Redistribution of Protein Kinase C Isoforms in Human Neutrophils Stimulated by Formyl Peptides and Phorbol-Myristate Acetate

Dang, Pham My-Chan; Rais, Samira; Hakim, Jacques; Périanin, Axel

doi:10.1006/bbrc.1995.2020

Cited by 52 publications

(30 citation statements)

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“…1A). As expected, PMA greatly decreased the kinase activity of cytosolic PKC in accord with the already described irreversible translocation of PKC induced by this stimulus (34).…”

Section: Src Kinase-dependent Activation Of Classical Pkc Isoforms Bysupporting

confidence: 87%

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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“…1A). As expected, PMA greatly decreased the kinase activity of cytosolic PKC in accord with the already described irreversible translocation of PKC induced by this stimulus (34).…”

Section: Src Kinase-dependent Activation Of Classical Pkc Isoforms Bysupporting

confidence: 87%

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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“…PKC in PMN-PMN express ␣, ␤ I , ␤ II , ␦, and but not several other PKC isoforms (25,29,30,(43)(44)(45)(46)(47)(48)(49). We confirmed that PMN contain the former but lack ⑀, , , or isoforms (36,37).…”

Section: Pdb Binding-[supporting

confidence: 68%

“…1). CFs, including FMLP, likewise have reduced ability to translocate various PKC isoforms in PMN deprived of Ca 2ϩ (43). In marked contrast, AA caused prominent PBD binding and PKC␤ II , ␣, and ␦ translocation (Figs.…”

Section: Pdb Binding-[mentioning

confidence: 94%

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Protein Kinases C Translocation Responses to Low Concentrations of Arachidonic Acid

O’Flaherty¹,

Chadwell²,

Kearns

et al. 2001

Journal of Biological Chemistry

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Arachidonic acid (AA) directly activates protein kinases C (PKC) and may thereby serve as a regulatory signal during cell stimulation. The effect, however, requires a >20 M concentration of the fatty acid. We find that human polymorphonuclear neutrophils ( or PKC␦ fused to the reporter enhanced green fluorescent protein (EGFP) were studied. AA caused EGFP-PKC␤ translocation from cytosol to plasma membrane at >0.5 M, and EGFP-PKC␦ translocation from cytosol to nuclear and, to a lesser extent, plasma membrane at as little as 30 nM. We conclude that AA induces PKC translocations to specific membrane targets at concentrations 2-4 orders of magnitude below those activating the enzymes. These responses, at least as they occur in PMN, do not require changes in cell Ca 2؉ or oxygenation of the fatty acid. AA seems more suited for signaling the movement than activation of PKC.

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“…Our observation that GF109203X, a PKC inhibitor, strongly inhibited PMA-induced phosphorylation and barely modified fMLP-induced phosphorylation, points to both PKC-dependent (isoforms sensitive to GF109203X) and PKC-independent (or GF109203X-insensitive) pathways in the phosphorylation of p67 phox . Indeed, human neutrophils express in addition to the ␣ and ␤ PKC isoforms the PKC (27). The PKC inhibitor GF109203X could be more effective against the ␣ and ␤ isoforms than the one.…”

Section: Discussionmentioning

confidence: 99%

Phosphorylation of the Respiratory Burst Oxidase Subunit p67 during Human Neutrophil Activation

Benna¹,

Dang²,

Gaudry³

et al. 1997

Journal of Biological Chemistry

152

132

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The respiratory burst oxidase of phagocytes and B lymphocytes catalyzes the reduction of oxygen to superoxide anion (O 2 . ) at the expense of NADPH. This multicomponent enzyme is dormant in resting cells but is activated on exposure to an appropriate stimulus. The phosphorylation-dependent mechanisms regulating the activation of the respiratory burst oxidase are unclear, particularly the phosphorylation status of the cytosolic component p67 phox. In this study, we found that activation of human neutrophils with formyl-methionylleucyl-phenylalanine (fMLP), a chemotactic peptide, or phorbol myristate acetate (PMA), a stimulator of protein kinase C (PKC), resulted in the phosphorylation of p67 phox . Using an anti-p67 phox antibody or an antip47 phox antibody, we showed that phosphorylated p67 phox and p47 phox form a complex. Phosphoamino acid analysis of the phosphorylated p67 phox revealed only 32 P-labeled serine residues. Two-dimensional tryptic peptide mapping analysis showed that p67 phox is phosphorylated at the same peptide whether fMLP or PMA is used as a stimulus. In addition, PKC induced the phosphorylation of recombinant GST-p67 phox in vitro, at the same peptide as that phosphorylated in intact cells. PMA-induced phosphorylation of p67 phox was strongly inhibited by the PKC inhibitor GF109203X. In contrast, fMLP-induced phosphorylation was minimally affected by this PKC inhibitor. Taken together, these results show that p67 phox is phosphorylated in human neutrophils by different pathways, one of which involves protein kinase C.

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Redistribution of Protein Kinase C Isoforms in Human Neutrophils Stimulated by Formyl Peptides and Phorbol-Myristate Acetate

Cited by 52 publications

References 0 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

Protein Kinases C Translocation Responses to Low Concentrations of Arachidonic Acid

Phosphorylation of the Respiratory Burst Oxidase Subunit p67 during Human Neutrophil Activation

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