Protein tyrosine phosphorylation in rabbit peritoneal neutrophils

Huang, Chi‐Kuang; Bonak, Valerie A.; Laramee, Gary R.; Casnellie, John E.

doi:10.1042/bj2690431

Cited by 64 publications

(22 citation statements)

References 40 publications

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“…The tyrosine phosphorylation response to MSU crystals was more rapid and more pronounced than that induced by CPPD crystals. Thus, the relative abilities of the microcrystals to stimulate tyrosine phosphorylation in human neutrophils parallel their phlogistic (22,25,26,29), platelet-activating factor (28), leukotriene B4 (27), and cytokines (24) has previously been shown to be associated with increased tyrosine phosphorylation. These results suggest that tyrosine phosphorylation may play important roles in the activation of neutrophils, a suggestion strengthened by the ability of tyrosine kinase inhibitors to inhibit the chemotactic factor-stimulated locomotory and adherence responses of the cells (29), generation of superoxide anions (25), and activation of phospholipase D (34a).…”

Section: Discussionmentioning

confidence: 99%

“…Stimulation of intact human neutrophils with GM-CSF (24), chemotactic peptides such as FMLP (22,(25)(26)(27), leukotriene B4 (27), and platelet-activating factor (28) or with phorbol esters (26,27) induces the rapid phosphorylation on tyrosine residues of several protein substrates. In addition, the results of recent studies have implicated the activation of tyrosine kinases in several neutrophil responses such as the oxidative burst (25), and adherence and chemotaxis (29).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Crystal-induced neutrophil activation. III. Inflammatory microcrystals induce a distinct pattern of tyrosine phosphorylation in human neutrophils.

Gaudry

Roberge²,

Médicis³

et al. 1993

J. Clin. Invest.

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The activation of human neutrophils by monosodium urate and calcium pyrophosphate dihydrate crystals is believed to play a critical role in the pathogenesis ofarthritides such as acute gout and pseudogout, respectively. In this study, we investigated the potential involvement of tyrosine phosphorylation in microcrystal-mediated activation of human neutrophils. Immunoblot analysis with antiphosphotyrosine antibodies demonstrated that triclinic monosodium urate and calcium pyrophosphate dihydrate crystals stimulated a time-and concentration-dependent tyrosine phosphorylation of at least five proteins (pp130, 118, 80, 70, and 60). While phosphoprotein (pp) 118 and pp7O were the major phosphorylated substrates, pp7O was the dominant one in reactivity with antiphosphotyrosine antibodies. When the temporal patterns, as well as the levels of tyrosine phosphorylation for both types of crystals were compared, monosodium urate crystals were found to be more potent activators than calcium pyrophosphate dihydrate crystals. The tyrosine phosphorylation patterns induced by microcrystals differed from those stimulated by other soluble (FMLP, C_%, or leukotriene B4) or particulate (unopsonized latex beads or zymosan) agonists which stimulated preferentially the tyrosine phosphorylation of ppl 18. The ratio of the intensities of ppl 18 and pp7O were specific of the stimulation with microcrystals when compared to those observed with the other soluble or particulate agonists. Colchicine, a drug used specifically in the treatment of gout and pseudogout, inhibited microcrystal-induced tyrosine phosphorylation, whileft-and y-lumicolchicine were without effect. On the other hand, colchicine failed to inhibit FMLP-induced tyrosine phosphorylation. Furthermore, while colchicine inhibited the activation of the NADPH oxidase by microcrystals, it, on the other hand, enhanced the production of superoxide anions by FMLP. Taken together, these results (a) demonstrate that tyrosine phosphorylation is involved in the mechanism of activation of human neutrophils induced by microcrystals; and (b) suggest, on the basis of the characteristics of the observed patterns of tyrosine phosphorylation, that this response may be specific to the microcrystals and relevant to their phlogistic properties. (J. Clin. Invest.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Crystal-induced neutrophil activation. III. Inflammatory microcrystals induce a distinct pattern of tyrosine phosphorylation in human neutrophils.

Gaudry

Roberge²,

Médicis³

et al. 1993

J. Clin. Invest.

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“…It occurs in neutrophils challenged with a variety of agonists, including Wet-Leu-Phe, leukotriene B4, phorbol ester and the calcium ionophore A23187 (Berkow and Dodson, 1990;Huang et al, 1990). Tyrosine phosphorylation has also been observed in neutrophils electropermeabilized in the presence of GTP [S]; it was found to be dependent on the presence of Mg2' and ATP and associated with a marked increase in 0; production, partially resistant to staurosporin, leading the authors to conclude that changes in the amounts of tyrosinephosphorylated proteins may signal activation of the respiratory burst (Nasmith et al, 1989;Grinstein and Furaya, 1991).…”

Section: Role Of Activated Protein Kinase C In the Respiratory Burstmentioning

confidence: 99%

The superoxide‐generating oxidase of phagocytic cells

Morel¹,

Doussière²,

Vignais³

1991

European Journal of Biochemistry

536

260

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Professional phagocytes (neutrophils, eosinophils, monocytes and macrophages) possess an enzymatic complex, the NADPH oxidase, which is able to catalyze the one-electron reduction of molecular oxygen to superoxide, 0;. The NADPH oxidase is dormant in non-activated phagocytes. It is suddenly activated upon exposure of phagocytes to the appropriate stimuli and thereby contributes to the microbicidal activity of these cells. Oxidase activation in phagocytes involves the assembly, in the plasma membrane, of membrane-bound and cytosolic components of the oxidase complex, which were disassembled in the resting state. One of the membrane-bound components in resting phagocytes has been identified as a low-potential b-type cytochrome, a heterodimer composed of two subunits of 22-kDa and 91-kDa. The link between NADPH and cytochrome b is probably a flavoprotein whose subcellular localization in resting phagocytes remains to be determined. Genetic defects in the cytochrome b subunits and in the cytosolic factors have been shown to be the molecular basis of chronic granulomatous disease, a group of inherited disorders in the host defense, characterized by severe, recurrent bacterial and fungal infections in which phagocytic cells fail to generate 0 , upon stimulation. The present review is focused on recent data concerning the signaling pathway which leads to oxidase activation, including specific receptors, the production of second messengers, the organization of the oxidase complex and the molecular defects responsible for granulomatous disease.

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“…The increase in tyrosyl phosphorylation might reflect the increase in tyrosine kinase activity and/or the decrease in the activity of phosphotyrosine phosphatase. PMAand FMLPalso increase tyrosyl phosphorylation in a time and concentration-dependent manner (40,41). An increase in tyrosyl phosphorylation of neutrophil proteins was also observed after treatment of cells with guanine .…”

Section: Discussionmentioning

confidence: 97%

Inhibition of Neutrophil Priming and Tyrosyl Phosphorylation by Cepharanthine, a Nonsteroidal Antiinflammatory Drug.

Kobuchi

Matsuno

et al. 1992

Cell Struct. Funct.

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ABSTRACT. Receptor-mediated superoxide (O2>generation and tyrosyl phosphorylation of neutrophil proteins, such as 58, 65, 84, 108 and 115 kDa, were enhanced by priming cells with granulocyte colony stimulating factor (G-CSF) [Akimura, K. et al. Arch. Biochem. Biophys. 298: 703-709, 1992]. To elucidate the possible involvement of tyrosyl phosphorylation of neutrophil proteins in the enhancing mechanismof O2 generation, the effect of cepharanthine, a biscoclaurine alkaloid that inhibits phorbol 12-myristate 13-acetate (PMA)-and receptor-mediated O2 generation, on the priming of human peripheral neutrophils (HPPMN)was studied. Both enhancement of formyl-methyonyl-leucyl-phenylalanine (FMLP)-mediated O2 generation and tyrosyl phosphorylation of some neutrophil proteins, i.e., 115, 108 and 84 kDa proteins, by HHPMNafter treatment with G-CSFwere strongly inhibited by cepharanthine in a concentration-and treatment-time-dependent manner. In contrast, inhibition of PMA-mediated O2 generation by cepharanthine was weak and independent of treatment time. These results suggest that cepharanthine might inhibit the priming step of neutrophil activation concomitantly with its inhibition of the tyrosyl phosphorylation of some neutrophil proteins that might underlie the mechanism for priming of neutrophils with G-CSF.

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Protein tyrosine phosphorylation in rabbit peritoneal neutrophils

Cited by 64 publications

References 40 publications

Crystal-induced neutrophil activation. III. Inflammatory microcrystals induce a distinct pattern of tyrosine phosphorylation in human neutrophils.

Crystal-induced neutrophil activation. III. Inflammatory microcrystals induce a distinct pattern of tyrosine phosphorylation in human neutrophils.

The superoxide‐generating oxidase of phagocytic cells

Inhibition of Neutrophil Priming and Tyrosyl Phosphorylation by Cepharanthine, a Nonsteroidal Antiinflammatory Drug.

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