Protein Kinases in Neutrophils: A Review

Huang, Chi‐Kuang

doi:10.3109/09687688909082261

Cited by 34 publications

(5 citation statements)

References 99 publications

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“…5a). The reasons for this remain unclear, however, others have reported difficulty in demonstrating membrane-associated tyrosine kinases in neutrophils [40], suggesting that the complexes may not survive the extraction procedures used, perhaps due to release of hydrolytic enzymes during solubilization. An alternative possibility is that the complexes in neutrophils are very large, as suggested by the markedly granular staining pattern shown in Fig.…”

Section: Discussionmentioning

confidence: 94%

Cross‐linking of CD59 and of other glycosyl phosphatidylinositol‐anchored molecules on neutrophils triggers cell activation via tyrosine kinase

et al. 1993

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Many membrane proteins are attached via a glycosyl phosphatidylinositol (GPI) anchor. Proteins anchored in this way make no direct contact with the interior of the cell, therefore a role in signaling or activation would seem unlikely. Nevertheless, cross-linking of GPI-anchored proteins on human and murine T lymphocytes has been shown to cause calcium transients and cell activation. Our studies address the non-lethal events caused by the membrane attack complex of complement, which include release of Ca2+ from intracellular stores, and have suggested that the GPI-anchored complement inhibitor CD59 may be involved in signaling these events. We here report that cross-linking of CD59 on human neutrophils using specific monoclonal antibody and second antibody caused a rapid increase in intracellular free Ca2+ concentration (Ca2+ transient) due to release of Ca2+ from stores and also caused neutrophil oxidase activation. All antibodies against CD59 tested were effective and cross-linking of any other GPI-anchored protein expressed on neutrophils also initiated an increase in intracellular free Ca2+ concentration, whereas cross-linking of transmembrane proteins caused little or no response. A tyrosine kinase-dependent activation pathway was indicated by the demonstration of tyrosine phosphorylation on cross-linking and by blocking of the Ca2+ transient with the tyrosine kinase inhibitor herbimycin.

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Section: Discussionmentioning

confidence: 94%

Cross‐linking of CD59 and of other glycosyl phosphatidylinositol‐anchored molecules on neutrophils triggers cell activation via tyrosine kinase

et al. 1993

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“…Neutrophils generally have higher mobility than the other phagocytes, including both monocytes and macrophages (18). It has also been shown that when engulfing untargeted microparticles, the cellular pedestal of the neutrophils goes through protrusion in the direction of the target in the initial phases of phagocytosis, which shows their capability for remodeling their actin network during phagocytosis (37,38). The amount of cortical tension and viscosity is an order of magnitude higher for macrophages compared with neutrophils.…”

Section: Discussionmentioning

confidence: 99%

Neutrophils preferentially phagocytose elongated particles—An opportunity for selective targeting in acute inflammatory diseases

et al. 2020

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Polymeric particles have recently been used to modulate the behavior of immune cells in the treatment of various inflammatory conditions. However, there is little understanding of how physical particle parameters affect their specific interaction with different leukocyte subtypes. While particle shape is known to be a crucial factor in their phagocytosis by macrophages, where elongated particles are reported to experience reduced uptake, it remains unclear how shape influences phagocytosis by circulating phagocytes, including neutrophils that are the most abundant leukocyte in human blood. In this study, we investigated the phagocytosis of rod-shaped polymeric particles by human neutrophils relative to other leukocytes. In contrast to macrophages and other mononuclear phagocytes, neutrophils were found to exhibit increased internalization of rods in ex vivo and in vivo experimentation. This result suggests that alteration of particle shape can be used to selectively target neutrophils in inflammatory pathologies where these cells play a substantial role.

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“…The involvement of PKC in the mechanisms underlying neutrophil stimulation by a variety of agonists (although not by MSU crystals) had been suggested by numerous studies based on pharmacological and biochemical approaches. PKC activators such as PMA, mezerein, bryostatin, and synthetic diacylglycerols potently stimulate the production of toxic oxygen metabolites and exocytosis, effects that can be prevented by PKC inhibitors (52)(53)(54). Despite the central role described for PKC in signal transduction, very little, if anything, is known about their participation in signaling pathways activated by MSU crystals in human neutrophils.…”

Section: Discussionmentioning

confidence: 99%

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

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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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Protein Kinases in Neutrophils: A Review

Cited by 34 publications

References 99 publications

Cross‐linking of CD59 and of other glycosyl phosphatidylinositol‐anchored molecules on neutrophils triggers cell activation via tyrosine kinase

Cross‐linking of CD59 and of other glycosyl phosphatidylinositol‐anchored molecules on neutrophils triggers cell activation via tyrosine kinase

Neutrophils preferentially phagocytose elongated particles—An opportunity for selective targeting in acute inflammatory diseases

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

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