pharmacological inhibitors of various kinases before measurements of fMLP-stimulated transferrin uptake.…”

Section: Clathrin-mediated Endocytosis Regulates Neutrophil Granule Ementioning

confidence: 99%

Counterregulation of clathrin-mediated endocytosis by the actin and microtubular cytoskeleton in human neutrophils

Uriarte¹,

Jog²,

Luerman³

et al. 2009

American Journal of Physiology-Cell Physiology

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We have recently reported that disruption of the actin cytoskeleton enhanced N-formylmethionyl-leucyl-phenylalanine (fMLP)-stimulated granule exocytosis in human neutrophils but decreased plasma membrane expression of complement receptor 1 (CR1), a marker of secretory vesicles. The present study was initiated to determine if reduced CR1 expression was due to fMLP-stimulated endocytosis, to determine the mechanism of this endocytosis, and to examine its impact on neutrophil functional responses. Stimulation of neutrophils with fMLP or ionomycin in the presence of latrunculin A resulted in the uptake of Alexa fluor 488-labeled albumin and transferrin and reduced plasma membrane expression of CR1. These effects were prevented by preincubation of the cells with sucrose, chlorpromazine, or monodansylcadaverine (MDC), inhibitors of clathrin-mediated endocytosis. Sucrose, chlorpromazine, and MDC also significantly inhibited fMLP- and ionomycin-stimulated specific and azurophil granule exocytosis. Disruption of microtubules with nocodazole inhibited endocytosis and azurophil granule exocytosis stimulated by fMLP in the presence of latrunculin A. Pharmacological inhibition of phosphatidylinositol 3-kinase, ERK1/2, and PKC significantly reduced fMLP-stimulated transferrin uptake in the presence of latrunculin A. Blockade of clathrin-mediated endocytosis had no significant effect on fMLP-stimulated phosphorylation of ERK1/2 in neutrophils pretreated with latrunculin A. From these data, we conclude that the actin cytoskeleton functions to limit microtubule-dependent, clathrin-mediated endocytosis in stimulated human neutrophils. The limitation of clathrin-mediated endocytosis by actin regulates the extent of both specific and azurophilic granule exocytosis.

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“…The method of Gaudreault et al (2005) was followed to assess secretion of β-hexosaminidase from neutrophil primary granules. The extent of lactoferrin secretion from secondary granules was performed as we described previously (Rosales and Ernst, 1997).…”

Section: Lactoferrin and β-Hexosaminidase Secretion Assaysmentioning

confidence: 99%

Cdk5 mediates vimentin ser56 phosphorylation during GTP‐induced secretion by neutrophils

Lee

Liu

Jin

et al. 2011

Journal Cellular Physiology

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Secretion by neutrophils contributes to acute inflammation following injury or infection. Vimentin has been shown to be important for secretion by neutrophils but little is known about its dynamics during secretion, which is regulated by cyclin-dependent kinase 5 (Cdk5). In this study, we sought to examine the vimentin dynamics and its potential regulation by Cdk5 during neutrophil secretion. We show that vimentin is a Cdk5 substrate that is specifically phosphorylated at Ser56. In response to neutrophil stimulation with GTP, vimentin Ser56 was phosphorylated and colocalized with Cdk5 in the cytoplasmic compartment. Vimentin pSer56 and Cdk5 colocalization was consistent with coimmunoprecipitation from stimulated cells. Vimentin Ser56 phosphorylation occurred immediately after stimulation, and a remarkable increase in phosphorylation was noted later in the secretory process. Decreased GTP-induced vimentin Ser56 phosphorylation and secretion resulted from inhibition of Cdk5 activity by roscovitine or olomoucine or by depletion of Cdk5 by siRNA, suggesting that GTP-induced Cdk5-mediated vimentinSer56 phosphorylation may be related to GTP-inducedCdk5-mediated secretion by neutrophils. Indeed, inhibition of vimentin Ser56 phosphorylation led to a corresponding inhibition of GTP-induced secretion, indicating a link between these two events. While fMLP also induced vimentin Ser56 phosphorylation, such phosphorylation was unaffected by roscovitine, which nonetheless, inhibited secretion, suggesting that Cdk5 regulates fMLP-induced secretion via a mechanism independent of Cdk5-mediated vimentin Ser56 phosphorylation. These findings demonstrate the distinct involvement of Cdk5 in GTP-and fMLP-induced secretion by neutrophils, and support the notion that specific targeting of Cdk5 may serve to inhibit the neutrophil secretory process.The neutrophil is the first cell type recruited to a site of infection or inflammation. One of the mechanisms used by the neutrophil to destroy infectious agents or to mediate the inflammatory process in a variety of clinical scenarios is to secrete its granule contents. Regulation of secretion from the neutrophil is key to the balance between host defense and tissue injury (Nathan, 2006 CIHR Author ManuscriptCIHR Author Manuscript CIHR Author Manuscript independent GTP-regulated mechanism of secretion in neutrophils (Rosales and Ernst, 2000). Other nucleotide-mediated mechanisms of activation in neutrophils such as adenosine-5′-triphosphate (ATP)-and uridine-5′-triphosphate (UTP)-induced stimulation have been shown to be regulated by protein kinases, including the p38 mitogen-activated protein kinase (p38MAPK) and the extracellular signal-regulated kinase (ERK1/2) (Meshki et al., 2004). Our studies showed that GTP-dependent secretion from neutrophils is mediated by cyclin-dependent kinase 5 (Cdk5) (Rosales et al., 2004a). However, the mechanisms underlying this process remain to be investigated.Cdk5, a small proline-directed serine/threonine kinase, has close structural homology with...

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Involvement of BLT1 Endocytosis and Yes Kinase Activation in Leukotriene B4-Induced Neutrophil Degranulation

Cited by 50 publications

References 61 publications

Characterisation of degranulation and phagocytic capacity of a human neutrophilic cellular model, PLB-985 cells☆

Characterisation of degranulation and phagocytic capacity of a human neutrophilic cellular model, PLB-985 cells☆

Counterregulation of clathrin-mediated endocytosis by the actin and microtubular cytoskeleton in human neutrophils

Cdk5 mediates vimentin ser56 phosphorylation during GTP‐induced secretion by neutrophils

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